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Conserved domains on  [gi|675620728|ref|XP_008938393|]
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PREDICTED: protein turtle homolog B, partial [Merops nubicus]

Protein Classification

Ig and FN3 domain-containing protein( domain architecture ID 10307510)

Ig and FN3 domain-containing protein similar to Homo sapiens contactins, which are comprised of six immunoglobulin (Ig)-like domains followed by four fibronectin type III (Fn3) domains anchored to the membrane by glycosylphosphatidylinositol, and to Robo (roundabout) receptors which typically contain five Ig-like domains and three FN3 domains

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 ...
 169-261 1.11e-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 pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  169 PFIVSPPENITVNISQDALFTCQAEAYPgnltylwywEEENVYFKNDLKL----RVRILIDG---TLIIFRVKPEDAGKY 241
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTP---------DPEVSWFKDGQPLrssdRFKVTYEGgtyTLTISNVQPDDSGKY 71

                          90       100
                  ....*....|....*....|
gi 675620728  242 TCIPSNSLGRSpSASAYLTV 261
Cdd:pfam07679  72 TCVATNSAGEA-EASAELTV 90
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
411-643 1.53e-11

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.72  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 411 GTLQSTSPHAPTSVHVVAAM-TSANVSWEPGYDG---GYEqtfsvwygplMKRAQFGPHDWLSLPVPAGSSWllVDT-LE 485
Cdd:COG3401  226 VTTPTTPPSAPTGLTATADTpGSVTLSWDPVTESdatGYR----------VYRSNSGDGPFTKVATVTTTSY--TDTgLT 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 486 PETAYQFSVLAQNKLGTSS-FSEVVTVNTLAFPVTTPEPLVlvtpprclTANRTQQGVLLSWlpPANHSFPIDRYIMEFR 564
Cdd:COG3401  294 NGTTYYYRVTAVDAAGNESaPSNVVSVTTDLTPPAAPSGLT--------ATAVGSSSITLSW--TASSDADVTGYNVYRS 363

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 565 IAE--RWEILDDGIpgTENEFFAKDLSQDTWYEFRVLAVMQD-LISEPSNVAGVSSTDVFPQPDLTDEGLARPVLAGIVA 641
Cdd:COG3401  364 TSGggTYTKIAETV--TTTSYTDTGLTPGTTYYYKVTAVDAAgNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGA 441


                 ..
gi 675620728 642 TI 643
Cdd:COG3401  442 TA 443
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 11-93 2.24e-08

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


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   11 VTARAGESVILGCDVihplTGQPPPyVVEWFKFGVPIpifikfgfyppHVDPEYAGRASlHDKASLRIEQVRSEDQGWYE 90
Cdd:pfam07679  10 VEVQEGESARFTCTV----TGTPDP-EVSWFKDGQPL-----------RSSDRFKVTYE-GGTYTLTISNVQPDDSGKYT 72


                  ...
gi 675620728   91 CKV 93
Cdd:pfam07679  73 CVA 75
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 284-345 8.23e-07

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 cd20952:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 87  Bit Score: 47.49  E-value: 8.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675620728 284 IRCPVEAEPpVTLVKWNKDGRPLRIeKYSGWNLLEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:cd20952   19 LNCQATGEP-VPTISWLKDGVPLLG-KDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 369-414 4.51e-04

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 cd20952:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 87  Bit Score: 39.79  E-value: 4.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 675620728 369 EYRQEAGRELLIPCAAAGDPFPIIAWRKVGKPSRSKH---NTLPGGTLQ 414
Cdd:cd20952    8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDeriTTLENGSLQ 56
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 118-147 1.77e-03

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 cd05728:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 85  Bit Score: 37.96  E-value: 1.77e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 675620728 118 CMAFGNPKPIVTWLREGDLLGANGKYQVGG 147
Cdd:cd05728   21 CKASGNPRPAYRWLKNGQPLASENRIEVEA 50
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
169-261 1.11e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  169 PFIVSPPENITVNISQDALFTCQAEAYPgnltylwywEEENVYFKNDLKL----RVRILIDG---TLIIFRVKPEDAGKY 241
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTP---------DPEVSWFKDGQPLrssdRFKVTYEGgtyTLTISNVQPDDSGKY 71

                          90       100
                  ....*....|....*....|
gi 675620728  242 TCIPSNSLGRSpSASAYLTV 261
Cdd:pfam07679  72 TCVATNSAGEA-EASAELTV 90
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
411-643 1.53e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.72  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 411 GTLQSTSPHAPTSVHVVAAM-TSANVSWEPGYDG---GYEqtfsvwygplMKRAQFGPHDWLSLPVPAGSSWllVDT-LE 485
Cdd:COG3401  226 VTTPTTPPSAPTGLTATADTpGSVTLSWDPVTESdatGYR----------VYRSNSGDGPFTKVATVTTTSY--TDTgLT 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 486 PETAYQFSVLAQNKLGTSS-FSEVVTVNTLAFPVTTPEPLVlvtpprclTANRTQQGVLLSWlpPANHSFPIDRYIMEFR 564
Cdd:COG3401  294 NGTTYYYRVTAVDAAGNESaPSNVVSVTTDLTPPAAPSGLT--------ATAVGSSSITLSW--TASSDADVTGYNVYRS 363

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 565 IAE--RWEILDDGIpgTENEFFAKDLSQDTWYEFRVLAVMQD-LISEPSNVAGVSSTDVFPQPDLTDEGLARPVLAGIVA 641
Cdd:COG3401  364 TSGggTYTKIAETV--TTTSYTDTGLTPGTTYYYKVTAVDAAgNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGA 441


                 ..
gi 675620728 642 TI 643
Cdd:COG3401  442 TA 443
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 175-261 4.97e-11

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: 59.44  E-value: 4.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   175 PENITVNISQDALFTCQAEAYPgNLTYLWYWEEENVYFKNDLKLRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLGrSPS 254
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSP-PPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                   ....*..
gi 675620728   255 ASAYLTV 261
Cdd:smart00410  79 SGTTLTV 85
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 172-261 1.01e-10

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: 58.56  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 172 VSPPENITVNISQDALFTCQAEAYPGNlTYLWYWEEENVyfkndLKLRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLGR 251
Cdd:cd05725    1 VKRPQNQVVLVDDSAEFQCEVGGDPVP-TVRWRKEDGEL-----PKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGK 74

                         90
                 ....*....|
gi 675620728 252 SpSASAYLTV 261
Cdd:cd05725   75 I-EASATLTV 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 418-513 6.24e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.74  E-value: 6.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 418 PHAPTSVHVVAAM-TSANVSWE-PGYDGGYEQTFSVWYGPLmkraqfGPHDWLSLPVPAGSS-WLLVDTLEPETAYQFSV 494
Cdd:cd00063    1 PSPPTNLRVTDVTsTSVTLSWTpPEDDGGPITGYVVEYREK------GSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRV 74

                         90
                 ....*....|....*....
gi 675620728 495 LAQNKLGTSSFSEVVTVNT 513
Cdd:cd00063   75 RAVNGGGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
11-93 2.24e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   11 VTARAGESVILGCDVihplTGQPPPyVVEWFKFGVPIpifikfgfyppHVDPEYAGRASlHDKASLRIEQVRSEDQGWYE 90
Cdd:pfam07679  10 VEVQEGESARFTCTV----TGTPDP-EVSWFKDGQPL-----------RSSDRFKVTYE-GGTYTLTISNVQPDDSGKYT 72


                  ...
gi 675620728   91 CKV 93
Cdd:pfam07679  73 CVA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 418-503 2.59e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.85  E-value: 2.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   418 PHAPTSVHVVAAM-TSANVSWEPGYD---GGYEQTFSVWYGPlmkraqfGPHDWLSLPVPAGSSWLLVDTLEPETAYQFS 493
Cdd:smart00060   1 PSPPSNLRVTDVTsTSVTLSWEPPPDdgiTGYIVGYRVEYRE-------EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFR 73

                           90
                   ....*....|
gi 675620728   494 VLAQNKLGTS 503
Cdd:smart00060  74 VRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 8-113 1.33e-07

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: 49.81  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728     8 PEFVTARAGESVILGCDVihplTGQPPPYVvEWFKFGvPIPIFIKFGFyppHVDPEyagraslHDKASLRIEQVRSEDQG 87
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEV-TWYKQG-GKLLAESGRF---SVSRS-------GSTSTLTISNVTPEDSG 64

                           90       100
                   ....*....|....*....|....*.
gi 675620728    88 WYECKVlmLDQQYDTFHNgswVHLTV 113
Cdd:smart00410  65 TYTCAA--TNSSGSASSG---TTLTV 85
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 5-91 6.57e-07

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.88  E-value: 6.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   5 REEPEFVTARAGESVILGCDVihplTGQPPPyVVEWFKFGVPIPIfikfgfypphVDPeyagRASLHDKASLRIEQVRSE 84
Cdd:cd20952    3 LQGPQNQTVAVGGTVVLNCQA----TGEPVP-TISWLKDGVPLLG----------KDE----RITTLENGSLQIKGAEKS 63


                 ....*..
gi 675620728  85 DQGWYEC 91
Cdd:cd20952   64 DTGEYTC 70
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 284-345 8.23e-07

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.49  E-value: 8.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675620728 284 IRCPVEAEPpVTLVKWNKDGRPLRIeKYSGWNLLEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:cd20952   19 LNCQATGEP-VPTISWLKDGVPLLG-KDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78
fn3 pfam00041
Fibronectin type III domain;
420-506 5.57e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  420 APTSVHVVAAM-TSANVSWEPGYDGGYEQT-FSVWYgplmkRAQFGPHDWLSLPVPAGSSWLLVDTLEPETAYQFSVLAQ 497
Cdd:pfam00041   2 APSNLTVTDVTsTSLTVSWTPPPDGNGPITgYEVEY-----RPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76


                  ....*....
gi 675620728  498 NKLGTSSFS 506
Cdd:pfam00041  77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
286-345 4.48e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 4.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675620728  286 CPVEAEPPVTlVKWNKDGRPLRIE-----KYSGwnllEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:pfam07679  22 CTVTGTPDPE-VSWFKDGQPLRSSdrfkvTYEG----GTYTLTISNVQPDDSGKYTCVATNSAGE 81
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 369-414 4.51e-04

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 39.79  E-value: 4.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 675620728 369 EYRQEAGRELLIPCAAAGDPFPIIAWRKVGKPSRSKH---NTLPGGTLQ 414
Cdd:cd20952    8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDeriTTLENGSLQ 56
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 359-414 1.22e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.32  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 675620728  359 PPYFTVLPGWEYRQEaGRELLIPCAAAGDPFPIIAWRKVGKP-----SRSKHNTLPGGTLQ 414
Cdd:pfam13927   1 KPVITVSPSSVTVRE-GETVTLTCEATGSPPPTITWYKNGEPissgsTRSRSLSGSNSTLT 60
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 284-345 1.60e-03

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: 38.26  E-value: 1.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675620728   284 IRCPVEAEPPVTlVKWNKDGRPLRIEK--YSGWNLLEDGSIRIEEAT-EDAlGTYTCVPYNALGT 345
Cdd:smart00410  14 LSCEASGSPPPE-VTWYKQGGKLLAESgrFSVSRSGSTSTLTISNVTpEDS-GTYTCAATNSSGS 76
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 118-147 1.77e-03

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 37.96  E-value: 1.77e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 675620728 118 CMAFGNPKPIVTWLREGDLLGANGKYQVGG 147
Cdd:cd05728   21 CKASGNPRPAYRWLKNGQPLASENRIEVEA 50
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
169-261 1.11e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 69.98  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  169 PFIVSPPENITVNISQDALFTCQAEAYPgnltylwywEEENVYFKNDLKL----RVRILIDG---TLIIFRVKPEDAGKY 241
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTP---------DPEVSWFKDGQPLrssdRFKVTYEGgtyTLTISNVQPDDSGKY 71

                          90       100
                  ....*....|....*....|
gi 675620728  242 TCIPSNSLGRSpSASAYLTV 261
Cdd:pfam07679  72 TCVATNSAGEA-EASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 168-247 7.28e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.21  E-value: 7.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  168 PPFIVSPPENITVNISQDALFTCQAEAYPGNlTYLWYWEEEnVYFKNDLKLRVRILIDGTLIIFRVKPEDAGKYTCIPSN 247
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPP-TITWYKNGE-PISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
411-643 1.53e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.72  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 411 GTLQSTSPHAPTSVHVVAAM-TSANVSWEPGYDG---GYEqtfsvwygplMKRAQFGPHDWLSLPVPAGSSWllVDT-LE 485
Cdd:COG3401  226 VTTPTTPPSAPTGLTATADTpGSVTLSWDPVTESdatGYR----------VYRSNSGDGPFTKVATVTTTSY--TDTgLT 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 486 PETAYQFSVLAQNKLGTSS-FSEVVTVNTLAFPVTTPEPLVlvtpprclTANRTQQGVLLSWlpPANHSFPIDRYIMEFR 564
Cdd:COG3401  294 NGTTYYYRVTAVDAAGNESaPSNVVSVTTDLTPPAAPSGLT--------ATAVGSSSITLSW--TASSDADVTGYNVYRS 363

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 565 IAE--RWEILDDGIpgTENEFFAKDLSQDTWYEFRVLAVMQD-LISEPSNVAGVSSTDVFPQPDLTDEGLARPVLAGIVA 641
Cdd:COG3401  364 TSGggTYTKIAETV--TTTSYTDTGLTPGTTYYYKVTAVDAAgNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGA 441


                 ..
gi 675620728 642 TI 643
Cdd:COG3401  442 TA 443
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 175-261 4.97e-11

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: 59.44  E-value: 4.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   175 PENITVNISQDALFTCQAEAYPgNLTYLWYWEEENVYFKNDLKLRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLGrSPS 254
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSP-PPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG-SAS 78


                   ....*..
gi 675620728   255 ASAYLTV 261
Cdd:smart00410  79 SGTTLTV 85
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 172-261 1.01e-10

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: 58.56  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 172 VSPPENITVNISQDALFTCQAEAYPGNlTYLWYWEEENVyfkndLKLRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLGR 251
Cdd:cd05725    1 VKRPQNQVVLVDDSAEFQCEVGGDPVP-TVRWRKEDGEL-----PKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGK 74

                         90
                 ....*....|
gi 675620728 252 SpSASAYLTV 261
Cdd:cd05725   75 I-EASATLTV 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 418-513 6.24e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.74  E-value: 6.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 418 PHAPTSVHVVAAM-TSANVSWE-PGYDGGYEQTFSVWYGPLmkraqfGPHDWLSLPVPAGSS-WLLVDTLEPETAYQFSV 494
Cdd:cd00063    1 PSPPTNLRVTDVTsTSVTLSWTpPEDDGGPITGYVVEYREK------GSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRV 74

                         90
                 ....*....|....*....
gi 675620728 495 LAQNKLGTSSFSEVVTVNT 513
Cdd:cd00063   75 RAVNGGGESPPSESVTVTT 93
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 171-261 7.71e-10

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 56.35  E-value: 7.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 171 IVSPPENITVNISQDALFTCQAEAYPGNlTYLWYWEEENVYFKNDlklRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLG 250
Cdd:cd20952    2 ILQGPQNQTVAVGGTVVLNCQATGEPVP-TISWLKDGVPLLGKDE---RITTLENGSLQIKGAEKSDTGEYTCVALNLSG 77

                         90
                 ....*....|.
gi 675620728 251 rSPSASAYLTV 261
Cdd:cd20952   78 -EATWSAVLDV 87
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
432-622 9.06e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 62.33  E-value: 9.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 432 SANVSWEPGYDGGYEQTFSVWYGPLMKRAQFGPHDWLSLPVPAGSSWLLVD---TLEPETAYQFSVLAQNKLGTSSFSEV 508
Cdd:COG3401  144 GAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDgggDIEPGTTYYYRVAATDTGGESAPSNE 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 509 VTVNTLAFPVTTPEPLVlvtpprclTANRTQQGVLLSWLPPANHSfpIDRYIMEFRIAE--RWEILDDgipGTENEFFAK 586
Cdd:COG3401  224 VSVTTPTTPPSAPTGLT--------ATADTPGSVTLSWDPVTESD--ATGYRVYRSNSGdgPFTKVAT---VTTTSYTDT 290

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 675620728 587 DLSQDTWYEFRVLAVMQD-LISEPSNVAGVsSTDVFP 622
Cdd:COG3401  291 GLTNGTTYYYRVTAVDAAgNESAPSNVVSV-TTDLTP 326
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 186-257 2.35e-09

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: 54.26  E-value: 2.35e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675620728 186 ALFTCQAEAYPgNLTYLWYWEEENVYFKNDLKlRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLGRSPSASA 257
Cdd:cd00096    1 VTLTCSASGNP-PPTITWYKNGKPLPPSSRDS-RRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 214-261 2.85e-09

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 54.71  E-value: 2.85e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 675620728 214 NDLKLRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLGRSPSASAYLTV 261
Cdd:cd05724   40 NLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERESRAARLSV 87
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 168-261 3.23e-09

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 54.50  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIvSPPENITVNISQDALFTCQAEAYP-GNLTylwyWEeenvyfKNDLKL----RVRILIDGTLIIFRV-KPEDAGKY 241
Cdd:cd20958    1 PPFI-RPMGNLTAVAGQTLRLHCPVAGYPiSSIT----WE------KDGRRLplnhRQRVFPNGTLVIENVqRSSDEGEY 69

                         90       100
                 ....*....|....*....|
gi 675620728 242 TCIPSNSLGRSPSASAYLTV 261
Cdd:cd20958   70 TCTARNQQGQSASRSVFVKV 89
I-set pfam07679
Immunoglobulin I-set domain;
11-93 2.24e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   11 VTARAGESVILGCDVihplTGQPPPyVVEWFKFGVPIpifikfgfyppHVDPEYAGRASlHDKASLRIEQVRSEDQGWYE 90
Cdd:pfam07679  10 VEVQEGESARFTCTV----TGTPDP-EVSWFKDGQPL-----------RSSDRFKVTYE-GGTYTLTISNVQPDDSGKYT 72


                  ...
gi 675620728   91 CKV 93
Cdd:pfam07679  73 CVA 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 529-611 2.44e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.11  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 529 PPRCLTA-NRTQQGVLLSWLPPANHSFPIDRYIMEFRIA--ERWEILDDGiPGTENEFFAKDLSQDTWYEFRVLAVMQDL 605
Cdd:cd00063    3 PPTNLRVtDVTSTSVTLSWTPPEDDGGPITGYVVEYREKgsGDWKEVEVT-PGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                 ....*.
gi 675620728 606 ISEPSN 611
Cdd:cd00063   82 ESPPSE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 418-503 2.59e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.85  E-value: 2.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   418 PHAPTSVHVVAAM-TSANVSWEPGYD---GGYEQTFSVWYGPlmkraqfGPHDWLSLPVPAGSSWLLVDTLEPETAYQFS 493
Cdd:smart00060   1 PSPPSNLRVTDVTsTSVTLSWEPPPDdgiTGYIVGYRVEYRE-------EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFR 73

                           90
                   ....*....|
gi 675620728   494 VLAQNKLGTS 503
Cdd:smart00060  74 VRAVNGAGEG 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 168-261 3.09e-08

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 51.69  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIVSPPENIT-VNISQDALFTCQAEAYPgNLTYLWYWEEENVyfKNDLklRVRILIDGTLIIFRVKPEDAGKYTCIPS 246
Cdd:cd04969    1 PDFELNPVKKKIlAAKGGDVIIECKPKASP-KPTISWSKGTELL--TNSS--RICILPDGSLKIKNVTKSDEGKYTCFAV 75

                         90
                 ....*....|....*
gi 675620728 247 NSLGrSPSASAYLTV 261
Cdd:cd04969   76 NFFG-KANSTGSLSV 89
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 168-261 3.65e-08

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: 51.62  E-value: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIVSPPENITVNISQDALFTCQAEAYPgnltylwywEEENVYFKNDLKL---RVRILI-DGTLIIFRVKPEDAGKYTC 243
Cdd:cd20978    1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVP---------QPKITWLHNGKPLqgpMERATVeDGTLTIINVQPEDTGYYGC 71

                         90
                 ....*....|....*...
gi 675620728 244 IPSNSLGRSPSaSAYLTV 261
Cdd:cd20978   72 VATNEIGDIYT-ETLLHV 88
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 169-261 6.27e-08

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 51.01  E-value: 6.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 169 PFIVSPPENITVNISQDALFTCQAEAYPgNLTYLWYWEEENVYF-KNDLKLRVRILIDGTLIIFRVKP-----EDAGKYT 242
Cdd:cd07693    1 PRIVEHPSDLIVSKGDPATLNCKAEGRP-TPTIQWLKNGQPLETdKDDPRSHRIVLPSGSLFFLRVVHgrkgrSDEGVYV 79

                         90
                 ....*....|....*....
gi 675620728 243 CIPSNSLGRSPSASAYLTV 261
Cdd:cd07693   80 CVAHNSLGEAVSRNASLEV 98
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 8-113 1.33e-07

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: 49.81  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728     8 PEFVTARAGESVILGCDVihplTGQPPPYVvEWFKFGvPIPIFIKFGFyppHVDPEyagraslHDKASLRIEQVRSEDQG 87
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEV-TWYKQG-GKLLAESGRF---SVSRS-------GSTSTLTISNVTPEDSG 64

                           90       100
                   ....*....|....*....|....*.
gi 675620728    88 WYECKVlmLDQQYDTFHNgswVHLTV 113
Cdd:smart00410  65 TYTCAA--TNSSGSASSG---TTLTV 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 171-262 1.33e-07

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 49.93  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 171 IVSPPENITVNISQDALFTCQAEAYPgNLTYLWYWEEENVYFKNdlklRVRILIDGTLIIFRVKPEDAGKYTCIPSNSLG 250
Cdd:cd20968    2 ITRPPTNVTIIEGLKAVLPCTTMGNP-KPSVSWIKGDDLIKENN----RIAVLESGSLRIHNVQKEDAGQYRCVAKNSLG 76

                         90
                 ....*....|..
gi 675620728 251 RSPSASAYLTVQ 262
Cdd:cd20968   77 IAYSKPVTIEVE 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 175-247 3.16e-07

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


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 48.68  E-value: 3.16e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 675620728 175 PENITVNISQDALFTCQAEAYPGNlTYLWYweeenvyfKNDLKL----RVRILIDGTLIIFRVKPEDAGKYTCIPSN 247
Cdd:cd20957    8 PPVQTVDFGRTAVFNCSVTGNPIH-TVLWM--------KDGKPLghssRVQILSEDVLVIPSVKREDKGMYQCFVRN 75
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 5-91 6.57e-07

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.88  E-value: 6.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   5 REEPEFVTARAGESVILGCDVihplTGQPPPyVVEWFKFGVPIPIfikfgfypphVDPeyagRASLHDKASLRIEQVRSE 84
Cdd:cd20952    3 LQGPQNQTVAVGGTVVLNCQA----TGEPVP-TISWLKDGVPLLG----------KDE----RITTLENGSLQIKGAEKS 63


                 ....*..
gi 675620728  85 DQGWYEC 91
Cdd:cd20952   64 DTGEYTC 70
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 284-345 8.23e-07

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 47.49  E-value: 8.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675620728 284 IRCPVEAEPpVTLVKWNKDGRPLRIeKYSGWNLLEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:cd20952   19 LNCQATGEP-VPTISWLKDGVPLLG-KDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 19-93 9.99e-07

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: 46.94  E-value: 9.99e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675620728  19 VILGCDVihplTGQPPPyVVEWFKFGVPIPifikfgfypphvDPEYAGRASLHDKASLRIEQVRSEDQGWYECKV 93
Cdd:cd00096    1 VTLTCSA----SGNPPP-TITWYKNGKPLP------------PSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA 58
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 285-345 1.27e-06

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: 47.00  E-value: 1.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 675620728 285 RCPVEAEPPVTlVKWNKDGRPLRIEKYsgwNLLEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:cd05725   18 QCEVGGDPVPT-VRWRKEDGELPKGRY---EILDDHSLKIRKVTAGDMGSYTCVAENMVGK 74
IgI_2_Dscam cd20953
Second immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 178-261 1.33e-06

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


Pssm-ID: 409545  Cd Length: 95  Bit Score: 47.15  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 178 ITVNISQDALFTCQAEAYPGNLtYLWYWEEENVYFKNDLKLRVRI-LIDGTLIIFRVKPEDAGKYTCIPSNSLGrSPSAS 256
Cdd:cd20953   13 LTVSSASSIALLCPAQGYPAPS-FRWYKFIEGTTRKQAVVLNDRVkQVSGTLIIKDAVVEDSGKYLCVVNNSVG-GESVE 90


                 ....*
gi 675620728 257 AYLTV 261
Cdd:cd20953   91 TVLTV 95
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 168-261 1.70e-06

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


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 46.92  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIVSPPENITVNISQDALFTCQAEAYPgNLTYLW---YWEEENVYfkNDLKLR--VRILIDGTLIIFRVKPEDAGKYT 242
Cdd:cd20954    1 PPRWIVEPVDANVAAGQDVMLHCQADGFP-TPTVTWkkaTGSTPGEY--KDLLYDpnVRILPNGTLVFGHVQKENEGHYL 77

                         90
                 ....*....|....*....
gi 675620728 243 CIPSNSLGRSPSASAYLTV 261
Cdd:cd20954   78 CEAKNGIGSGLSKVIFLKV 96
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 11-93 1.85e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   11 VTARAGESVILGCDVihplTGQPPPyVVEWFKFGVPIPifikfgfypphvDPEYAGRASLHDKASLRIEQVRSEDQGWYE 90
Cdd:pfam13927  11 VTVREGETVTLTCEA----TGSPPP-TITWYKNGEPIS------------SGSTRSRSLSGSNSTLTISNVTRSDAGTYT 73


                  ...
gi 675620728   91 CKV 93
Cdd:pfam13927  74 CVA 76
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 168-261 2.34e-06

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 46.72  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIVSPPENitvnisQDALF------TCQAEAYPGNlTYLWYWEE----ENVYFKNDLKLRVRILIDGTLIIFRVKPED 237
Cdd:cd05734    1 PPRFVVQPND------QDGIYgkavvlNCSADGYPPP-TIVWKHSKgsgvPQFQHIVPLNGRIQLLSNGSLLIKHVLEED 73

                         90       100
                 ....*....|....*....|....
gi 675620728 238 AGKYTCIPSNSLGRSPSASAYLTV 261
Cdd:cd05734   74 SGYYLCKVSNDVGADISKSMYLTV 97
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 266-345 4.58e-06

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: 45.78  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 266 RVVNMPPVIYIPIGIHGYIRCPVEAEPPvTLVKWNKDGRPLR--IEKYSGWNLLEDGsIRIEEATEDALGTYTCVPYNAL 343
Cdd:cd20949    1 TFTENAYVTTVKEGQSATILCEVKGEPQ-PNVTWHFNGQPISasVADMSKYRILADG-LLINKVTQDDTGEYTCRAYQVN 78


                 ..
gi 675620728 344 GT 345
Cdd:cd20949   79 SI 80
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 173-250 5.00e-06

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.26  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  173 SPPENITVNISQDALFTCQAEAYPGNLTYLW-----YWEEENVYFKNDLKLRVrilidGTLIIFRVKPEDAGKYTCIPSN 247
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWskeggTLIESLKVKHDNGRTTQ-----SSLLISNVTKEDAGTYTCVVNN 75


                  ...
gi 675620728  248 SLG 250
Cdd:pfam00047  76 PGG 78
fn3 pfam00041
Fibronectin type III domain;
420-506 5.57e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  420 APTSVHVVAAM-TSANVSWEPGYDGGYEQT-FSVWYgplmkRAQFGPHDWLSLPVPAGSSWLLVDTLEPETAYQFSVLAQ 497
Cdd:pfam00041   2 APSNLTVTDVTsTSLTVSWTPPPDGNGPITgYEVEY-----RPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76


                  ....*....
gi 675620728  498 NKLGTSSFS 506
Cdd:pfam00041  77 NGGGEGPPS 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 284-345 5.72e-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: 5.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675620728 284 IRCPVEAEPPVTlVKWNKDGRPLRIEK-YSGWNLLEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:cd00096    3 LTCSASGNPPPT-ITWYKNGKPLPPSSrDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 291-354 8.66e-06

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 44.70  E-value: 8.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 675620728 291 EPPVTlvkWNKDGRPLRIEKySGWNLLEDGSIRIEEATEDALGTYTCVPYNALGTMgQSPPARL 354
Cdd:cd05724   27 EPTVS---WRKDGQPLNLDN-ERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGER-ESRAARL 85
fn3 pfam00041
Fibronectin type III domain;
529-610 1.07e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  529 PPRCLTA-NRTQQGVLLSWLPPANHSFPIDRYIMEFRIAER-WEILDDGIPGTENEFFAKDLSQDTWYEFRVLAVMQDLI 606
Cdd:pfam00041   2 APSNLTVtDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                  ....
gi 675620728  607 SEPS 610
Cdd:pfam00041  82 GPPS 85
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 173-262 1.15e-05

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: 44.42  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 173 SPPENITVNISQDALFTCQAEAYPgnltylwywEEENVYFKNDLKL-----RVRILIDGT-LIIFRVKPEDAGKYTCIPS 246
Cdd:cd20970    7 QPSFTVTAREGENATFMCRAEGSP---------EPEISWTRNGNLIiefntRYIVRENGTtLTIRNIRRSDMGIYLCIAS 77

                         90
                 ....*....|....*.
gi 675620728 247 NslGRSPSASAYLTVQ 262
Cdd:cd20970   78 N--GVPGSVEKRITLQ 91
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 168-264 1.39e-05

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


Pssm-ID: 409359  Cd Length: 102  Bit Score: 44.46  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIVSPPENITVNISQDALFTCQAEAYPG-NLTYLWY-------WEEENVYFKNDLKLRVriliDGTLIIFRVKPEDAG 239
Cdd:cd04970    2 ATRITLAPSNADITVGENATLQCHASHDPTlDLTFTWSfngvpidLEKIEGHYRRRYGKDS----NGDLEIVNAQLKHAG 77

                         90       100
                 ....*....|....*....|....*
gi 675620728 240 KYTCIPSNSLGrSPSASAYLTVQYP 264
Cdd:cd04970   78 RYTCTAQTVVD-SDSASATLVVRGP 101
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 7-91 1.59e-05

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


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 43.92  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   7 EPEFVTARAGESVILGCDVihplTGQPPPyVVEWFKFGVPIPIfikfgfypphvdpeyaGRASLHDKASLRIEQVRSEDQ 86
Cdd:cd05725    3 RPQNQVVLVDDSAEFQCEV----GGDPVP-TVRWRKEDGELPK----------------GRYEILDDHSLKIRKVTAGDM 61


                 ....*
gi 675620728  87 GWYEC 91
Cdd:cd05725   62 GSYTC 66
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 175-261 1.90e-05

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


Pssm-ID: 409444  Cd Length: 105  Bit Score: 44.18  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 175 PENITVNISQDALFTCQ--AEAYPgNLTYLWYWEEENVYFKNDLKLRVRIL----IDGT------LIIFRVKPEDAGKYT 242
Cdd:cd05858    8 PANTSVVVGTDAEFVCKvySDAQP-HIQWLKHVEKNGSKYGPDGLPYVEVLktagVNTTdkeievLYLRNVTFEDAGEYT 86

                         90
                 ....*....|....*....
gi 675620728 243 CIPSNSLGRSpSASAYLTV 261
Cdd:cd05858   87 CLAGNSIGIS-HHSAWLTV 104
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 167-263 2.08e-05

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


Pssm-ID: 409435  Cd Length: 96  Bit Score: 43.78  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 167 GPPFIVSPPENITVNISQD--ALFTCQAEAYPgNLTYLWYWEEENVYFKNDLKLRvriLIDGTLIIFRV-KPEDAGKYTC 243
Cdd:cd05848    1 GPVFVQEPDDAIFPTDSDEkkVILNCEARGNP-VPTYRWLRNGTEIDTESDYRYS---LIDGNLIISNPsEVKDSGRYQC 76

                         90       100
                 ....*....|....*....|
gi 675620728 244 IPSNSLGRSPSASAYLTVQY 263
Cdd:cd05848   77 LATNSIGSILSREALLQFAY 96
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 6-93 3.08e-05

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: 43.85  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   6 EEPEFVTARAGESVILGCDVIH-PLTGQPPPYVVEWFK----FGVPIPIFIKFGF----YPphvdpEYAGRASLHDK--- 73
Cdd:cd05877    2 TVQAKVFSHRGGNVTLPCRYHYePELSAPRKIRVKWTKlevdYAKEEDVLVAIGTrhksYG-----SYQGRVFLRRAddl 76

                         90       100
                 ....*....|....*....|.
gi 675620728  74 -ASLRIEQVRSEDQGWYECKV 93
Cdd:cd05877   77 dASLVITDLRLEDYGRYRCEV 97
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 8-108 4.29e-05

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). 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), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; 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" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 43.59  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   8 PEFVTARAGESVILGCDVIHPLtgqpPPYV--VEWFKFGVP----IPIF-IKFGfypPHVDPEYAGRASLHDK------A 74
Cdd:cd05718    6 PTEVTGFLGGSVTLPCSLTSPG----TTKItqVTWMKIGAGssqnVAVFhPQYG---PSVPNPYAERVEFLAArlglrnA 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 675620728  75 SLRIEQVRSEDQGWYECkvlmldqQYDTFHNGSW 108
Cdd:cd05718   79 TLRIRNLRVEDEGNYIC-------EFATFPQGNR 105
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 177-261 5.89e-05

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 42.56  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 177 NITVNISQDALFTCQAEAYPgnltylwywEEENVYFKNDLKL----RVRILIDG----TLIIFRVKPEDAGKYTCIPSNS 248
Cdd:cd20973    6 DKEVVEGSAARFDCKVEGYP---------DPEVKWMKDDNPIvesrRFQIDQDEdglcSLIISDVCGDDSGKYTCKAVNS 76

                         90
                 ....*....|...
gi 675620728 249 LGRSpSASAYLTV 261
Cdd:cd20973   77 LGEA-TCSAELTV 88
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 16-93 6.30e-05

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 42.48  E-value: 6.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675620728  16 GESVILGCDVihplTGQPPPYVVEWFKFGVPIPIFikfgfYPPHVdpeYAGRASLHDKASLRIEQVRSEDQGWYECKV 93
Cdd:cd05734   16 GKAVVLNCSA----DGYPPPTIVWKHSKGSGVPQF-----QHIVP---LNGRIQLLSNGSLLIKHVLEEDSGYYLCKV 81
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 169-261 9.62e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 41.61  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  169 PFIVSPPenITVNISQDALFTCQAEAYPGnLTYLWYweeenvyfKNDLKLRVRilidGTLIIFRVKPEDAGKYTCIPSNS 248
Cdd:pfam13895   2 PVLTPSP--TVVTEGEPVTLTCSAPGNPP-PSYTWY--------KDGSAISSS----PNFFTLSVSAEDSGTYTCVARNG 66

                          90
                  ....*....|...
gi 675620728  249 LGRSPSASAYLTV 261
Cdd:pfam13895  67 RGGKVSNPVELTV 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 529-601 1.36e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.06  E-value: 1.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 675620728   529 PPRCLTA-NRTQQGVLLSWLPPA--NHSFPIDRYIMEFR-IAERWEILDDgiPGTENEFFAKDLSQDTWYEFRVLAV 601
Cdd:smart00060   3 PPSNLRVtDVTSTSVTLSWEPPPddGITGYIVGYRVEYReEGSEWKEVNV--TPSSTSYTLTGLKPGTEYEFRVRAV 77
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 167-263 1.53e-04

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: 41.46  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 167 GPPFIVSPPENI--TVNISQDALFTCQAEAYPGNlTYLWYWEEENVYFKNDLKLRvriLIDGTLIIFR-VKPEDAGKYTC 243
Cdd:cd04967    1 GPVFEEQPDDTIfpEDSDEKKVALNCRARANPVP-SYRWLMNGTEIDLESDYRYS---LVDGTLVISNpSKAKDAGHYQC 76

                         90       100
                 ....*....|....*....|
gi 675620728 244 IPSNSLGRSPSASAYLTVQY 263
Cdd:cd04967   77 LATNTVGSVLSREATLQFGY 96
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 175-261 1.57e-04

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


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 41.45  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 175 PENITVNISQDALFTCQAEAYPgnlTYLWYWEEEN-VYFKNDLKLRVRILI-DGTLIIFRVKPEDAGKYTCIPSNSLGrS 252
Cdd:cd05763    6 PHDITIRAGSTARLECAATGHP---TPQIAWQKDGgTDFPAARERRMHVMPeDDVFFIVDVKIEDTGVYSCTAQNSAG-S 81


                 ....*....
gi 675620728 253 PSASAYLTV 261
Cdd:cd05763   82 ISANATLTV 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 168-261 3.91e-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: 40.31  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIVSPPENITVNISQDALFTCQAEAYPGNlTYLWYWEEENVYFKNDlKLRVRILIdGTLIIFRVKPEDAGKYTCIPSN 247
Cdd:cd20976    1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVP-RITWIRNAQPLQYAAD-RSTCEAGV-GELHIQDVLPEDHGTYTCLAKN 77

                         90
                 ....*....|....
gi 675620728 248 SLGRSpSASAYLTV 261
Cdd:cd20976   78 AAGQV-SCSAWVTV 90
I-set pfam07679
Immunoglobulin I-set domain;
286-345 4.48e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 4.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675620728  286 CPVEAEPPVTlVKWNKDGRPLRIE-----KYSGwnllEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:pfam07679  22 CTVTGTPDPE-VSWFKDGQPLRSSdrfkvTYEG----GTYTLTISNVQPDDSGKYTCVATNSAGE 81
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 369-414 4.51e-04

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 39.79  E-value: 4.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 675620728 369 EYRQEAGRELLIPCAAAGDPFPIIAWRKVGKPSRSKH---NTLPGGTLQ 414
Cdd:cd20952    8 NQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDeriTTLENGSLQ 56
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 8-93 4.78e-04

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


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 39.82  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   8 PEFVTARAGESVILGCDVihplTGQPPpYVVEWFKFGVPIPifikfgfypphvdpeYAGRASLHDKASLRIEQVRSEDQG 87
Cdd:cd20957    8 PPVQTVDFGRTAVFNCSV----TGNPI-HTVLWMKDGKPLG---------------HSSRVQILSEDVLVIPSVKREDKG 67


                 ....*.
gi 675620728  88 WYECKV 93
Cdd:cd20957   68 MYQCFV 73
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 285-349 5.36e-04

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 39.84  E-value: 5.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 675620728 285 RCPVEAEPPVTlVKWNKDGRPLRIE-KYSGWNL-LEDGSIRIEEATEDALGTYTCVPYNALGTMGQS 349
Cdd:cd05857   25 RCPAAGNPTPT-MRWLKNGKEFKQEhRIGGYKVrNQHWSLIMESVVPSDKGNYTCVVENEYGSINHT 90
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 177-261 6.11e-04

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 39.80  E-value: 6.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 177 NITVNISQDALFTCQAEAYPGNLTYLWYWEEENVYFKNDLKLRVRILIDGT-LIIFRVKPEDAGKYTCIPSNSLGRSpSA 255
Cdd:cd05750    8 SQTVQEGSKLVLKCEATSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSeLQINKAKLEDSGEYTCVVENILGKD-TV 86


                 ....*.
gi 675620728 256 SAYLTV 261
Cdd:cd05750   87 TGNVTV 92
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 11-113 6.68e-04

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 39.47  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  11 VTARAGESVILGCDVI-HPLTGqpppyvVEWFKFGVPIPIfikfgfypPHvdpeyagRASLHDKASLRIEQV-RSEDQGW 88
Cdd:cd20958   10 LTAVAGQTLRLHCPVAgYPISS------ITWEKDGRRLPL--------NH-------RQRVFPNGTLVIENVqRSSDEGE 68

                         90       100
                 ....*....|....*....|....*
gi 675620728  89 YECKVlmLDQQyDTFHNGSwVHLTV 113
Cdd:cd20958   69 YTCTA--RNQQ-GQSASRS-VFVKV 89
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 170-250 7.67e-04

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


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 39.24  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 170 FIVSPpENITVNISQDALFTCQAEAYPG-NLTylWYWEEENVYFKNDLKLRVRILIDGtLIIFRVKPEDAGKYTCIPSNS 248
Cdd:cd20949    2 FTENA-YVTTVKEGQSATILCEVKGEPQpNVT--WHFNGQPISASVADMSKYRILADG-LLINKVTQDDTGEYTCRAYQV 77


                 ..
gi 675620728 249 LG 250
Cdd:cd20949   78 NS 79
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 284-345 8.84e-04

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 38.91  E-value: 8.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675620728 284 IRCPVEAEPPVTlVKWNKDGRPLriEKYSGWNLLEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:cd20978   21 LPCQVTGVPQPK-ITWLHNGKPL--QGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGD 79
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 293-349 8.89e-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: 39.16  E-value: 8.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 675620728 293 PVTLVKWNKDGRPLRIEKYSGWNLLEDGSIRIEEATEDALGTYTCVPYNALGTMGQS 349
Cdd:cd20976   29 PVPRITWIRNAQPLQYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCS 85
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 8-113 9.25e-04

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: 39.62  E-value: 9.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   8 PEFVTARAGESVILGCDVihplTGQPPPYVVEWF--KFGVPiPIFI-----KFGFYPPHVDPEYAGRASLHDKASLRIEQ 80
Cdd:cd00099    5 PRSLSVQEGESVTLSCEV----SSSFSSTYIYWYrqKPGQG-PEFLiylssSKGKTKGGVPGRFSGSRDGTSSFSLTISN 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 675620728  81 VRSEDQGWYECkVLMLDQQYDTFHNGSWVHLTV 113
Cdd:cd00099   80 LQPEDSGTYYC-AVSESGGTDKLTFGSGTRLTV 111
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 177-261 1.02e-03

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: 39.14  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 177 NITVNISQDALFTCQAEAYPgNLTYLW------YWEEENVYFKNDlklrvriliDGT-LIIFRVKPEDAGKYTCIPSNSL 249
Cdd:cd05730   12 NATANLGQSVTLACDADGFP-EPTMTWtkdgepIESGEEKYSFNE---------DGSeMTILDVDKLDEAEYTCIAENKA 81

                         90
                 ....*....|..
gi 675620728 250 GRSpSASAYLTV 261
Cdd:cd05730   82 GEQ-EAEIHLKV 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 5-93 1.06e-03

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


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 38.92  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   5 REEPEFVTARAGESVILGCDvihPLTGQPPPyVVEWFKFGVPIPIfikfgfypphVDPeyaGRASLHDkASLRIEQVRSE 84
Cdd:cd05724    1 RVEPSDTQVAVGEMAVLECS---PPRGHPEP-TVSWRKDGQPLNL----------DNE---RVRIVDD-GNLLIAEARKS 62


                 ....*....
gi 675620728  85 DQGWYECKV 93
Cdd:cd05724   63 DEGTYKCVA 71
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 169-250 1.09e-03

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


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 39.07  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 169 PFIVSPPENITVNISQDALFTCQAEAYPG-NLTylwyWE-----EENVYFK-NDLKLRVRILIDGTLIIFRVKPEDAGKY 241
Cdd:cd05765    1 PALVNSPTHQTVKVGETASFHCDVTGRPQpEIT----WEkqvpgKENLIMRpNHVRGNVVVTNIGQLVIYNAQPQDAGLY 76


                 ....*....
gi 675620728 242 TCIPSNSLG 250
Cdd:cd05765   77 TCTARNSGG 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 359-414 1.22e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.32  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 675620728  359 PPYFTVLPGWEYRQEaGRELLIPCAAAGDPFPIIAWRKVGKP-----SRSKHNTLPGGTLQ 414
Cdd:pfam13927   1 KPVITVSPSSVTVRE-GETVTLTCEATGSPPPTITWYKNGEPissgsTRSRSLSGSNSTLT 60
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 266-345 1.25e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 39.07  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 266 RVVNMPPVIYIPIGIHGYIRCPVEAEPPVTlVKWNKDGRPLRIEKY---SGWNLLEDGSI--------RIEEATEdalGT 334
Cdd:cd07693    2 RIVEHPSDLIVSKGDPATLNCKAEGRPTPT-IQWLKNGQPLETDKDdprSHRIVLPSGSLfflrvvhgRKGRSDE---GV 77

                         90
                 ....*....|.
gi 675620728 335 YTCVPYNALGT 345
Cdd:cd07693   78 YVCVAHNSLGE 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 271-341 1.29e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.32  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675620728  271 PPVIYIP-------IGIHGYIRCPVEAEPPVTlVKWNKDGRPLRIEKYSGWNLLED-GSIRIEEATEDALGTYTCVPYN 341
Cdd:pfam13927   1 KPVITVSpssvtvrEGETVTLTCEATGSPPPT-ITWYKNGEPISSGSTRSRSLSGSnSTLTISNVTRSDAGTYTCVASN 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 227-250 1.46e-03

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: 38.74  E-value: 1.46e-03
                         10        20
                 ....*....|....*....|....
gi 675620728 227 TLIIFRVKPEDAGKYTCIPSNSLG 250
Cdd:cd05729   62 SLIIERAIPRDKGKYTCIVENEYG 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 284-345 1.60e-03

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: 38.26  E-value: 1.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675620728   284 IRCPVEAEPPVTlVKWNKDGRPLRIEK--YSGWNLLEDGSIRIEEAT-EDAlGTYTCVPYNALGT 345
Cdd:smart00410  14 LSCEASGSPPPE-VTWYKQGGKLLAESgrFSVSRSGSTSTLTISNVTpEDS-GTYTCAATNSSGS 76
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 118-147 1.77e-03

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 37.96  E-value: 1.77e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 675620728 118 CMAFGNPKPIVTWLREGDLLGANGKYQVGG 147
Cdd:cd05728   21 CKASGNPRPAYRWLKNGQPLASENRIEVEA 50
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 173-264 2.33e-03

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 37.82  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 173 SPPENITVNISQDALFTCQAEAYPGNLTYLWYWEEENVYFKNDLKLRVriliDGTLIIFRVKPEDAGKYTCIPSNSLGRS 252
Cdd:cd04979    1 TSFKQISVKEGDTVILSCSVKSNNAPVTWIHNGKKVPRYRSPRLVLKT----ERGLLIRSAQEADAGVYECHSGERVLGS 76

                         90
                 ....*....|..
gi 675620728 253 PSASAYLTVQYP 264
Cdd:cd04979   77 TLRSVTLHVLER 88
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
 169-261 2.60e-03

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. 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. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 37.76  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 169 PFIVSPPENiTVNISQDALFTCqaEAYPGNLTYLWyweeenvyFKNDLKLRV--RILIDG---TLIIFRVKPEDAGKYTC 243
Cdd:cd05740    2 PFISSNNSN-PVEDKDAVTLTC--EPETQNTSYLW--------WFNGQSLPVtpRLTLSNgnrTLTLLNVTREDAGAYQC 70

                         90
                 ....*....|....*...
gi 675620728 244 IPSNSLGRSPSASAYLTV 261
Cdd:cd05740   71 EISNPVSANRSDPVTLDV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 266-355 2.81e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 37.37  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  266 RVVNMPPVIYIPIGIHGYIRCPVEAEPPVTlVKWNKDGRPLRiekysgwnllEDGSIRIEEATEDALGTYTCVPYNAlGT 345
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSAPGNPPPS-YTWYKDGSAIS----------SSPNFFTLSVSAEDSGTYTCVARNG-RG 68

                          90
                  ....*....|
gi 675620728  346 MGQSPPARLV 355
Cdd:pfam13895  69 GKVSNPVELT 78
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 6-113 3.39e-03

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: 37.82  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728    6 EEPEFVTARAGESVILGCDVihPLTGQPPPYVVEWFK---FGVPIPIFIKFGF-YPPHVDPE-YAGRA--SLHDkASLRI 78
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTY--SSSMSEASTSVYWYRqppGKGPTFLIAYYSNgSEEGVKKGrFSGRGdpSNGD-GSLTI 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 675620728   79 EQVRSEDQGWYECKVlmLDQQYDTFHNGswVHLTV 113
Cdd:pfam07686  78 QNLTLSDSGTYTCAV--IPSGEGVFGKG--TRLTV 108
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 15-93 4.39e-03

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 37.75  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728  15 AGESVILGC----DVIHPLTGQP-PPYVVEWFKFGVPIPIFIkfgFY--PPHV---DPEYAGRASL------HDKASLRI 78
Cdd:cd16091    1 AVSEVIVVCllseDCILPCSFTPgSEVVIHWYKQDSDIKVHS---YYygKDQLesqDQRYRNRTSLfkdqisNGNASLLL 77

                         90
                 ....*....|....*
gi 675620728  79 EQVRSEDQGWYECKV 93
Cdd:cd16091   78 RRVQLQDEGRYKCYT 92
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 270-346 4.44e-03

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: 37.20  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 270 MPPVIYIPIGIHGYIRCPVEAEPPVTlVKWNKDGRPL----RIEKY----SGWNLLedgsirIEEATEDALGTYTCVPYN 341
Cdd:cd05729   10 EEREHALPAANKVRLECGAGGNPMPN-ITWLKDGKEFkkehRIGGTkveeKGWSLI------IERAIPRDKGKYTCIVEN 82


                 ....*
gi 675620728 342 ALGTM 346
Cdd:cd05729   83 EYGSI 87
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 167-263 4.51e-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: 37.21  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 167 GPPFIVSP-----PENITvniSQDALFTCQAEAYPGnLTYLWYWEEENVYFKNDLKLRvriLIDGTLIIFR-VKPEDAGK 240
Cdd:cd05850    2 GPVFEEQPsstlfPEGSA---EEKVTLACRARASPP-ATYRWKMNGTELKMEPDSRYR---LVAGNLVISNpVKAKDAGS 74

                         90       100
                 ....*....|....*....|...
gi 675620728 241 YTCIPSNSLGRSPSASAYLTVQY 263
Cdd:cd05850   75 YQCLASNRRGTVVSREASLRFGF 97
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 172-249 4.63e-03

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409412  Cd Length: 85  Bit Score: 36.77  E-value: 4.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675620728 172 VSPPENITVNISQDALFTCQAEAYPGNLTYLWYweeenvyfKNDLKLRVRIL-IDGTLIIFRVKPEDAGKYTCIPSNSL 249
Cdd:cd05754    5 VEEPRSQEVRPGADVSFICRAKSKSPAYTLVWT--------RVNGTLPSRAMdFNGILTIRNVQLSDAGTYVCTGSNML 75
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 284-345 5.02e-03

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 37.05  E-value: 5.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675620728 284 IRCPVEAEPPVTlVKWNKDGRPLRIEKYSgwNLLEDGSIRIEEATEDALGTYTCVPYNALGT 345
Cdd:cd04969   22 IECKPKASPKPT-ISWSKGTELLTNSSRI--CILPDGSLKIKNVTKSDEGKYTCFAVNFFGK 80
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 5-91 6.18e-03

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 36.99  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   5 REEPEFVTARAGESVILGCDVihpltgqPPPYVVE---WFKFG--VPIPIFIKFGFYPPhvdpeyaGRASLHDKA----- 74
Cdd:cd05716    1 SVGPEVVTGVEGGSVTIQCPY-------PPKYASSrkyWCKWGseGCQTLVSSEGVVPG-------GRISLTDDPdngvf 66

                         90
                 ....*....|....*..
gi 675620728  75 SLRIEQVRSEDQGWYEC 91
Cdd:cd05716   67 TVTLNQLRKEDAGWYWC 83
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 170-261 6.52e-03

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: 36.66  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 170 FIVSPPENITVNISQDALFTCQAEAYPgNLTYLWyweEENVYFKNDLKLRVRILIDGTLIIFR-VKPEDAGKYTCIPSNS 248
Cdd:cd04978    1 YWIIEPPSLVLSPGETGELICEAEGNP-QPTITW---RLNGVPIEPAPEDMRRTVDGRTLIFSnLQPNDTAVYQCNASNV 76

                         90
                 ....*....|...
gi 675620728 249 LGRSpSASAYLTV 261
Cdd:cd04978   77 HGYL-LANAFLHV 88
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 168-261 7.34e-03

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 36.41  E-value: 7.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728 168 PPFIVSPPENITVNISQDALFTCQAEaypGNLTYLWYWEEENVYFKNDLKlrVRILIDG---TLIIFRVKPEDAGKYTCI 244
Cdd:cd20972    1 PPQFIQKLRSQEVAEGSKVRLECRVT---GNPTPVVRWFCEGKELQNSPD--IQIHQEGdlhSLIIAEAFEEDTGRYSCL 75

                         90
                 ....*....|....*..
gi 675620728 245 PSNSLGRSpSASAYLTV 261
Cdd:cd20972   76 ATNSVGSD-TTSAEIFV 91
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 8-112 8.24e-03

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, 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, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 36.98  E-value: 8.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675620728   8 PEFVTARAGESVILGCDVIHPLTGQPPPYV-VEWFkFGVPIPifikfGFYPP--------HVDPEYAGRASL-----HDK 73
Cdd:cd05712    6 PKSVTVQEGLCVLIPCSFSYPADYWVSNPVhGYWY-RGGPYP-----KYRPPvatnnrtrEVHESTQGRFRLlgdpgKKN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 675620728  74 ASLRIEQVRSEDQGWYECKV-LMLDQQYDTFHNGSWVHLT 112
Cdd:cd05712   80 CSLSISDARPEDSGKYFFRVeRGDSNKYSYLSNQLSLTVT 119
 
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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