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Conserved domains on  [gi|2068696253|ref|XP_042239871|]
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irregular chiasm C-roughest protein-like isoform X2 [Homarus americanus]

Protein Classification

IG_like and Ig domain-containing protein( domain architecture ID 12209121)

protein containing domains IG_like, and Ig

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 ...
 141-228 3.61e-15

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 cd05759:

Pssm-ID: 472250  Cd Length: 98  Bit Score: 71.71  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 141 TAGVPLTLTCSSSGGRPAPEIQWL-DGsgaEIHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARSLTCLTHNPALHTP 219
Cdd:cd05759    13 QAGVPYNLTCRARGAKPAAEIIWFrDG---EQLEGAVYSKELLKDGKRETTVSTLLITPSDLDTGRTFTCRARNEAIPNG 89


                  ....*....
gi 2068696253 220 LAAKVRLNV 228
Cdd:cd05759    90 KETSITLDV 98
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 400-494 1.45e-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.


The actual alignment was detected with superfamily member cd05758:

Pssm-ID: 472250  Cd Length: 98  Bit Score: 69.87  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 400 GPPLIRAQAVVAVPEGQPAVLRCGVVAVPHPVSVTWT-REGALVVSEDGRYVNEEQRAD-GVVSTLTINKTSHRDFA-SY 476
Cdd:cd05758     1 GPPIITAEATQPAILGEKARLECLVFSSPPPDRIVWSwDEGFLESGSSGRFSVETFPTEpGVISVLHISGTQRSDFQtSF 80

                          90
                  ....*....|....*...
gi 2068696253 477 NCSVINEYGVDTHQILLQ 494
Cdd:cd05758    81 NCSAWNRFGEGTAIVSLG 98
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 33-125 3.92e-10

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


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.74  E-value: 3.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253   33 PSHQTAVLGSTAVLPCRVINQRGL-VQWTRDGFGLGTQRGlegfeRYSMIGadEEGDFSLRISPVTLEDDAEYQCQVSSa 111
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPeVTWYKQGGKLLAESG-----RFSVSR--SGSTSTLTISNVTPEDSGTYTCAATN- 72

                           90
                   ....*....|....
gi 2068696253  112 tELPLRSQVARLTV 125
Cdd:smart00410  73 -SSGSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 318-383 5.72e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.03  E-value: 5.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNPKVVGRGPEL----------LVSATPTSAGLYVCSAR 383
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRslsgsnstltISNVTRSDAGTYTCVAS 77
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 231-301 3.96e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 231 PPEVQLQFSPEELSEGVEASVTCRVEANPgEVTYRWFRGGSEVAGAQ---------GSTLPLGVLSRADNASpVACEVTN 301
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSP-PPTITWYKNGEPISSGStrsrslsgsNSTLTISNVTRSDAGT-YTCVASN 78
 
Name Accession Description Interval E-value
IgI_2_KIRREL3-like cd05759
Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 141-228 3.61e-15

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, 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 of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 409416  Cd Length: 98  Bit Score: 71.71  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 141 TAGVPLTLTCSSSGGRPAPEIQWL-DGsgaEIHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARSLTCLTHNPALHTP 219
Cdd:cd05759    13 QAGVPYNLTCRARGAKPAAEIIWFrDG---EQLEGAVYSKELLKDGKRETTVSTLLITPSDLDTGRTFTCRARNEAIPNG 89


                  ....*....
gi 2068696253 220 LAAKVRLNV 228
Cdd:cd05759    90 KETSITLDV 98
IgI_5_KIRREL3-like cd05758
Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 400-494 1.45e-14

Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (also known as Neph1), Kirrel2 (also known as Neph3), and Drosophila RST (also known as irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 319310  Cd Length: 98  Bit Score: 69.87  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 400 GPPLIRAQAVVAVPEGQPAVLRCGVVAVPHPVSVTWT-REGALVVSEDGRYVNEEQRAD-GVVSTLTINKTSHRDFA-SY 476
Cdd:cd05758     1 GPPIITAEATQPAILGEKARLECLVFSSPPPDRIVWSwDEGFLESGSSGRFSVETFPTEpGVISVLHISGTQRSDFQtSF 80

                          90
                  ....*....|....*...
gi 2068696253 477 NCSVINEYGVDTHQILLQ 494
Cdd:cd05758    81 NCSAWNRFGEGTAIVSLG 98
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 126-219 9.29e-13

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 64.36  E-value: 9.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 126 FVPPKPPTVTHPafataGVPLTLTCSSSGGRPAPEIQWLDGSGAEIHSGVQLSEDlmEDEKRVNAHATLTFTPTRHHHAR 205
Cdd:pfam08205   2 TIEPPASLLEGE-----GPEVVATCSSAGGKPAPRITWYLDGKPLEAAETSSEQD--PESGLVTVTSELKLVPSRSDHGQ 74

                          90
                  ....*....|....
gi 2068696253 206 SLTCLTHNPALHTP 219
Cdd:pfam08205  75 SLTCQVSYGALRGS 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 409-494 6.58e-12

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.75  E-value: 6.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  409 VVAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSEDGRYvneEQRADGVVSTLTINKTSHRDFASYNCSVINEYGVDT 488
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLAESGRF---SVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78


                   ....*.
gi 2068696253  489 HQILLQ 494
Cdd:smart00410  79 SGTTLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 33-125 3.92e-10

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.74  E-value: 3.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253   33 PSHQTAVLGSTAVLPCRVINQRGL-VQWTRDGFGLGTQRGlegfeRYSMIGadEEGDFSLRISPVTLEDDAEYQCQVSSa 111
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPeVTWYKQGGKLLAESG-----RFSVSR--SGSTSTLTISNVTPEDSGTYTCAATN- 72

                           90
                   ....*....|....
gi 2068696253  112 tELPLRSQVARLTV 125
Cdd:smart00410  73 -SSGSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 401-482 4.40e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.42  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 401 PPLIRAQ-AVVAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSEDGRYVNEeqraDGVVSTLTINKTSHRDFASYNCS 479
Cdd:pfam13927   1 KPVITVSpSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSRSL----SGSNSTLTISNVTRSDAGTYTCV 75


                  ...
gi 2068696253 480 VIN 482
Cdd:pfam13927  76 ASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 318-383 5.72e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.03  E-value: 5.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNPKVVGRGPEL----------LVSATPTSAGLYVCSAR 383
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRslsgsnstltISNVTRSDAGTYTCVAS 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 324-398 1.21e-08

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: 52.51  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  324 PSSQSAEPDQRVTLKCRVDANPPPDITWSRpNNPKVVGRGPELLVS------------ATPTSAGLYVCSARSPGFSpLE 391
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYK-QGGKLLAESGRFSVSrsgststltisnVTPEDSGTYTCAATNSSGS-AS 78


                   ....*..
gi 2068696253  392 GRVHLRI 398
Cdd:smart00410  79 SGTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 31-125 2.48e-08

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 52.46  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  31 TMPSHQTAVLGSTAVLPC----RVINQRGLVQWTRDGFGLGTQ---------RGLEGF-ERYSMIGADEEGDFSLRISPV 96
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCtyssSMSEASTSVYWYRQPPGKGPTfliayysngSEEGVKkGRFSGRGDPSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
gi 2068696253  97 TLEDDAEYQCQVSSATELPLRSQVaRLTV 125
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGT-RLTV 108
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 324-382 1.95e-07

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: 48.93  E-value: 1.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068696253 324 PSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNPKVVGRGPEL------LVSATPTSAGLYVCSA 382
Cdd:cd05725     4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILddhslkIRKVTAGDMGSYTCVA 68
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 231-301 3.96e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 231 PPEVQLQFSPEELSEGVEASVTCRVEANPgEVTYRWFRGGSEVAGAQ---------GSTLPLGVLSRADNASpVACEVTN 301
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSP-PPTITWYKNGEPISSGStrsrslsgsNSTLTISNVTRSDAGT-YTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 44-109 5.29e-06

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.63  E-value: 5.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253  44 AVLPCRVINQRGL-VQWTRDGFGLGTQRGLEGFErysmigadEEGDFSLRISPVTLEDDAEYQCQVS 109
Cdd:cd00096     1 VTLTCSASGNPPPtITWYKNGKPLPPSSRDSRRS--------ELGNGTLTISNVTLEDSGTYTCVAS 59
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 247-314 3.43e-05

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 42.94  E-value: 3.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068696253 247 VEASVTCRVEANPGEVTYRWfrggSEVAG-------AQGSTLPLGVLSRADNASPVaCEVTNAVGTTRKTQSLNV 314
Cdd:cd20930    17 NEATLTCDVRSNPEPTGYDW----STTSGpfptsavAQGPQLLIHSVDRLVNTTFI-CTVTNAVGTGRAEQTIFV 86
IGc1 smart00407
Immunoglobulin C-Type;
145-219 1.33e-03

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 38.06  E-value: 1.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253  145 PLTLTCSSSGGRPAP-EIQWLDGsGAEIHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARSLTC-LTHnPALHTP 219
Cdd:smart00407   1 KATLVCLVSGFYPPDiTVTWLRN-GQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCqVTH-EGLKEP 75
 
Name Accession Description Interval E-value
IgI_2_KIRREL3-like cd05759
Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 141-228 3.61e-15

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, 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 of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 409416  Cd Length: 98  Bit Score: 71.71  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 141 TAGVPLTLTCSSSGGRPAPEIQWL-DGsgaEIHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARSLTCLTHNPALHTP 219
Cdd:cd05759    13 QAGVPYNLTCRARGAKPAAEIIWFrDG---EQLEGAVYSKELLKDGKRETTVSTLLITPSDLDTGRTFTCRARNEAIPNG 89


                  ....*....
gi 2068696253 220 LAAKVRLNV 228
Cdd:cd05759    90 KETSITLDV 98
IgI_5_KIRREL3-like cd05758
Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 400-494 1.45e-14

Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (also known as Neph1), Kirrel2 (also known as Neph3), and Drosophila RST (also known as irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 319310  Cd Length: 98  Bit Score: 69.87  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 400 GPPLIRAQAVVAVPEGQPAVLRCGVVAVPHPVSVTWT-REGALVVSEDGRYVNEEQRAD-GVVSTLTINKTSHRDFA-SY 476
Cdd:cd05758     1 GPPIITAEATQPAILGEKARLECLVFSSPPPDRIVWSwDEGFLESGSSGRFSVETFPTEpGVISVLHISGTQRSDFQtSF 80

                          90
                  ....*....|....*...
gi 2068696253 477 NCSVINEYGVDTHQILLQ 494
Cdd:cd05758    81 NCSAWNRFGEGTAIVSLG 98
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 126-219 9.29e-13

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 64.36  E-value: 9.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 126 FVPPKPPTVTHPafataGVPLTLTCSSSGGRPAPEIQWLDGSGAEIHSGVQLSEDlmEDEKRVNAHATLTFTPTRHHHAR 205
Cdd:pfam08205   2 TIEPPASLLEGE-----GPEVVATCSSAGGKPAPRITWYLDGKPLEAAETSSEQD--PESGLVTVTSELKLVPSRSDHGQ 74

                          90
                  ....*....|....
gi 2068696253 206 SLTCLTHNPALHTP 219
Cdd:pfam08205  75 SLTCQVSYGALRGS 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 409-494 6.58e-12

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 61.75  E-value: 6.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  409 VVAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSEDGRYvneEQRADGVVSTLTINKTSHRDFASYNCSVINEYGVDT 488
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLAESGRF---SVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78


                   ....*.
gi 2068696253  489 HQILLQ 494
Cdd:smart00410  79 SGTTLT 84
IgI_5_KIRREL3 cd05898
Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 protein; ...
 400-494 2.24e-11

Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 protein (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1). These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development. Neph1 and 2 may mediate axonal guidance and synapse formation in certain areas of the CNS. In the kidney they participate in the formation of the slit diaphragm.


Pssm-ID: 409479  Cd Length: 98  Bit Score: 60.74  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 400 GPPLIRAQAVVAVPEGQPAVLRCGVVAVPHPVSVTWT-REGALVVSEDGRY-VNEEQRADGVVSTLTINKTSHRDFAS-Y 476
Cdd:cd05898     1 GPPIISSEQVQYAVRGERGKVKCFIGSTPPPDRIAWAwKENVLESGTLERYtVERTSTGSGVLSTLTINNIMEADFQThY 80

                          90
                  ....*....|....*...
gi 2068696253 477 NCSVINEYGVDTHQILLQ 494
Cdd:cd05898    81 NCTAWNSFGSGTAIIQLE 98
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 33-125 3.92e-10

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 56.74  E-value: 3.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253   33 PSHQTAVLGSTAVLPCRVINQRGL-VQWTRDGFGLGTQRGlegfeRYSMIGadEEGDFSLRISPVTLEDDAEYQCQVSSa 111
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPeVTWYKQGGKLLAESG-----RFSVSR--SGSTSTLTISNVTPEDSGTYTCAATN- 72

                           90
                   ....*....|....
gi 2068696253  112 tELPLRSQVARLTV 125
Cdd:smart00410  73 -SSGSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 401-482 4.40e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.42  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 401 PPLIRAQ-AVVAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSEDGRYVNEeqraDGVVSTLTINKTSHRDFASYNCS 479
Cdd:pfam13927   1 KPVITVSpSSVTVREGETVTLTCEATGSPPP-TITWYKNGEPISSGSTRSRSL----SGSNSTLTISNVTRSDAGTYTCV 75


                  ...
gi 2068696253 480 VIN 482
Cdd:pfam13927  76 ASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 318-383 5.72e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 56.03  E-value: 5.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNPKVVGRGPEL----------LVSATPTSAGLYVCSAR 383
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRslsgsnstltISNVTRSDAGTYTCVAS 77
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 412-488 4.83e-09

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: 53.96  E-value: 4.83e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253 412 VPEGQPAVLRCGVVAVPHPVsVTWTREGALV--VSEDGRYvnEEQRADGVvSTLTINKTSHRDFASYNCSVINEYGVDT 488
Cdd:cd20951    12 VWEKSDAKLRVEVQGKPDPE-VKWYKNGVPIdpSSIPGKY--KIESEYGV-HVLHIRRVTVEDSAVYSAVAKNIHGEAS 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 324-398 1.21e-08

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: 52.51  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  324 PSSQSAEPDQRVTLKCRVDANPPPDITWSRpNNPKVVGRGPELLVS------------ATPTSAGLYVCSARSPGFSpLE 391
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYK-QGGKLLAESGRFSVSrsgststltisnVTPEDSGTYTCAATNSSGS-AS 78


                   ....*..
gi 2068696253  392 GRVHLRI 398
Cdd:smart00410  79 SGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
410-494 1.95e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 410 VAVPEGQPAVLRCGVVAVPHPvSVTWTREGAlVVSEDGRYVneeQRADGVVSTLTINKTSHRDFASYNCSVINEYGVDTH 489
Cdd:pfam07679  10 VEVQEGESARFTCTVTGTPDP-EVSWFKDGQ-PLRSSDRFK---VTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEA 84


                  ....*
gi 2068696253 490 QILLQ 494
Cdd:pfam07679  85 SAELT 89
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 31-125 2.48e-08

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 52.46  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  31 TMPSHQTAVLGSTAVLPC----RVINQRGLVQWTRDGFGLGTQ---------RGLEGF-ERYSMIGADEEGDFSLRISPV 96
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCtyssSMSEASTSVYWYRQPPGKGPTfliayysngSEEGVKkGRFSGRGDPSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
gi 2068696253  97 TLEDDAEYQCQVSSATELPLRSQVaRLTV 125
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGT-RLTV 108
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 324-382 1.95e-07

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: 48.93  E-value: 1.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068696253 324 PSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNPKVVGRGPEL------LVSATPTSAGLYVCSA 382
Cdd:cd05725     4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILddhslkIRKVTAGDMGSYTCVA 68
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 406-488 3.42e-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: 48.35  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 406 AQAVVAVPEGQPAVLRCGVVAVPHPVSVTWTREGAlvVSEDGRYVNEEQRADGvVSTLTINKTSHRDFASYNCSVINEYG 485
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGG--TLIESLKVKHDNGRTT-QSSLLISNVTKEDAGTYTCVVNNPGG 78


                  ...
gi 2068696253 486 VDT 488
Cdd:pfam00047  79 SAT 81
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 318-386 4.22e-07

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: 48.70  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWS-----------RPN----NPKVVGRGPELLVSATPTSAGLYVCSA 382
Cdd:cd05765     1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEkqvpgkenlimRPNhvrgNVVVTNIGQLVIYNAQPQDAGLYTCTA 80


                  ....
gi 2068696253 383 RSPG 386
Cdd:cd05765    81 RNSG 84
I-set pfam07679
Immunoglobulin I-set domain;
29-109 4.93e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  29 FATMPSHQTAVLGSTAVLPCRVI-NQRGLVQWTRDGFGLGTQRglegfeRYSMigADEEGDFSLRISPVTLEDDAEYQCQ 107
Cdd:pfam07679   3 FTQKPKDVEVQEGESARFTCTVTgTPDPEVSWFKDGQPLRSSD------RFKV--TYEGGTYTLTISNVQPDDSGKYTCV 74


                  ..
gi 2068696253 108 VS 109
Cdd:pfam07679  75 AT 76
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 401-488 6.52e-07

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: 47.88  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 401 PPLIRAQAVVAVPEGQPAVLRCGVVAVPHPvSVTWTREGALV--VSEDGRYVNEeqraDGVVStLTINKTSHRDFASYNC 478
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTP-DLFWQLNGKPVrpDSAHKMLVRE----NGRHS-LIIEPVTKRDAGIYTC 74

                          90
                  ....*....|
gi 2068696253 479 SVINEYGVDT 488
Cdd:cd05744    75 IARNRAGENS 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 33-109 7.87e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.18  E-value: 7.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068696253  33 PSHQTAVLGSTAVLPCRVI-NQRGLVQWTRDGfglgtQRGLEGFERYSMIGadeEGDFSLRISPVTLEDDAEYQCQVS 109
Cdd:pfam13927   8 PSSVTVREGETVTLTCEATgSPPPTITWYKNG-----EPISSGSTRSRSLS---GSNSTLTISNVTRSDAGTYTCVAS 77
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 318-383 8.32e-07

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: 47.49  E-value: 8.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNP-----------KVVGRGPELLVSATPTSAGLYVCSAR 383
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPvrpdsahkmlvRENGRHSLIIEPVTKRDAGIYTCIAR 77
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 410-494 1.02e-06

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 47.50  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 410 VAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSEDGRYvneEQRADGvvSTLTINKTSHRDFASYNCSVINE-YGVDT 488
Cdd:cd20970    12 VTAREGENATFMCRAEGSPEP-EISWTRNGNLIIEFNTRY---IVRENG--TTLTIRNIRRSDMGIYLCIASNGvPGSVE 85


                  ....*.
gi 2068696253 489 HQILLQ 494
Cdd:cd20970    86 KRITLQ 91
IgC2_CD33_d2_like cd20987
Second immunoglobulin domain of Cluster of Differentiation (CD) 33 and related Siglecs; member ...
 132-209 1.72e-06

Second immunoglobulin domain of Cluster of Differentiation (CD) 33 and related Siglecs; member of the C2-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 33 (also known as sialic-acid binding immunoglobulin type-lectin 3 (Siglec-3)) and related Siglecs. CD33, a Siglec family member, is a well-known immunotherapeutic target in acute myeloid leukemia (AML). It is an inhibitory sialoadhesin expressed in human leukocytes of the myeloid lineage and some lymphoid subsets, including natural killer (NK) cells. Siglecs are primarily expressed on immune cells and recognize sialic acid-containing glycan ligands. Siglecs are organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4, myelin-associated glycoprotein), the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11. CD33 (Siglec-3) is the smallest Siglec member. It preferentially binds to alpha2-6- and alpha2-3-sialylated glycans and strongly binds to sialylated ligands on leukemic cell lines. 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. This group includes CD33-related Siglecs which belong to the C2-set of IgSF domains. Unlike the C1-set, the C2-set structures do not have a D strand.


Pssm-ID: 409579  Cd Length: 94  Bit Score: 46.79  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 132 PTVTHPAFATAGVPLTLTCSSSGGRPA--PEIQWLdgsGAEIHSGVQLSEDLmEDEKRVNAHATLTFTPTRHHHARSLTC 209
Cdd:cd20987     1 PNIHVPEELEAGQEVTLTCSVPDNCPAlsPEFSWL---GAALTPLPPVLGRL-EEEGTTTHSSVLTFTPRPEDHGTNLTC 76
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 401-494 1.96e-06

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: 46.46  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 401 PPLIRA-QAVVAVPE--GQPAVLRCGVVAVPHPVsVTWTREGALVVSEDGRYVNEEqraDGvvSTLTINKTSHRDFASYN 477
Cdd:cd05730     1 PPTIRArQSEVNATAnlGQSVTLACDADGFPEPT-MTWTKDGEPIESGEEKYSFNE---DG--SEMTILDVDKLDEAEYT 74

                          90
                  ....*....|....*..
gi 2068696253 478 CSVINEYGVDTHQILLQ 494
Cdd:cd05730    75 CIAENKAGEQEAEIHLK 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 231-301 3.96e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 231 PPEVQLQFSPEELSEGVEASVTCRVEANPgEVTYRWFRGGSEVAGAQ---------GSTLPLGVLSRADNASpVACEVTN 301
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSP-PPTITWYKNGEPISSGStrsrslsgsNSTLTISNVTRSDAGT-YTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 44-109 5.29e-06

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.63  E-value: 5.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253  44 AVLPCRVINQRGL-VQWTRDGFGLGTQRGLEGFErysmigadEEGDFSLRISPVTLEDDAEYQCQVS 109
Cdd:cd00096     1 VTLTCSASGNPPPtITWYKNGKPLPPSSRDSRRS--------ELGNGTLTISNVTLEDSGTYTCVAS 59
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 131-213 5.91e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.86  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 131 PPTVT---HPAFATAGVPLTLTCSSSGGrPAPEIQWLdgsgaeiHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARSL 207
Cdd:pfam13927   1 KPVITvspSSVTVREGETVTLTCEATGS-PPPTITWY-------KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTY 72


                  ....*.
gi 2068696253 208 TCLTHN 213
Cdd:pfam13927  73 TCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 146-215 6.63e-06

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.24  E-value: 6.63e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 146 LTLTCSSSGgRPAPEIQWLdgsgaeiHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARSLTCLTHNPA 215
Cdd:cd00096     1 VTLTCSASG-NPPPTITWY-------KNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSA 62
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 402-493 6.98e-06

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: 44.77  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 402 PLI-RAQAVVAVPEGQPAVLRCGVVAVPHPVsVTWtregalvVSEDGRYVNEEQRA----DGvvsTLTINKTSHRDFASY 476
Cdd:cd05764     1 PLItRHTHELRVLEGQRATLRCKARGDPEPA-IHW-------ISPEGKLISNSSRTlvydNG---TLDILITTVKDTGAF 69

                          90
                  ....*....|....*..
gi 2068696253 477 NCSVINEYGVDTHQILL 493
Cdd:cd05764    70 TCIASNPAGEATARVEL 86
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 324-383 8.30e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 44.31  E-value: 8.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068696253 324 PSSQSAEPDQRVTLKCRVDANPPPDITWSRPNnpKVVGRGPELLV-SATPTSAGLYVCSAR 383
Cdd:pfam13895   6 PSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDG--SAISSSPNFFTlSVSAEDSGTYTCVAR 64
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 412-488 9.74e-06

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: 44.49  E-value: 9.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253 412 VPEGQPAVLRCGVVAVPHPvSVTWTREGALVVseDGRYVNEEQRADGVVStLTINKTSHRDFASYNCSVINEYGVDT 488
Cdd:cd20973     9 VVEGSAARFDCKVEGYPDP-EVKWMKDDNPIV--ESRRFQIDQDEDGLCS-LIISDVCGDDSGKYTCKAVNSLGEAT 81
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 318-384 1.01e-05

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: 1.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253 318 PLFVTAPSSQSA-EPDQRVTLKCRVDANPPPDITWSRPNNPKVVGRGPE---------LLVSATPTSAGLYVCSARS 384
Cdd:cd05760     1 PVVLKHPASAAEiQPSSRVTLRCHIDGHPRPTYQWFRDGTPLSDGQGNYsvsskertlTLRSAGPDDSGLYYCCAHN 77
I-set pfam07679
Immunoglobulin I-set domain;
318-382 1.09e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.17  E-value: 1.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNP---------KVVGRGPELLVS-ATPTSAGLYVCSA 382
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPlrssdrfkvTYEGGTYTLTISnVQPDDSGKYTCVA 75
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 409-494 1.18e-05

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 44.31  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 409 VVAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSEDGRYVNEEqradgvvSTLTINKTSHRDFASYNCSVINEYGVDT 488
Cdd:cd20978    10 NVVVKGGQDVTLPCQVTGVPQP-KITWLHNGKPLQGPMERATVED-------GTLTIINVQPEDTGYYGCVATNEIGDIY 81


                  ....*.
gi 2068696253 489 HQILLQ 494
Cdd:cd20978    82 TETLLH 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 418-492 1.79e-05

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: 43.09  E-value: 1.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068696253 418 AVLRCGVVAVPHPvSVTWTREGALVVSEDgryvNEEQRADGVVSTLTINKTSHRDFASYNCSVINEYGVDTHQIL 492
Cdd:cd00096     1 VTLTCSASGNPPP-TITWYKNGKPLPPSS----RDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 335-385 1.89e-05

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: 43.09  E-value: 1.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068696253 335 VTLKCRVDANPPPDITWSRPNNPKVVGRGPE----------LLVSATPTSAGLYVCSARSP 385
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSrrselgngtlTISNVTLEDSGTYTCVASNS 61
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 409-486 2.02e-05

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: 43.47  E-value: 2.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068696253 409 VVAVPEGQPAVLRCGVVAVPHPVsVTWTREGAlVVSEDGRYvneEQRADGVVSTLTINKTSHRDFASYNCSVINEYGV 486
Cdd:cd20949     8 VTTVKEGQSATILCEVKGEPQPN-VTWHFNGQ-PISASVAD---MSKYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 127-228 3.07e-05

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.


Pssm-ID: 409418  Cd Length: 102  Bit Score: 43.57  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 127 VPPKPPTVThpAFATA---GVPLTLTCSSSGGRPAPEIQWLDGSgAEIHSGVQLSEDlmEDEKRVNAHATLTFTPTRHHH 203
Cdd:cd05761     2 GVPEKPVIT--GFTSPvveGDEITLTCTTSGSKPAADIRWFKND-KELKGVKEVQES--GAGKTFTVTSTLRFRVDRDDD 76

                          90       100
                  ....*....|....*....|....*.
gi 2068696253 204 ARSLTCLTHNPAL-HTPLAAKVRLNV 228
Cdd:cd05761    77 GVAVICRVDHESLtSTPKQTQQVLEV 102
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 247-314 3.43e-05

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 42.94  E-value: 3.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068696253 247 VEASVTCRVEANPGEVTYRWfrggSEVAG-------AQGSTLPLGVLSRADNASPVaCEVTNAVGTTRKTQSLNV 314
Cdd:cd20930    17 NEATLTCDVRSNPEPTGYDW----STTSGpfptsavAQGPQLLIHSVDRLVNTTFI-CTVTNAVGTGRAEQTIFV 86
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 321-386 6.64e-05

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: 42.05  E-value: 6.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068696253 321 VTAPSSQSAEPDQRVTLKCRVDANPPPDITWS--------RPNNPKVVGRGPELLVSA-TPTSAGLYVCSARSPG 386
Cdd:cd04978     3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRlngvpiepAPEDMRRTVDGRTLIFSNlQPNDTAVYQCNASNVH 77
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 33-109 8.75e-05

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: 41.80  E-value: 8.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  33 PSHQTAVL-GSTAVLPCRVINQRGLVQ--WTRDGfglgtQRGLEGfeRYSMIGADEEGDFSLRISPVTLEDDAEYQCQVS 109
Cdd:pfam00047   2 APPTVTVLeGDSATLTCSASTGSPGPDvtWSKEG-----GTLIES--LKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVN 74
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 240-311 9.64e-05

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first 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: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 41.85  E-value: 9.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253 240 PEELSEGvEASVTCRVEANPgEVTYRWFRGGSEVAGAQ-------GSTLPLGVLSRADNASPVACEVTNAVGTTRKTQS 311
Cdd:cd04967    14 PEDSDEK-KVALNCRARANP-VPSYRWLMNGTEIDLESdyryslvDGTLVISNPSKAKDAGHYQCLATNTVGSVLSREA 90
IgV_1_Necl_like cd05717
First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the ...
 34-125 1.09e-04

First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2), and similar proteins. At least five nectin-like molecules have been identified (Necl-1 to Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1, Necl-2, and Necl-3 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue, and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Necl-3 accumulates in central and peripheral nervous system tissue and has been shown to selectively interact with oligodendrocytes. This group also contains Class-I MHC-restricted T-cell-associated molecule (CRTAM), whose expression pattern is consistent with its expression in Class-I MHC-restricted T-cells.


Pssm-ID: 409382  Cd Length: 94  Bit Score: 41.73  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  34 SHQTAVLGSTAVLPCRV-INQRGLVQW-TRDGFGL--GTQRGLEGfERYSMIGADEEgDFSLRISPVTLEDDAEYQCQVS 109
Cdd:cd05717     4 QDVTVVEGETLTLKCQVsLRDDSSLQWlNPNGQTIyfNDKRALRD-SRYQLLNHSAS-ELSISVSNVTLSDEGVYTCLHY 81

                          90
                  ....*....|....*.
gi 2068696253 110 SateLPLRSQVARLTV 125
Cdd:cd05717    82 T---DPVSTKKVTVTV 94
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 323-389 1.27e-04

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: 41.41  E-value: 1.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253 323 APSSQSAEPDQRVTLKCRV-DANPPPDITWSRPN-----------NPKVVGRGPELLVSATPTSAGLYVCSARSPGFSP 389
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGgtlieslkvkhDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSA 80
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 41-113 1.44e-04

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 41.93  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  41 GSTAVLPCRVINQRGL-------VQWTR---DGF-------GLGTQRGLEG-FE-RYSMIGADEeGDFSLRISPVTLEDD 101
Cdd:cd05877    12 GGNVTLPCRYHYEPELsaprkirVKWTKlevDYAkeedvlvAIGTRHKSYGsYQgRVFLRRADD-LDASLVITDLRLEDY 90

                          90
                  ....*....|..
gi 2068696253 102 AEYQCQVSSATE 113
Cdd:cd05877    91 GRYRCEVIDGLE 102
IGv smart00406
Immunoglobulin V-Type;
43-108 1.52e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 40.83  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253   43 TAVLPCRV---INQRGLVQWTRDGFG-----------LGTQRGLEGF-ERYSMIGADEEGDFSLRISPVTLEDDAEYQCQ 107
Cdd:smart00406   1 SVTLSCKFsgsTFSSYYVSWVRQPPGkglewlgyigsNGSSYYQESYkGRFTISKDTSKNDVSLTISNLRVEDTGTYYCA 80


                   .
gi 2068696253  108 V 108
Cdd:smart00406  81 V 81
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 318-382 1.64e-04

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 40.84  E-value: 1.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068696253 318 PLFVTAPSSQ-SAEPDQRVTLKCRVDANPPPDITW-------SRPNNPKVVGRGPELLVSATPTSAGLYVCSA 382
Cdd:cd20978     1 PKFIQKPEKNvVVKGGQDVTLPCQVTGVPQPKITWlhngkplQGPMERATVEDGTLTIINVQPEDTGYYGCVA 73
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 317-385 1.69e-04

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 41.03  E-value: 1.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253 317 APLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRP-----NNPKV-VGRGPEL----LVSATPTSAGLYVCSARSP 385
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEgkelqNSPDIqIHQEGDLhsliIAEAFEEDTGRYSCLATNS 79
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 318-382 1.72e-04

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


Pssm-ID: 409473  Cd Length: 92  Bit Score: 40.91  E-value: 1.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRPN-----NPKVV-------GRGPELLVSATPTSAGLYVCSA 382
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNemlqyNTDRIslyqdncGRICLLIQNANKKDAGWYTVSA 77
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 317-384 1.95e-04

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.01  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 317 APLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSRPNNPkvVGRGPELLVSATPTSA-----------------GLYV 379
Cdd:cd20956     1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFP--IPESPRFRVGDYVTSDgdvvsyvnissvrvedgGEYT 78


                  ....*
gi 2068696253 380 CSARS 384
Cdd:cd20956    79 CTATN 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 134-214 2.22e-04

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: 40.64  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 134 VTHPAFATAGVPLTLTCSSSGGRPAPEIQWLDGSGAEIHsgvqlSEDLMEDEKRVnAHATLTFTPTRHHHARSLTCLTHN 213
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIE-----SLKVKHDNGRT-TQSSLLISNVTKEDAGTYTCVVNN 75


                  .
gi 2068696253 214 P 214
Cdd:pfam00047  76 P 76
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
 430-496 2.67e-04

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: 40.55  E-value: 2.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253 430 PVSVTWTREGALV-VSEDGRY-VNEEQRADGVVSTLTINKTSHRDFASYNCSVINEYGVDTHQILLQRQ 496
Cdd:cd05735    32 PIIVRWEKEDTIInPSEMSRYlVTTKEVGDEVISTLQILPTVREDSGFFSCHAINSYGEDRGIIQLTVQ 100
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 321-382 2.99e-04

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: 40.18  E-value: 2.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068696253 321 VTAPSSQS---AEPDQRVTLKCRVDANPPPDITWSRPNNP--------KVVGRGPELLV-SATPTSAGLYVCSA 382
Cdd:cd20970     3 ISTPQPSFtvtAREGENATFMCRAEGSPEPEISWTRNGNLiiefntryIVRENGTTLTIrNIRRSDMGIYLCIA 76
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 129-216 3.18e-04

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


Pssm-ID: 409501  Cd Length: 96  Bit Score: 40.57  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 129 PKPPTVTHPAFATAGVPLTL--TCSSSGGRPAPEIQWldgsgaEIHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARS 206
Cdd:cd07704     1 PLVSLNPGPALLIDGGNETLaaSCTAETGKPAASVTW------ETDLGGMESSRTFEHNRTATVTSEYHLVPTRFANGRP 74

                          90
                  ....*....|
gi 2068696253 207 LTCLTHNPAL 216
Cdd:cd07704    75 LTCVVSHPAL 84
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 410-485 3.28e-04

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: 40.42  E-value: 3.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068696253 410 VAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSEDGRYVNEEQRAdgvvSTLTINKTSHRDFASYNCSVINEYG 485
Cdd:cd05747    13 LTVSEGESARFSCDVDGEPAP-TVTWMREGQIIVSSQRHQITSTEYK----STFEISKVQMSDEGNYTVVVENSEG 83
C1-set pfam07654
Immunoglobulin C1-set domain;
125-216 3.72e-04

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 39.93  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 125 VFV-PPKPPTVTHPAfatagvplTLTCSSSGGRPAP-EIQWLDgSGAEIHSGVQLSEDLMEDEKRVNAHATLTFTPTRHH 202
Cdd:pfam07654   1 VYVfPPSPEELGKPN--------TLTCLVTGFYPPDiTVTWLK-NGQEVTEGVKTTPPSPNSDWTYQLSSYLTVTPSDWE 71

                          90
                  ....*....|....
gi 2068696253 203 HARSLTCLTHNPAL 216
Cdd:pfam07654  72 SGDEYTCRVEHEGL 85
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 318-386 4.15e-04

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: 39.94  E-value: 4.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253 318 PLFVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSR------PNNPK---VVGRGPELLVSATP-TSAGLYVCSARSPG 386
Cdd:cd05736     1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKngmdinPKLSKqltLIANGSELHISNVRyEDTGAYTCIAKNEG 79
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 324-389 4.45e-04

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. 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' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 39.40  E-value: 4.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253 324 PSSQSAEPDQRVTLKCRVDANPPPDITWSrpNNPKVVGRGPELLVSA-TPTSAGLYVCSARSPGFSP 389
Cdd:cd20948     2 PSDTYYLSGENLNLSCHAASNPPAQYSWT--INGTFQTSSQELFLPAiTENNEGTYTCSAHNSLTGK 66
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 235-304 4.94e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 39.30  E-value: 4.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 235 QLQFSPEELSEGVEASVTCRVEANPgEVTYRWFRGGSEVAGAQGSTLPlgvLSRADNASPVACEVTNAVG 304
Cdd:pfam13895   3 VLTPSPTVVTEGEPVTLTCSAPGNP-PPSYTWYKDGSAISSSPNFFTL---SVSAEDSGTYTCVARNGRG 68
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 321-385 6.05e-04

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: 39.49  E-value: 6.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068696253 321 VTAPSSQSAEPDQRVTLKCRVdANPPPDITWSR------PNNPKVVgRGPELLVS-ATPTSAGLYVCSARSP 385
Cdd:cd04973    13 ISEVESYSAHPGDLLQLRCRL-RDDVQSINWTKdgvqlgENNRTRI-TGEEVQIKdAVPRDSGLYACVTSSP 82
Ig6_Contactin-4 cd05853
Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth ...
 33-129 6.05e-04

Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-4. 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 different contactins show different expression patterns in the central nervous system. Highest expression of contactin-4 is in testes, thyroid, small intestine, uterus, and brain. Contactin-4 plays a role in the response of neuroblastoma cells to differentiating agents, such as retinoids. The contactin 4 gene is associated with cerebellar degeneration in spinocerebellar ataxia type 16.


Pssm-ID: 409439  Cd Length: 102  Bit Score: 39.61  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  33 PSHQTAVLGSTAVLPCRVINQRGL---VQWTRDGFGLGTQRGLEGFERYSmiGADEEGDfsLRISPVTLEDDAEYQCQVS 109
Cdd:cd05853     9 PSSMDVTVGESIVLPCQVSHDHSLdivFTWSFNGHLIDFQKDGDHFERVG--GQDSAGD--LMIRSIQLKHAGKYVCMVQ 84

                          90       100
                  ....*....|....*....|
gi 2068696253 110 saTELPLRSQVARLTVFVPP 129
Cdd:cd05853    85 --TSVDKLSAAADLIVRGPP 102
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 401-486 6.24e-04

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 39.54  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 401 PPLIRAQAVVAVPEGQPAVLRCGVVAVPHPvSVTWTREGalvvsEDGRYVNEEQRADGVVSTLTINKTSHRDFASYNCSV 480
Cdd:cd20976     2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVP-RITWIRNA-----QPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLA 75


                  ....*.
gi 2068696253 481 INEYGV 486
Cdd:cd20976    76 KNAAGQ 81
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 405-489 8.11e-04

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: 39.13  E-value: 8.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 405 RAQAVVAVPEGQPAVLRCGVVAVPHPvSVTWTREGALVVSED--GRYVNEEQRAdgvvsTLTINKTSHRDFASYNCSVIN 482
Cdd:cd05729     9 MEEREHALPAANKVRLECGAGGNPMP-NITWLKDGKEFKKEHriGGTKVEEKGW-----SLIIERAIPRDKGKYTCIVEN 82


                  ....*..
gi 2068696253 483 EYGVDTH 489
Cdd:cd05729    83 EYGSINH 89
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 332-384 8.34e-04

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


Pssm-ID: 143259  Cd Length: 88  Bit Score: 38.85  E-value: 8.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253 332 DQRVTLKCRVDANPPPDITWSRPNNP-----KVVGRGPEL-LVSATPTSAGLYVCSARS 384
Cdd:cd05851    16 GQNVTLECFALGNPVPVIRWRKILEPmpataEISMSGAVLkIFNIQPEDEGTYECEAEN 74
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 320-382 8.58e-04

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: 39.17  E-value: 8.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068696253 320 FVTAPSSQSAEPDQRVTLKCRVDANPPPDITWSR--------PNNPK-------VVGRGPELLVSATPTSAGLYVCSA 382
Cdd:cd05726     2 FVVKPRDQVVALGRTVTFQCETKGNPQPAIFWQKegsqnllfPYQPPqpssrfsVSPTGDLTITNVQRSDVGYYICQA 79
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 232-314 8.89e-04

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.


Pssm-ID: 409418  Cd Length: 102  Bit Score: 39.33  E-value: 8.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 232 PEVQLQFSPeeLSEGVEASVTCRVEANPGEVTYRWFRGGSEVAGAQ-------------GSTLPLGVlSRADNASPVACE 298
Cdd:cd05761     7 PVITGFTSP--VVEGDEITLTCTTSGSKPAADIRWFKNDKELKGVKevqesgagktftvTSTLRFRV-DRDDDGVAVICR 83

                          90
                  ....*....|....*....
gi 2068696253 299 VTNAV--GTTRKT-QSLNV 314
Cdd:cd05761    84 VDHESltSTPKQTqQVLEV 102
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 33-107 9.24e-04

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: 38.53  E-value: 9.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068696253  33 PSHQTAVLGSTAVLPCRVinqRG----LVQWTRDGFGLGTQRglegferysmigADEEGDFSLRISPVTLEDDAEYQCQ 107
Cdd:cd05725     4 PQNQVVLVDDSAEFQCEV---GGdpvpTVRWRKEDGELPKGR------------YEILDDHSLKIRKVTAGDMGSYTCV 67
IgI_2_KIRREL3-like cd05759
Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 397-483 1.16e-03

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, 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 of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 409416  Cd Length: 98  Bit Score: 38.97  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 397 RIRGPPLIRAQAvvavpeGQPAVLRC-GVVAVPHPvSVTWTREGALVvseDGRYVNEEQRADG----VVSTLTINKTSHR 471
Cdd:cd05759     3 VIEGGPVISLQA------GVPYNLTCrARGAKPAA-EIIWFRDGEQL---EGAVYSKELLKDGkretTVSTLLITPSDLD 72

                          90
                  ....*....|..
gi 2068696253 472 DFASYNCSVINE 483
Cdd:cd05759    73 TGRTFTCRARNE 84
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 33-111 1.21e-03

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: 39.24  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  33 PSHQTAVLGSTAVLPCRVINQRGL--VQW--TRDGFGL---------GTQRGLEGFERYSMIGaDEEGDFSLRISPVTLE 99
Cdd:cd00099     5 PRSLSVQEGESVTLSCEVSSSFSStyIYWyrQKPGQGPefliylsssKGKTKGGVPGRFSGSR-DGTSSFSLTISNLQPE 83

                          90
                  ....*....|..
gi 2068696253 100 DDAEYQCQVSSA 111
Cdd:cd00099    84 DSGTYYCAVSES 95
C1-set pfam07654
Immunoglobulin C1-set domain;
412-483 1.22e-03

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 38.39  E-value: 1.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068696253 412 VPEGQPAVLRCGVVAV-PHPVSVTWTREGALVvSEDGRYVNEEQRADG---VVSTLTINKTSHRDFASYNCSVINE 483
Cdd:pfam07654   9 EELGKPNTLTCLVTGFyPPDITVTWLKNGQEV-TEGVKTTPPSPNSDWtyqLSSYLTVTPSDWESGDEYTCRVEHE 83
IgI_2_Necl-1 cd07705
Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set ...
 127-217 1.31e-03

Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1; also known as cell adhesion molecule3 (CADM3)). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains is essential to cell-cell adhesion and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 409502  Cd Length: 103  Bit Score: 38.80  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 127 VPPKPPTVTHPAFATAGVPLTLTCSSSGGRPAPEIQWLDGSgAEIHsGVQLSedLMED--EKRVNAHATLTFTPTRHHHA 204
Cdd:cd07705     3 IPQKPQITGYESAFKEKDKAKLRCTSSGSKPAANIKWRKGD-QELE-GAPTS--VQEDgnGKTFTVSSSVEFQVTREDDG 78

                          90
                  ....*....|...
gi 2068696253 205 RSLTCLTHNPALH 217
Cdd:cd07705    79 AEITCSVGHESLH 91
IGc1 smart00407
Immunoglobulin C-Type;
145-219 1.33e-03

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 38.06  E-value: 1.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068696253  145 PLTLTCSSSGGRPAP-EIQWLDGsGAEIHSGVQLSEDLMEDEKRVNAHATLTFTPTRHHHARSLTC-LTHnPALHTP 219
Cdd:smart00407   1 KATLVCLVSGFYPPDiTVTWLRN-GQEVTEGVSTTDPLKNSDGTYFLSSYLTVPASTWESGDVYTCqVTH-EGLKEP 75
IGc1 smart00407
Immunoglobulin C-Type;
417-483 1.78e-03

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 37.68  E-value: 1.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068696253  417 PAVLRCGVVAV-PHPVSVTWTREGALVVSEdgrYVNEEQRADG-----VVSTLTINKTSHRDFASYNCSVINE 483
Cdd:smart00407   1 KATLVCLVSGFyPPDITVTWLRNGQEVTEG---VSTTDPLKNSdgtyfLSSYLTVPASTWESGDVYTCQVTHE 70
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 415-490 1.87e-03

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 38.31  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 415 GQPAVLRCGVVAVPHPVsVTWTREGaLVVSEDGR-----YVNEEQRadgVVSTLTINKTSHRDFASYNCSVINEYGVDTH 489
Cdd:cd20956    16 GPSVSLKCVASGNPLPQ-ITWTLDG-FPIPESPRfrvgdYVTSDGD---VVSYVNISSVRVEDGGEYTCTATNDVGSVSH 90


                  .
gi 2068696253 490 Q 490
Cdd:cd20956    91 S 91
IgV_1_Necl-1 cd05882
First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-1 (Necl-1); member ...
 34-125 2.38e-03

First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-1 (Necl-1); member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-1, Necl-1 (also known as celll adhesion molecule 3 (CADM3), SynCAM2, or IGSF4). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons.


Pssm-ID: 143290  Cd Length: 95  Bit Score: 37.72  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  34 SHQTAVLGSTAVLPCRVI-NQRGLVQWT---RDGFGLGTQRGLEGfERYSMIGADEEgDFSLRISPVTLEDDAEYQCQVS 109
Cdd:cd05882     5 QDETVAVGGTVTLKCGVKeHDNSSLQWSntaQQTLYFGEKRALRD-NRIQLVKSTPT-ELIISISNVQLSDEGEYTCSIF 82

                          90
                  ....*....|....*.
gi 2068696253 110 SateLPLRSQVARLTV 125
Cdd:cd05882    83 T---MPVRTAKATVTV 95
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 149-228 2.86e-03

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 37.86  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 149 TCSSSGGRPAPEIQW---LDGsgaeihsgvqlsedlMEDEKRV-NAHATLTFT------PTRHHHARSLTCLTHNPALHT 218
Cdd:cd05719    22 TCISANGKPPASVTWetdLKG---------------EASTTQVrGSNGTVTVTsryrlvPSREADGQPLTCVVEHPSLEK 86

                          90
                  ....*....|
gi 2068696253 219 PLAAKVRLNV 228
Cdd:cd05719    87 DQRISVTLNV 96
IgC1_hNephrin_like cd05773
Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig ...
 399-493 3.90e-03

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.


Pssm-ID: 143250  Cd Length: 109  Bit Score: 37.60  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253 399 RGPPLIRaqavVAVP--EGQPAVLRCGVVAVPHpVSVTWTREGALVVSEDGRYVNEEQRADGV-VSTLTI-NKTSHRDFA 474
Cdd:cd05773     9 KGPQLRK----VASRgdGSSDANLVCQAQGVPR-VQFRWAKNGVPLDLGNPRYEETTEHTGTVhTSILTIiNVSAALDYA 83

                          90
                  ....*....|....*....
gi 2068696253 475 SYNCSVINEYGVDTHQILL 493
Cdd:cd05773    84 LFTCTAHNSLGEDSLDIQL 102
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 33-125 3.91e-03

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: 37.64  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068696253  33 PSHQTAVLGSTAVLPCR--VINQRGLvQWTRDGFGLGTQ--------RGLEGFERYSMIGADEEGDFSLRISPVTLEDDA 102
Cdd:cd04983     5 PQSLSVQEGENVTLNCNysTSTFYYL-FWYRQYPGQGPQfliyissdSGNKKKGRFSATLDKSRKSSSLHISAAQLSDSA 83

                          90       100
                  ....*....|....*....|....*
gi 2068696253 103 EYQCQVS--SATELPLRSQVARLTV 125
Cdd:cd04983    84 VYFCALSesGGTGKLTFGKGTRLTV 108
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 240-305 5.74e-03

First immunoglobulin (Ig) domain of contactin-2; 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-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. 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. 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-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409437 [Multi-domain]  Cd Length: 97  Bit Score: 36.83  E-value: 5.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068696253 240 PEELSEGvEASVTCRVEANPgEVTYRWFRGGSEVAGAQGS--TLPLGVL-----SRADNASPVACEVTNAVGT 305
Cdd:cd05850    15 PEGSAEE-KVTLACRARASP-PATYRWKMNGTELKMEPDSryRLVAGNLvisnpVKAKDAGSYQCLASNRRGT 85
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 77-111 6.00e-03

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 37.05  E-value: 6.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2068696253  77 RYSMIGADEEGDFSLRISPVTLEDDAEYQCQVSSA 111
Cdd:cd20960    69 RVAFTSNDLSGDASLNISNLKLSDTGTYQCKVKKA 103
 
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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