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Conserved domains on  [gi|1804387592|ref|XP_032149168|]
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myomesin-1 isoform X1 [Sapajus apella]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1572-1663 9.27e-50

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 cd05737:

Pssm-ID: 472250  Cd Length: 92  Bit Score: 171.23  E-value: 9.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1572 ARVLGGLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNK 1651
Cdd:cd05737      1 ARVLGGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNK 80

                           90
                   ....*....|..
gi 1804387592 1652 YGSETSDFTISV 1663
Cdd:cd05737     81 YGSETSDVTVSV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 277-370 3.42e-49

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


:

Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 169.52  E-value: 3.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMN 356
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80

                           90
                   ....*....|....
gi 1804387592  357 VKGELSAYASVVVK 370
Cdd:cd20951     81 IHGEASSSASVVVE 94
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
571-857 9.88e-30

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 127.04  E-value: 9.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  571 VTGLIEGRSYIFRVRAVNKTGIGFPSRVSEPVAALDPaekarlksrpsapwtgqiivteeepsegivPGPPTDLSVTEAT 650
Cdd:COG3401    196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP------------------------------PSAPTGLTATADT 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  651 RSYVVLSWKPPGQRGHEGimYFVEKCEAGTENWQRVNTelpVKSPRFALFDLVEGKSYCFRVRCSNSAGV-GEPSEATEV 729
Cdd:COG3401    246 PGSVTLSWDPVTESDATG--YRVYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSV 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  730 TVvgdKLDIPKAPGNIIPSRNTDTSVVVTWEESKDAKeLVGYYIEASVAGSGKWEPCNNnPVKGSRFTCHGLVTGQSYIF 809
Cdd:COG3401    321 TT---DLTPPAAPSGLTATAVGSSSITLSWTASSDAD-VTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYY 395

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1804387592  810 RVRAVNAAGL-SEYSRDSEAIEVKAAIGGGVSPDVCPALSDEPGGLTAS 857
Cdd:COG3401    396 KVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1039-1128 1.89e-19

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: 84.86  E-value: 1.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1039 PGPPHSLKYSEVRKDSLVLHWKPPIHSGRtPVTGYFVDLKEAqaKEDQWRGLNEAAIKTLYLKVRGLKEGISYVFRVRAI 1118
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREK--GSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|
gi 1804387592 1119 NQAGVGKPSD 1128
Cdd:cd00063     78 NGGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 510-600 3.52e-19

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: 84.09  E-value: 3.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  510 PAAPLDVKCLEANKDYIIISWKQPAvDGGSPILGYFIDKCEVGTDSWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNK 589
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|.
gi 1804387592  590 TGIGFPSRVSE 600
Cdd:cd00063     80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 934-1028 3.69e-17

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: 78.31  E-value: 3.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  934 PSPPYDITCLESFRDSMVLGWKQPDKIGGaEITGYYVNYREVIGGvpgKWREANVKAVSEEAYKISNLKENVVYQFQVAA 1013
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSG---DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                           90
                   ....*....|....*
gi 1804387592 1014 MNMAGLGAPSAVSEC 1028
Cdd:cd00063     77 VNGGGESPPSESVTV 91
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 417-484 7.39e-12

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


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 7.39e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  417 REGETMSLGCRVVITPEikhfqPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRV 484
Cdd:pfam07679   13 QEGESARFTCTVTGTPD-----PEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVA 75
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1374-1443 3.01e-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.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 46.87  E-value: 3.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804387592 1374 VLLKCKVANiKKETHIVWYKDEREISVDEKH--DFKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKL 1443
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRFkvTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1155-1210 1.31e-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 pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 1.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1804387592 1155 SLNFECD-QMTPKSEFTWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGLYSC 1210
Cdd:pfam07679   17 SARFTCTvTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
 
Name Accession Description Interval E-value
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 1572-1663 9.27e-50

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 171.23  E-value: 9.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1572 ARVLGGLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNK 1651
Cdd:cd05737      1 ARVLGGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNK 80

                           90
                   ....*....|..
gi 1804387592 1652 YGSETSDFTISV 1663
Cdd:cd05737     81 YGSETSDVTVSV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 277-370 3.42e-49

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 169.52  E-value: 3.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMN 356
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80

                           90
                   ....*....|....
gi 1804387592  357 VKGELSAYASVVVK 370
Cdd:cd20951     81 IHGEASSSASVVVE 94
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
571-857 9.88e-30

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 127.04  E-value: 9.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  571 VTGLIEGRSYIFRVRAVNKTGIGFPSRVSEPVAALDPaekarlksrpsapwtgqiivteeepsegivPGPPTDLSVTEAT 650
Cdd:COG3401    196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP------------------------------PSAPTGLTATADT 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  651 RSYVVLSWKPPGQRGHEGimYFVEKCEAGTENWQRVNTelpVKSPRFALFDLVEGKSYCFRVRCSNSAGV-GEPSEATEV 729
Cdd:COG3401    246 PGSVTLSWDPVTESDATG--YRVYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSV 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  730 TVvgdKLDIPKAPGNIIPSRNTDTSVVVTWEESKDAKeLVGYYIEASVAGSGKWEPCNNnPVKGSRFTCHGLVTGQSYIF 809
Cdd:COG3401    321 TT---DLTPPAAPSGLTATAVGSSSITLSWTASSDAD-VTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYY 395

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1804387592  810 RVRAVNAAGL-SEYSRDSEAIEVKAAIGGGVSPDVCPALSDEPGGLTAS 857
Cdd:COG3401    396 KVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444
I-set pfam07679
Immunoglobulin I-set domain;
1579-1663 1.89e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 95.79  E-value: 1.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEaGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSD 1658
Cdd:pfam07679    7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYE-GGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85


                   ....*
gi 1804387592 1659 FTISV 1663
Cdd:pfam07679   86 AELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 638-731 5.79e-22

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: 91.79  E-value: 5.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  638 PGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCEAGTENWQRVNTElPVKSPRFALFDLVEGKSYCFRVRCSNS 717
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVT-PGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1804387592  718 AGVGEPSEATEVTV 731
Cdd:cd00063     80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1039-1128 1.89e-19

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: 84.86  E-value: 1.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1039 PGPPHSLKYSEVRKDSLVLHWKPPIHSGRtPVTGYFVDLKEAqaKEDQWRGLNEAAIKTLYLKVRGLKEGISYVFRVRAI 1118
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREK--GSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|
gi 1804387592 1119 NQAGVGKPSD 1128
Cdd:cd00063     78 NGGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 510-600 3.52e-19

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: 84.09  E-value: 3.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  510 PAAPLDVKCLEANKDYIIISWKQPAvDGGSPILGYFIDKCEVGTDSWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNK 589
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|.
gi 1804387592  590 TGIGFPSRVSE 600
Cdd:cd00063     80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 934-1028 3.69e-17

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: 78.31  E-value: 3.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  934 PSPPYDITCLESFRDSMVLGWKQPDKIGGaEITGYYVNYREVIGGvpgKWREANVKAVSEEAYKISNLKENVVYQFQVAA 1013
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSG---DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                           90
                   ....*....|....*
gi 1804387592 1014 MNMAGLGAPSAVSEC 1028
Cdd:cd00063     77 VNGGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 638-721 6.22e-16

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: 74.19  E-value: 6.22e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   638 PGPPTDLSVTEATRSYVVLSWKPPGQRGHEG--IMYFVEKCEAGtENWQRVNTelPVKSPRFALFDLVEGKSYCFRVRCS 715
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyiVGYRVEYREEG-SEWKEVNV--TPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1804387592   716 NSAGVG 721
Cdd:smart00060   78 NGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
920-1137 1.98e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 81.59  E-value: 1.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  920 SKSHPLKKKTDRAPPSPPYDITCLESFRDSMVLGWkqpDKIGGAEITGYYVnYREVIGGvpGKWREanVKAVSEEAYKIS 999
Cdd:COG3401    219 APSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW---DPVTESDATGYRV-YRSNSGD--GPFTK--VATVTTTSYTDT 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1000 NLKENVVYQFQVAAMNMAGL-GAPSAVSECFKCeewtIAVPGPPHSLKYSEVRKDSLVLHWKPPihSGrTPVTGYFVdlK 1078
Cdd:COG3401    291 GLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTD----LTPPAAPSGLTATAVGSSSITLSWTAS--SD-ADVTGYNV--Y 361

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592 1079 EAQAKEDQWRGLNEAAIKTLYlKVRGLKEGISYVFRVRAINQAGVGkpSDLAGPVVAET 1137
Cdd:COG3401    362 RSTSGGGTYTKIAETVTTTSY-TDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATT 417
fn3 pfam00041
Fibronectin type III domain;
1040-1127 6.39e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 71.29  E-value: 6.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1040 GPPHSLKYSEVRKDSLVLHWKPPiHSGRTPVTGYFVDLKEAQaKEDQWRGLNEAAIKTLYlKVRGLKEGISYVFRVRAIN 1119
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSV-TLTGLKPGTEYEVRVQAVN 77


                   ....*...
gi 1804387592 1120 QAGVGKPS 1127
Cdd:pfam00041   78 GGGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 284-369 9.31e-15

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: 71.00  E-value: 9.31e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   284 RSHTVWEKENVKLHCSVAGWPEPRVTWYKNqvPINVHANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMNVKGELSA 363
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQ--GGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ....*.
gi 1804387592   364 YASVVV 369
Cdd:smart00410   80 GTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1039-1124 1.60e-14

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: 70.34  E-value: 1.60e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  1039 PGPPHSLKYSEVRKDSLVLHWKPPIHSGRT-PVTGYFVDLKEaqaKEDQWRGLNEAAIKTLYlKVRGLKEGISYVFRVRA 1117
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYRE---EGSEWKEVNVTPSSTSY-TLTGLKPGTEYEFRVRA 76


                    ....*..
gi 1804387592  1118 INQAGVG 1124
Cdd:smart00060   77 VNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 510-593 1.69e-14

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: 70.34  E-value: 1.69e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   510 PAAPLDVKCLEANKDYIIISWKQPAVDGG-SPILGYFIDKCEVGtDSWSQCNDTPVKFaRFPVTGLIEGRSYIFRVRAVN 588
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1804387592   589 KTGIG 593
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
512-596 3.69e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  512 APLDVKCLEANKDYIIISWkQPAVDGGSPILGYFIDKCEVGT-DSWSQCNDTPVKFaRFPVTGLIEGRSYIFRVRAVNKT 590
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSgEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1804387592  591 GIGFPS 596
Cdd:pfam00041   80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1579-1663 4.88e-14

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: 69.07  E-value: 4.88e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKN-EKALASDDHCTLKFEaGKTAYFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQgGKLLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ....*.
gi 1804387592  1658 DFTISV 1663
Cdd:smart00410   80 GTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
277-369 1.35e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINvhaNPGKYIIESRYGMHTLEINACDFEDTAQYRASAMN 356
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR---SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 1804387592  357 VKGELSAYASVVV 369
Cdd:pfam07679   78 SAGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 934-1020 1.61e-12

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: 64.56  E-value: 1.61e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   934 PSPPYDITCLESFRDSMVLGWKQPDKIGGaeiTGYYVNYREVIGGVPGKWREANVKaVSEEAYKISNLKENVVYQFQVAA 1013
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYRVEYREEGSEWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*..
gi 1804387592  1014 MNMAGLG 1020
Cdd:smart00060   77 VNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
935-1023 2.11e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 2.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  935 SPPYDITCLESFRDSMVLGWKQPDKiGGAEITGYYVNYREVigGVPGKWREANVKAvSEEAYKISNLKENVVYQFQVAAM 1014
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPK--NSGEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 1804387592 1015 NMAGLGAPS 1023
Cdd:pfam00041   77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
417-484 7.39e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 7.39e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  417 REGETMSLGCRVVITPEikhfqPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRV 484
Cdd:pfam07679   13 QEGESARFTCTVTGTPD-----PEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVA 75
fn3 pfam00041
Fibronectin type III domain;
741-823 8.94e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 8.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  741 APGNIIPSRNTDTSVVVTWEESKDAK-ELVGYYIEASVAGSGkwEPCNNNPVKGSRFTC--HGLVTGQSYIFRVRAVNAA 817
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSG--EPWNEITVPGTTTSVtlTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1804387592  818 GLSEYS 823
Cdd:pfam00041   80 GEGPPS 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 423-485 2.39e-08

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 52.33  E-value: 2.39e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1804387592  423 SLGCRVVITPEikhfqPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVR 485
Cdd:cd00096      2 TLTCSASGNPP-----PTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 416-499 6.00e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.74  E-value: 6.00e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   416 GREGETMSLGCRVVITPEikhfqPEIQWYRNG-VPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVRMGEYYEQYS 494
Cdd:smart00410    6 VKEGESVTLSCEASGSPP-----PEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1804387592   495 AYVFV 499
Cdd:smart00410   81 TTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
987-1137 2.85e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.39  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  987 NVKAVSEEAYKISNLKENVVYQFQVAAMNMAGLGAPSAVSECFkceeWTIAVPGPPHSLKYSEVRKDSLVLHWKPPIHSG 1066
Cdd:COG3401    185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVT----TPTTPPSAPTGLTATADTPGSVTLSWDPVTESD 260

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804387592 1067 rtpVTGYFVdlKEAQAKEDQWRGLneAAIKTLYLKVRGLKEGISYVFRVRAINQAGVgkPSDLAGPVVAET 1137
Cdd:COG3401    261 ---ATGYRV--YRSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTT 322
I-set pfam07679
Immunoglobulin I-set domain;
1374-1443 3.01e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 46.87  E-value: 3.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804387592 1374 VLLKCKVANiKKETHIVWYKDEREISVDEKH--DFKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKL 1443
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRFkvTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
 1378-1443 1.43e-05

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin 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-M1 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: 409521  Cd Length: 90  Bit Score: 45.03  E-value: 1.43e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592 1378 CKVANIKKETHIVWYKDEREISVDEKHD--FKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKL 1443
Cdd:cd20927     21 CKIENYDQSTQVTWYFGVRQLENSEKYEitYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAEL 88
I-set pfam07679
Immunoglobulin I-set domain;
1155-1210 1.31e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 1.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1804387592 1155 SLNFECD-QMTPKSEFTWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGLYSC 1210
Cdd:pfam07679   17 SARFTCTvTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
440-592 1.60e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.48  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  440 EIQWYRNGvplspSKWVQTlwsgERATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVrdADAEIEGAPAAPLDVKCL 519
Cdd:COG4733    568 EVEWRRDD-----GNWVSV----PRTSGTSFEVPGIYAGDYEVRVRAINALGVSSAWAAS--SETTVTGKTAPPPAPTGL 636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  520 EANKDY--IIISWKQPAvdgGSPILGYfidkcEV---GTDSW--SQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKTGI 592
Cdd:COG4733    637 TATGGLggITLSWSFPV---DADTLRT-----EIrysTTGDWasATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGN 708
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 1162-1221 1.26e-03

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


Pssm-ID: 143223  Cd Length: 69  Bit Score: 39.09  E-value: 1.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1162 QMTPKSEFTWSKDYVSTEDSPRLEVESKGNktkMTFKDLGMDDLGLYSCDVIDTDGIASS 1221
Cdd:cd05746      8 QGDPEPTITWNKDGVQVTESGKFHISPEGY---LAIRDVGVADQGRYECVARNTIGYASV 64
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1155-1221 1.30e-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: 39.41  E-value: 1.30e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592  1155 SLNFECD-QMTPKSEFTWSKDYVST-EDSPRLEVESKGNKTKMTFKDLGMDDLGLYSCDVIDTDGIASS 1221
Cdd:smart00410   11 SVTLSCEaSGSPPPEVTWYKQGGKLlAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1373-1443 2.66e-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: 38.64  E-value: 2.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804387592  1373 NVLLKCKVANiKKETHIVWYKDEREIsVDEKHDFK----DGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKL 1443
Cdd:smart00410   11 SVTLSCEASG-SPPPEVTWYKQGGKL-LAESGRFSvsrsGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
 
Name Accession Description Interval E-value
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 1572-1663 9.27e-50

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 171.23  E-value: 9.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1572 ARVLGGLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNK 1651
Cdd:cd05737      1 ARVLGGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTVYFTINGVSSEDSGKYGLVVKNK 80

                           90
                   ....*....|..
gi 1804387592 1652 YGSETSDFTISV 1663
Cdd:cd05737     81 YGSETSDVTVSV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 277-370 3.42e-49

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 169.52  E-value: 3.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMN 356
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80

                           90
                   ....*....|....
gi 1804387592  357 VKGELSAYASVVVK 370
Cdd:cd20951     81 IHGEASSSASVVVE 94
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 1573-1663 2.50e-34

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 126.95  E-value: 2.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1573 RVLGGLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKY 1652
Cdd:cd05891      2 KVIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQGKYASLTIKGVTSEDSGKYSINVKNKY 81

                           90
                   ....*....|.
gi 1804387592 1653 GSETSDFTISV 1663
Cdd:cd05891     82 GGETVDVTVSV 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
571-857 9.88e-30

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 127.04  E-value: 9.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  571 VTGLIEGRSYIFRVRAVNKTGIGFPSRVSEPVAALDPaekarlksrpsapwtgqiivteeepsegivPGPPTDLSVTEAT 650
Cdd:COG3401    196 GGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTP------------------------------PSAPTGLTATADT 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  651 RSYVVLSWKPPGQRGHEGimYFVEKCEAGTENWQRVNTelpVKSPRFALFDLVEGKSYCFRVRCSNSAGV-GEPSEATEV 729
Cdd:COG3401    246 PGSVTLSWDPVTESDATG--YRVYRSNSGDGPFTKVAT---VTTTSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSV 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  730 TVvgdKLDIPKAPGNIIPSRNTDTSVVVTWEESKDAKeLVGYYIEASVAGSGKWEPCNNnPVKGSRFTCHGLVTGQSYIF 809
Cdd:COG3401    321 TT---DLTPPAAPSGLTATAVGSSSITLSWTASSDAD-VTGYNVYRSTSGGGTYTKIAE-TVTTTSYTDTGLTPGTTYYY 395

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1804387592  810 RVRAVNAAGL-SEYSRDSEAIEVKAAIGGGVSPDVCPALSDEPGGLTAS 857
Cdd:COG3401    396 KVTAVDAAGNeSAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444
I-set pfam07679
Immunoglobulin I-set domain;
1579-1663 1.89e-23

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 95.79  E-value: 1.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEaGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSD 1658
Cdd:pfam07679    7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYE-GGTYTLTISNVQPDDSGKYTCVATNSAGEAEAS 85


                   ....*
gi 1804387592 1659 FTISV 1663
Cdd:pfam07679   86 AELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 638-731 5.79e-22

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: 91.79  E-value: 5.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  638 PGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCEAGTENWQRVNTElPVKSPRFALFDLVEGKSYCFRVRCSNS 717
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVT-PGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1804387592  718 AGVGEPSEATEVTV 731
Cdd:cd00063     80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1039-1128 1.89e-19

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: 84.86  E-value: 1.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1039 PGPPHSLKYSEVRKDSLVLHWKPPIHSGRtPVTGYFVDLKEAqaKEDQWRGLNEAAIKTLYLKVRGLKEGISYVFRVRAI 1118
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREK--GSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|
gi 1804387592 1119 NQAGVGKPSD 1128
Cdd:cd00063     78 NGGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 510-600 3.52e-19

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: 84.09  E-value: 3.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  510 PAAPLDVKCLEANKDYIIISWKQPAvDGGSPILGYFIDKCEVGTDSWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNK 589
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|.
gi 1804387592  590 TGIGFPSRVSE 600
Cdd:cd00063     80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 739-829 2.47e-18

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: 81.39  E-value: 2.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  739 PKAPGNIIPSRNTDTSVVVTWEESK-DAKELVGYYIEASVAGSGKWEPCNNNPVKGSRFTCHGLVTGQSYIFRVRAVNAA 817
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEdDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1804387592  818 GLSEYSRDSEAI 829
Cdd:cd00063     81 GESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 934-1028 3.69e-17

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: 78.31  E-value: 3.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  934 PSPPYDITCLESFRDSMVLGWKQPDKIGGaEITGYYVNYREVIGGvpgKWREANVKAVSEEAYKISNLKENVVYQFQVAA 1013
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSG---DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

                           90
                   ....*....|....*
gi 1804387592 1014 MNMAGLGAPSAVSEC 1028
Cdd:cd00063     77 VNGGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 638-721 6.22e-16

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: 74.19  E-value: 6.22e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   638 PGPPTDLSVTEATRSYVVLSWKPPGQRGHEG--IMYFVEKCEAGtENWQRVNTelPVKSPRFALFDLVEGKSYCFRVRCS 715
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyiVGYRVEYREEG-SEWKEVNV--TPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1804387592   716 NSAGVG 721
Cdd:smart00060   78 NGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
920-1137 1.98e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 81.59  E-value: 1.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  920 SKSHPLKKKTDRAPPSPPYDITCLESFRDSMVLGWkqpDKIGGAEITGYYVnYREVIGGvpGKWREanVKAVSEEAYKIS 999
Cdd:COG3401    219 APSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSW---DPVTESDATGYRV-YRSNSGD--GPFTK--VATVTTTSYTDT 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1000 NLKENVVYQFQVAAMNMAGL-GAPSAVSECFKCeewtIAVPGPPHSLKYSEVRKDSLVLHWKPPihSGrTPVTGYFVdlK 1078
Cdd:COG3401    291 GLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTD----LTPPAAPSGLTATAVGSSSITLSWTAS--SD-ADVTGYNV--Y 361

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592 1079 EAQAKEDQWRGLNEAAIKTLYlKVRGLKEGISYVFRVRAINQAGVGkpSDLAGPVVAET 1137
Cdd:COG3401    362 RSTSGGGTYTKIAETVTTTSY-TDTGLTPGTTYYYKVTAVDAAGNE--SAPSEEVSATT 417
fn3 pfam00041
Fibronectin type III domain;
1040-1127 6.39e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 71.29  E-value: 6.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1040 GPPHSLKYSEVRKDSLVLHWKPPiHSGRTPVTGYFVDLKEAQaKEDQWRGLNEAAIKTLYlKVRGLKEGISYVFRVRAIN 1119
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSV-TLTGLKPGTEYEVRVQAVN 77


                   ....*...
gi 1804387592 1120 QAGVGKPS 1127
Cdd:pfam00041   78 GGGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 284-369 9.31e-15

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: 71.00  E-value: 9.31e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   284 RSHTVWEKENVKLHCSVAGWPEPRVTWYKNqvPINVHANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMNVKGELSA 363
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQ--GGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ....*.
gi 1804387592   364 YASVVV 369
Cdd:smart00410   80 GTTLTV 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1039-1124 1.60e-14

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: 70.34  E-value: 1.60e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  1039 PGPPHSLKYSEVRKDSLVLHWKPPIHSGRT-PVTGYFVDLKEaqaKEDQWRGLNEAAIKTLYlKVRGLKEGISYVFRVRA 1117
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYRE---EGSEWKEVNVTPSSTSY-TLTGLKPGTEYEFRVRA 76


                    ....*..
gi 1804387592  1118 INQAGVG 1124
Cdd:smart00060   77 VNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 510-593 1.69e-14

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: 70.34  E-value: 1.69e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   510 PAAPLDVKCLEANKDYIIISWKQPAVDGG-SPILGYFIDKCEVGtDSWSQCNDTPVKFaRFPVTGLIEGRSYIFRVRAVN 588
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItGYIVGYRVEYREEG-SEWKEVNVTPSST-SYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1804387592   589 KTGIG 593
Cdd:smart00060   79 GAGEG 83
fn3 pfam00041
Fibronectin type III domain;
512-596 3.69e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 3.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  512 APLDVKCLEANKDYIIISWkQPAVDGGSPILGYFIDKCEVGT-DSWSQCNDTPVKFaRFPVTGLIEGRSYIFRVRAVNKT 590
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSW-TPPPDGNGPITGYEVEYRPKNSgEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1804387592  591 GIGFPS 596
Cdd:pfam00041   80 GEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1579-1663 4.88e-14

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: 69.07  E-value: 4.88e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKN-EKALASDDHCTLKFEaGKTAYFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQgGKLLAESGRFSVSRS-GSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ....*.
gi 1804387592  1658 DFTISV 1663
Cdd:smart00410   80 GTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
277-369 1.35e-13

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.05  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINvhaNPGKYIIESRYGMHTLEINACDFEDTAQYRASAMN 356
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR---SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATN 77

                           90
                   ....*....|...
gi 1804387592  357 VKGELSAYASVVV 369
Cdd:pfam07679   78 SAGEAEASAELTV 90
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 739-820 1.53e-12

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: 64.56  E-value: 1.53e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   739 PKAPGNIIPSRNTDTSVVVTWEESKDA---KELVGYYIEaSVAGSGKWEPCNNNPVKgSRFTCHGLVTGQSYIFRVRAVN 815
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDgitGYIVGYRVE-YREEGSEWKEVNVTPSS-TSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1804387592   816 AAGLS 820
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 934-1020 1.61e-12

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: 64.56  E-value: 1.61e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   934 PSPPYDITCLESFRDSMVLGWKQPDKIGGaeiTGYYVNYREVIGGVPGKWREANVKaVSEEAYKISNLKENVVYQFQVAA 1013
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGI---TGYIVGYRVEYREEGSEWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRA 76


                    ....*..
gi 1804387592  1014 MNMAGLG 1020
Cdd:smart00060   77 VNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
935-1023 2.11e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 2.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  935 SPPYDITCLESFRDSMVLGWKQPDKiGGAEITGYYVNYREVigGVPGKWREANVKAvSEEAYKISNLKENVVYQFQVAAM 1014
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPK--NSGEPWNEITVPG-TTTSVTLTGLKPGTEYEVRVQAV 76


                   ....*....
gi 1804387592 1015 NMAGLGAPS 1023
Cdd:pfam00041   77 NGGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
417-484 7.39e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 7.39e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  417 REGETMSLGCRVVITPEikhfqPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRV 484
Cdd:pfam07679   13 QEGESARFTCTVTGTPD-----PEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVA 75
fn3 pfam00041
Fibronectin type III domain;
741-823 8.94e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.43  E-value: 8.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  741 APGNIIPSRNTDTSVVVTWEESKDAK-ELVGYYIEASVAGSGkwEPCNNNPVKGSRFTC--HGLVTGQSYIFRVRAVNAA 817
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSG--EPWNEITVPGTTTSVtlTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 1804387592  818 GLSEYS 823
Cdd:pfam00041   80 GEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
639-724 1.86e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  639 GPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCEAGTEN-WQRVNTELPvkSPRFALFDLVEGKSYCFRVRCSNS 717
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEpWNEITVPGT--TTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 1804387592  718 AGVGEPS 724
Cdd:pfam00041   79 GGEGPPS 85
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 1572-1662 4.72e-11

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


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 60.83  E-value: 4.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1572 ARVLGGlPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASddhcTLKFEAGKTAY---FAITGVSTDDSGKYGLVV 1648
Cdd:cd05747      4 ATILTK-PRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVS----SQRHQITSTEYkstFEISKVQMSDEGNYTVVV 78

                           90
                   ....*....|....
gi 1804387592 1649 KNKYGSETSDFTIS 1662
Cdd:cd05747     79 ENSEGKQEAQFTLT 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 277-356 5.15e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 60.27  E-value: 5.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPInvhaNPGKYIIESRYGMH-TLEINACDFEDTAQYRASAM 355
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPI----SSGSTRSRSLSGSNsTLTISNVTRSDAGTYTCVAS 77


                   .
gi 1804387592  356 N 356
Cdd:pfam13927   78 N 78
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 276-369 8.35e-11

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: 59.90  E-value: 8.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  276 APEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINvhaNPGKYIIESRYGMHTLEINACDFEDTAQYRASAM 355
Cdd:cd20972      1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQ---NSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLAT 77

                           90
                   ....*....|....
gi 1804387592  356 NVKGELSAYASVVV 369
Cdd:cd20972     78 NSVGSDTTSAEIFV 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 1579-1650 1.40e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.12  E-value: 1.40e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHcTLKFEAGKTAYFAITGVSTDDSGKYGLVVKN 1650
Cdd:pfam13927    8 PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGST-RSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1590-1657 3.60e-10

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 57.34  E-value: 3.60e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592 1590 LNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGkTAYFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELG-NGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 1581-1663 4.50e-10

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 57.60  E-value: 4.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1581 VVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHctLKFEAGKT-AYFAITGVSTDDSGKYGLVVKNKYGSETSDF 1659
Cdd:cd05748      1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGR--VQIETTASsTSLVIKNAKRSDSGKYTLTLKNSAGEKSATI 78


                   ....
gi 1804387592 1660 TISV 1663
Cdd:cd05748     79 NVKV 82
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
654-818 4.74e-10

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 64.58  E-value: 4.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  654 VVLSWKPPGQRGHegimYFVEKcEAGTENWQRVNTelpVKSPRFALFDLVEGkSYCFRVRCSNSAGV-GEPSEATEVTVV 732
Cdd:COG4733    554 LTVSWDAPAGAVA----YEVEW-RRDDGNWVSVPR---TSGTSFEVPGIYAG-DYEVRVRAINALGVsSAWAASSETTVT 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  733 GdKLDIPKAPGNIIPSRNTDtSVVVTWEESKDAkELVGYYIEASVAGSGKWEPCNNNPVKGSRFTCHGLVTGQSYIFRVR 812
Cdd:COG4733    625 G-KTAPPPAPTGLTATGGLG-GITLSWSFPVDA-DTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRAR 701


                   ....*.
gi 1804387592  813 AVNAAG 818
Cdd:COG4733    702 AVDRSG 707
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 277-369 4.98e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 54.81  E-value: 4.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESryGMHTLEINACDFEDTAQYRASAMN 356
Cdd:cd05744      1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVREN--GRHSLIIEPVTKRDAGIYTCIARN 78

                           90
                   ....*....|...
gi 1804387592  357 VKGELSAYASVVV 369
Cdd:cd05744     79 RAGENSFNAELVV 91
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 277-369 1.90e-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: 53.16  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEK-ENVKLHCSVAGWPEPRVTWYKNQVPINvhANPGKYIIESrygmHTLEINACDFEDTAQYRASAM 355
Cdd:cd20978      1 PKFIQKPEKNVVVKGgQDVTLPCQVTGVPQPKITWLHNGKPLQ--GPMERATVED----GTLTIINVQPEDTGYYGCVAT 74

                           90
                   ....*....|....
gi 1804387592  356 NVKGELSAYASVVV 369
Cdd:cd20978     75 NEIGDIYTETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 423-485 2.39e-08

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 52.33  E-value: 2.39e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1804387592  423 SLGCRVVITPEikhfqPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVR 485
Cdd:cd00096      2 TLTCSASGNPP-----PTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 1579-1653 3.40e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 3.40e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDD-HCTLKFEAGKTAyFAITGVSTDDSGKYGLVVKNKYG 1653
Cdd:cd05744      7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSaHKMLVRENGRHS-LIIEPVTKRDAGIYTCIARNRAG 81
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 417-485 5.31e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 51.80  E-value: 5.31e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592  417 REGETMSLGCRVVITPEikhfqPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVR 485
Cdd:pfam13927   14 REGETVTLTCEATGSPP-----PTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 416-499 6.00e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.74  E-value: 6.00e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592   416 GREGETMSLGCRVVITPEikhfqPEIQWYRNG-VPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVRMGEYYEQYS 494
Cdd:smart00410    6 VKEGESVTLSCEASGSPP-----PEVTWYKQGgKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1804387592   495 AYVFV 499
Cdd:smart00410   81 TTLTV 85
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 1583-1663 7.75e-08

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 51.42  E-value: 7.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSDFTIS 1662
Cdd:cd20973      8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87


                   .
gi 1804387592 1663 V 1663
Cdd:cd20973     88 V 88
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 1582-1663 9.16e-08

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 51.26  E-value: 9.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1582 VTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFeaGKTayFAITGVSTDDSGKYGLVVKNKYGSETSDFTI 1661
Cdd:cd05731      5 TMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKFENF--NKT--LKIENVSEADSGEYQCTASNTMGSARHTISV 80


                   ..
gi 1804387592 1662 SV 1663
Cdd:cd05731     81 TV 82
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 1577-1663 1.10e-07

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 50.85  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1577 GLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALaSDDHCTLKFEAGKtayFAITGVSTDDSGKYGLVVKNKYGSET 1656
Cdd:cd20978      6 KPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGT---LTIINVQPEDTGYYGCVATNEIGDIY 81


                   ....*..
gi 1804387592 1657 SDFTISV 1663
Cdd:cd20978     82 TETLLHV 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 292-369 1.69e-07

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 50.28  E-value: 1.69e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  292 ENVKLHCSVAGWPEPRVTWYKNQVPInvhANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMNVKGELSAYASVVV 369
Cdd:cd05748      8 ESLRLDIPIKGRPTPTVTWSKDGQPL---KETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 294-365 1.71e-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: 50.02  E-value: 1.71e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1804387592  294 VKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESRygmHTLEINACDFEDTAQYRASAMN-VKGELSAYA 365
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN---GTLTISNVTLEDSGTYTCVASNsAGGSASASV 70
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 277-369 2.03e-07

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


Pssm-ID: 409473  Cd Length: 92  Bit Score: 50.54  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVpiNVHANPGKY-IIESRYGMHTLEINACDFEDTAQYRASAM 355
Cdd:cd05892      1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNE--MLQYNTDRIsLYQDNCGRICLLIQNANKKDAGWYTVSAV 78

                           90
                   ....*....|....
gi 1804387592  356 NVKGELSAYASVVV 369
Cdd:cd05892     79 NEAGVVSCNARLDV 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
987-1137 2.85e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.39  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  987 NVKAVSEEAYKISNLKENVVYQFQVAAMNMAGLGAPSAVSECFkceeWTIAVPGPPHSLKYSEVRKDSLVLHWKPPIHSG 1066
Cdd:COG3401    185 LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVT----TPTTPPSAPTGLTATADTPGSVTLSWDPVTESD 260

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804387592 1067 rtpVTGYFVdlKEAQAKEDQWRGLneAAIKTLYLKVRGLKEGISYVFRVRAINQAGVgkPSDLAGPVVAET 1137
Cdd:COG3401    261 ---ATGYRV--YRSNSGDGPFTKV--ATVTTTSYTDTGLTNGTTYYYRVTAVDAAGN--ESAPSNVVSVTT 322
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 1582-1663 3.44e-07

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


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.66  E-value: 3.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1582 VTIQEGKALNLTCNVWGDPTPEVSWLKNEKA--LASDDHCTLKFEAGKtAYFAITGVSTDDSGKYGLVVKNKYGSETSDF 1659
Cdd:cd20974     10 VVVLEGSTATFEAHVSGKPVPEVSWFRDGQVisTSTLPGVQISFSDGR-AKLSIPAVTKANSGRYSLTATNGSGQATSTA 88


                   ....
gi 1804387592 1660 TISV 1663
Cdd:cd20974     89 ELLV 92
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 277-370 3.95e-07

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


Pssm-ID: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 49.66  E-value: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYiIESRYGMHTLEINACDFEDTAQYRASAMN 356
Cdd:cd20974      1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQ-ISFSDGRAKLSIPAVTKANSGRYSLTATN 79

                           90
                   ....*....|....
gi 1804387592  357 VKGELSAYASVVVK 370
Cdd:cd20974     80 GSGQATSTAELLVL 93
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 1586-1663 4.38e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.93  E-value: 4.38e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592 1586 EGKALNLTCNVWGDPTPEVSWLKNEKALASddhctlkfeagKTAYFaITGVSTDDSGKYGLVVKNKYGSETSD-FTISV 1663
Cdd:pfam13895   13 EGEPVTLTCSAPGNPPPSYTWYKDGSAISS-----------SPNFF-TLSVSAEDSGTYTCVARNGRGGKVSNpVELTV 79
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 1587-1654 4.41e-07

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: 49.14  E-value: 4.41e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592 1587 GKALNLTCNVWGDPTPEVSWLKNEKALASDDHctLKFEAGKtayFAITGVSTDDSGKYGLVVKNKYGS 1654
Cdd:cd05728     14 GSSLRWECKASGNPRPAYRWLKNGQPLASENR--IEVEAGD---LRITKLSLSDSGMYQCVAENKHGT 76
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 1579-1657 5.43e-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: 49.16  E-value: 5.43e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLkFEAGKtayFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:cd20968      6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAV-LESGS---LRIHNVQKEDAGQYRCVAKNSLGIAYS 80
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 276-369 6.52e-07

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: 48.79  E-value: 6.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  276 APEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANpgKYIIESRYGMhtLEINACDFEDTAQYRASAM 355
Cdd:cd20976      1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAAD--RSTCEAGVGE--LHIQDVLPEDHGTYTCLAK 76

                           90
                   ....*....|....
gi 1804387592  356 NVKGELSAYASVVV 369
Cdd:cd20976     77 NAAGQVSCSAWVTV 90
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 1584-1653 8.10e-07

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


Pssm-ID: 409474  Cd Length: 92  Bit Score: 48.55  E-value: 8.10e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804387592 1584 IQEGKALNLTCNVWGDPTPEVSWLKNEKALA-SDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYG 1653
Cdd:cd05893     12 IFEGMPVTFTCRVAGNPKPKIYWFKDGKQISpKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQG 82
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 1577-1663 1.25e-06

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1577 GLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASD-DHCTLkfEAGkTAYFAITGVSTDDSGKYGLVVKNKYGSE 1655
Cdd:cd20976      6 SVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAaDRSTC--EAG-VGELHIQDVLPEDHGTYTCLAKNAAGQV 82


                   ....*...
gi 1804387592 1656 TSDFTISV 1663
Cdd:cd20976     83 SCSAWVTV 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 280-367 2.20e-06

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


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 47.35  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  280 IIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHAnpgKYIIESRYGMHTLEINACDFEDTAQYRASAMNVKG 359
Cdd:cd05747      7 LTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQ---RHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83


                   ....*...
gi 1804387592  360 ELSAYASV 367
Cdd:cd05747     84 KQEAQFTL 91
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 277-370 2.66e-06

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


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 47.26  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINvHANPGKYIIESRYGmhTLEINACDFEDTAQYRASAMN 356
Cdd:cd05736      1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDIN-PKLSKQLTLIANGS--ELHISNVRYEDTGAYTCIAKN 77

                           90
                   ....*....|....
gi 1804387592  357 VKGELSAYASVVVK 370
Cdd:cd05736     78 EGGVDEDISSLFVE 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 1579-1653 2.70e-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: 47.33  E-value: 2.70e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEaGKTAYFAITGVSTDDSGKYGLVVKNKYG 1653
Cdd:cd20949      6 AYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYR-ILADGLLINKVTQDDTGEYTCRAYQVNS 79
I-set pfam07679
Immunoglobulin I-set domain;
1374-1443 3.01e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 46.87  E-value: 3.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804387592 1374 VLLKCKVANiKKETHIVWYKDEREISVDEKH--DFKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKL 1443
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRFkvTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 287-369 3.59e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 46.62  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  287 TVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHtleinacdfedtaqYRASAMNVKG-ELSAYA 365
Cdd:pfam13895   10 VVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTLSVSAEDSGT--------------YTCVARNGRGgKVSNPV 75


                   ....
gi 1804387592  366 SVVV 369
Cdd:pfam13895   76 ELTV 79
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 277-369 3.75e-06

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


Pssm-ID: 409474  Cd Length: 92  Bit Score: 47.01  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANpgKYIIESRY-GMHTLEINACDFEDTAQYRASAM 355
Cdd:cd05893      1 PFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSD--HYTIQRDLdGTCSLHTTASTLDDDGNYTIMAA 78

                           90
                   ....*....|....
gi 1804387592  356 NVKGELSAYASVVV 369
Cdd:cd05893     79 NPQGRISCTGRLMV 92
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 1579-1663 4.48e-06

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


Pssm-ID: 409582  Cd Length: 91  Bit Score: 46.63  E-value: 4.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDD-HCTLKFEAGKTAyFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:cd20990      7 PGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSaHKMLVRENGVHS-LIIEPVTSRDAGIYTCIATNRAGQNSF 85


                   ....*.
gi 1804387592 1658 DFTISV 1663
Cdd:cd20990     86 NLELVV 91
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 279-359 5.79e-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: 46.17  E-value: 5.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  279 FIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGmhtLEINACDFEDTAQYRASAMNVK 358
Cdd:cd20949      2 FTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRILADG---LLINKVTQDDTGEYTCRAYQVN 78


                   .
gi 1804387592  359 G 359
Cdd:cd20949     79 S 79
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 1580-1657 7.85e-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: 45.85  E-value: 7.85e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592 1580 DVVTIQeGKALNLTCNV-WGDPTPEVSWLKNEKALASDDHCTLKFEAGKtayFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:cd05724      6 DTQVAV-GEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVDDGN---LLIAEARKSDEGTYKCVATNMVGERES 80
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 1592-1662 1.10e-05

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


Pssm-ID: 143223  Cd Length: 69  Bit Score: 44.87  E-value: 1.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804387592 1592 LTCNVWGDPTPEVSWLKNEKALASddhcTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSDFTIS 1662
Cdd:cd05746      3 IPCSAQGDPEPTITWNKDGVQVTE----SGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYASVSMVLS 69
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
739-843 1.20e-05

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 49.77  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  739 PKAPGNIIPSRNTDTSVVVTWEESKDAKELVGY--YIEASVAGSgkwepcnnnpVKGS-RFTCHGLVTGQSYIFRVRAVN 815
Cdd:COG3979      3 PTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYdvYRGGDQVAT----------VTGLtAWTVTGLTPGTEYTFTVGACD 72

                           90       100
                   ....*....|....*....|....*....
gi 1804387592  816 AAG-LSEYSRDSEAIEVKAAIGGGVSPDV 843
Cdd:COG3979     73 AAGnVSAASGTSTAMFGGSSTTLGSAEGV 101
IgI_Titin_M1-like cd20927
Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members ...
 1378-1443 1.43e-05

Immunoglobulin-like M1 domain from Titin; a member of the I-set of IgSF domains; The members here are composed of the Immunoglobulin-like M1 I-set domain from Titin 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-M1 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: 409521  Cd Length: 90  Bit Score: 45.03  E-value: 1.43e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592 1378 CKVANIKKETHIVWYKDEREISVDEKHD--FKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKL 1443
Cdd:cd20927     21 CKIENYDQSTQVTWYFGVRQLENSEKYEitYEDGVAILYVKDITKFDDGTYRCKVVNDYGEDSSYAEL 88
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 1583-1654 1.50e-05

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 45.24  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHctlkFEAGK--------TAYFAITGVSTDDSGKYGLVVKNKYGS 1654
Cdd:cd20956     12 TLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPR----FRVGDyvtsdgdvVSYVNISSVRVEDGGEYTCTATNDVGS 87
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 412-485 1.58e-05

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.90  E-value: 1.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804387592  412 DVSFGREGETMSLGCRVVITPEikhfqPEIQWYRNGVPLSPSK-WVQTLWSGERATLTFSHLNKEDEGLYTIRVR 485
Cdd:cd05891      9 DVVTIMEGKTLNLTCTVFGNPD-----PEVIWFKNDQDIELSEhYSVKLEQGKYASLTIKGVTSEDSGKYSINVK 78
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 418-500 1.58e-05

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 44.75  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  418 EGETMSLGCRVVITPeikhfQPEIQWYRNGVPLSPSKWVQTLWsGERATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYV 497
Cdd:cd04978     13 PGETGELICEAEGNP-----QPTITWRLNGVPIEPAPEDMRRT-VDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANAFL 86


                   ...
gi 1804387592  498 FVR 500
Cdd:cd04978     87 HVL 89
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 274-369 1.70e-05

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


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 44.89  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  274 LHAPEfiiklrSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANPGKYIIESrygmHTLEINACDFEDTAQYRAS 353
Cdd:cd05867      3 TRRPQ------SHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSS----GALILTDVQPSDTAVYQCE 72

                           90
                   ....*....|....*.
gi 1804387592  354 AMNVKGELSAYASVVV 369
Cdd:cd05867     73 ARNRHGNLLANAHVHV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 1579-1650 2.35e-05

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: 44.44  E-value: 2.35e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEagktAYFAITGVSTDDSGKYGLVVKN 1650
Cdd:cd20957      8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSE----DVLVIPSVKREDKGMYQCFVRN 75
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 406-485 3.22e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 44.02  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  406 HFDDKFDVSFGREGETMSLGCRVVITPeikhfQPEIQWYRNGVPLSP-SKWVQTLWSGERATLTFSHLNKEDEGLYTIRV 484
Cdd:cd05744      2 HFLQAPGDLEVQEGRLCRFDCKVSGLP-----TPDLFWQLNGKPVRPdSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIA 76


                   .
gi 1804387592  485 R 485
Cdd:cd05744     77 R 77
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 296-370 4.04e-05

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


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 43.85  E-value: 4.04e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804387592  296 LHCSVAGWPEPRVTWYKNQVPINVHANPGKyIIESRYGMhtLEINACDFEDTAQYRASAMNVKG-ELSAYASVVVK 370
Cdd:cd05738     19 MLCAASGNPDPEISWFKDFLPVDTATSNGR-IKQLRSGA--LQIENSEESDQGKYECVATNSAGtRYSAPANLYVR 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 1583-1663 4.98e-05

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: 43.65  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGD-PTPEVSWLKNEKALASDDHCTLKFEAG-KTAYFAITGVSTDDSGKYGLVVKNKYGSETSDFT 1660
Cdd:cd05750     10 TVQEGSKLVLKCEATSEnPSPRYRWFKDGKELNRKRPKNIKIRNKkKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89


                   ...
gi 1804387592 1661 ISV 1663
Cdd:cd05750     90 VTV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1374-1427 5.09e-05

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.09  E-value: 5.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1804387592 1374 VLLKCKVANiKKETHIVWYKDEREISVDEKHD--FKDGICTLLITEFSKKDAGIYE 1427
Cdd:cd00096      1 VTLTCSASG-NPPPTITWYKNGKPLPPSSRDSrrSELGNGTLTISNVTLEDSGTYT 55
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
716-859 5.31e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 48.02  E-value: 5.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  716 NSAGVGEPSEATEVTVVGDKLDIPKAPGNIIpsrntdTSVVVTWEESKDAkelVGYYIEASvAGSGKWepcNNNP-VKGS 794
Cdd:COG4733    521 AGAFDDVPPQWPPVNVTTSESLSVVAQGTAV------TTLTVSWDAPAGA---VAYEVEWR-RDDGNW---VSVPrTSGT 587

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804387592  795 RFTCHGLVTGQsYIFRVRAVNAAGLSeySRDSEAIEVkaAIGGGVSPdvcPAlsdEPGGLTASRG 859
Cdd:COG4733    588 SFEVPGIYAGD-YEVRVRAINALGVS--SAWAASSET--TVTGKTAP---PP---APTGLTATGG 641
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 1579-1663 6.18e-05

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


Pssm-ID: 409475  Cd Length: 86  Bit Score: 43.29  E-value: 6.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALaSDDHCTLKFEAGK-TAYFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:cd05894      2 ENTIVVVAGNKLRLDVPISGEPAPTVTWSRGDKAF-TATEGRVRVESYKdLSSFVIEGAEREDEGVYTITVTNPVGEDHA 80


                   ....*.
gi 1804387592 1658 DFTISV 1663
Cdd:cd05894     81 SLFVKV 86
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 1587-1668 7.21e-05

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


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.40  E-value: 7.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1587 GKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAyFAITGVSTDDSGKYGLVVKNKYGSeTSDFTiSVFIP 1666
Cdd:cd05736     15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSE-LHISNVRYEDTGAYTCIAKNEGGV-DEDIS-SLFVE 91


                   ..
gi 1804387592 1667 EE 1668
Cdd:cd05736     92 DS 93
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 1571-1663 7.90e-05

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


Pssm-ID: 409561  Cd Length: 92  Bit Score: 43.15  E-value: 7.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1571 RARVLGGLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALAS-DDHCTLKFEAGKTAYFAITGVStdDSGKYGLVVK 1649
Cdd:cd20969      1 RAAIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSaKSNGRLTVFPDGTLEVRYAQVQ--DNGTYLCIAA 78

                           90
                   ....*....|....
gi 1804387592 1650 NKYGSETSDFTISV 1663
Cdd:cd20969     79 NAGGNDSMPAHLHV 92
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 277-359 8.44e-05

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


Pssm-ID: 409567  Cd Length: 91  Bit Score: 42.84  E-value: 8.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPinVHANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMN 356
Cdd:cd20975      1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQP--VRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVN 78


                   ...
gi 1804387592  357 VKG 359
Cdd:cd20975     79 EYG 81
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 1583-1663 8.47e-05

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 43.18  E-value: 8.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGDPTPEVSWLKNEKAL-ASDDHCTLKFEA-GKTAYFAITGVSTDDSGKYGLVVKNKYGSETSDFT 1660
Cdd:cd20951     11 TVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdPSSIPGKYKIESeYGVHVLHIRRVTVEDSAVYSAVAKNIHGEASSSAS 90


                   ...
gi 1804387592 1661 ISV 1663
Cdd:cd20951     91 VVV 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 418-497 1.25e-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: 42.38  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  418 EGETMSLGCRVVITPeikhfQPEIQWYRNGVPLSPSKWVQTLwsgERATLTFSHLNKEDEGLYTIRV--RMGEYYEQYSA 495
Cdd:cd20978     15 GGQDVTLPCQVTGVP-----QPKITWLHNGKPLQGPMERATV---EDGTLTIINVQPEDTGYYGCVAtnEIGDIYTETLL 86


                   ..
gi 1804387592  496 YV 497
Cdd:cd20978     87 HV 88
I-set pfam07679
Immunoglobulin I-set domain;
1155-1210 1.31e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 1.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1804387592 1155 SLNFECD-QMTPKSEFTWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGLYSC 1210
Cdd:pfam07679   17 SARFTCTvTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 1587-1654 1.38e-04

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 42.59  E-value: 1.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592 1587 GKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGS 1654
Cdd:cd05729     19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGS 86
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
440-592 1.60e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.48  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  440 EIQWYRNGvplspSKWVQTlwsgERATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVrdADAEIEGAPAAPLDVKCL 519
Cdd:COG4733    568 EVEWRRDD-----GNWVSV----PRTSGTSFEVPGIYAGDYEVRVRAINALGVSSAWAAS--SETTVTGKTAPPPAPTGL 636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  520 EANKDY--IIISWKQPAvdgGSPILGYfidkcEV---GTDSW--SQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKTGI 592
Cdd:COG4733    637 TATGGLggITLSWSFPV---DADTLRT-----EIrysTTGDWasATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGN 708
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 1583-1665 1.63e-04

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


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.18  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGDPTPEVSWLKNEKALasddHCTLKFE---AGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSdf 1659
Cdd:cd20972     12 EVAEGSKVRLECRVTGNPTPVVRWFCEGKEL----QNSPDIQihqEGDLHSLIIAEAFEEDTGRYSCLATNSVGSDTT-- 85


                   ....*.
gi 1804387592 1660 TISVFI 1665
Cdd:cd20972     86 SAEIFV 91
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 1587-1663 1.84e-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: 42.15  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1587 GKALNLTCNVWGDPTPEVSWLKNEKALASDD----------HCTLKFEAgktayfaitgVSTDDSGKYGLVVKNKYGSET 1656
Cdd:cd05857     19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHriggykvrnqHWSLIMES----------VVPSDKGNYTCVVENEYGSIN 88


                   ....*..
gi 1804387592 1657 SDFTISV 1663
Cdd:cd05857     89 HTYHLDV 95
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 276-362 2.44e-04

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 41.78  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  276 APEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPI--NVHANPGKYIIESRYGMHTLEINACDFEDTAQYRAS 353
Cdd:cd20956      1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIpeSPRFRVGDYVTSDGDVVSYVNISSVRVEDGGEYTCT 80


                   ....*....
gi 1804387592  354 AMNVKGELS 362
Cdd:cd20956     81 ATNDVGSVS 89
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 1582-1663 3.99e-04

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.95  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1582 VTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTayFAITGVSTDDSGKYGLVVKNK-YGSETSDFT 1660
Cdd:cd20970     12 VTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGTT--LTIRNIRRSDMGIYLCIASNGvPGSVEKRIT 89


                   ...
gi 1804387592 1661 ISV 1663
Cdd:cd20970     90 LQV 92
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 1579-1663 5.03e-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: 40.68  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNekalASDDhctlkFEAGKT---------AYFAITGVSTDDSGKYGLVVK 1649
Cdd:cd05763      6 PHDITIRAGSTARLECAATGHPTPQIAWQKD----GGTD-----FPAARErrmhvmpedDVFFIVDVKIEDTGVYSCTAQ 76

                           90
                   ....*....|....
gi 1804387592 1650 NKYGSETSDFTISV 1663
Cdd:cd05763     77 NSAGSISANATLTV 90
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 1579-1657 5.61e-04

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


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 41.00  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDD-----HCTLkFEAGKTAYFAITG--VSTDDSGKYGLVVKNK 1651
Cdd:cd07693      7 PSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKddprsHRIV-LPSGSLFFLRVVHgrKGRSDEGVYVCVAHNS 85


                   ....*.
gi 1804387592 1652 YGSETS 1657
Cdd:cd07693     86 LGEAVS 91
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 287-369 5.79e-04

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.57  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  287 TVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANpgKYIIESRygMHTLEINACDFEDTAQYRASAMN-VKGELSAYA 365
Cdd:cd20970     13 TAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNT--RYIVREN--GTTLTIRNIRRSDMGIYLCIASNgVPGSVEKRI 88


                   ....
gi 1804387592  366 SVVV 369
Cdd:cd20970     89 TLQV 92
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 1583-1663 7.27e-04

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: 40.22  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGDPTPEVSWLKN----EKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSD 1658
Cdd:cd05765     11 TVKVGETASFHCDVTGRPQPEITWEKQvpgkENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGLLRAN 90


                   ....*
gi 1804387592 1659 FTISV 1663
Cdd:cd05765     91 FPLSV 95
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 1586-1656 7.34e-04

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


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 40.15  E-value: 7.34e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804387592 1586 EGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGkTAYFAITGVStdDSGKYGLVVKNKYGSET 1656
Cdd:cd05764     14 EGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTLVYDNG-TLDILITTVK--DTGAFTCIASNPAGEAT 81
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 280-359 7.72e-04

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


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 40.20  E-value: 7.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  280 IIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPINVHANP--GKYIIESRYGMHTLEINACDFEDTAQYRASAMNV 357
Cdd:cd05732      5 ITYLENQTAVELEQITLTCEAEGDPIPEITWRRATRGISFEEGDldGRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNR 84


                   ..
gi 1804387592  358 KG 359
Cdd:cd05732     85 IG 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 417-486 8.31e-04

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 39.87  E-value: 8.31e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804387592  417 REGETMSLGCRVVITPEikhfQPEIQWYRNG-VPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVRM 486
Cdd:pfam00047    9 LEGDSATLTCSASTGSP----GPDVTWSKEGgTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNN 75
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 1586-1663 8.97e-04

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 39.89  E-value: 8.97e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592 1586 EGKALNLTCNVWGDPTPEVSWLKNEKALASDDhcTLKFEAGKTayFAITGVSTDDSGKYGLVVKNKYGSETSDFTISV 1663
Cdd:cd05876      9 RGQSLVLECIAEGLPTPTVKWLRPSGPLPPDR--VKYQNHNKT--LQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 277-370 9.50e-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: 39.86  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  277 PEFIIKLRSHTVWEKENVKLHCSVAGWPEPRVTWYKN--QVPIN----VHANpGkyiiesrygmhTLEINACDF-EDTAQ 349
Cdd:cd20958      1 PPFIRPMGNLTAVAGQTLRLHCPVAGYPISSITWEKDgrRLPLNhrqrVFPN-G-----------TLVIENVQRsSDEGE 68

                           90       100
                   ....*....|....*....|.
gi 1804387592  350 YRASAMNVKGElSAYASVVVK 370
Cdd:cd20958     69 YTCTARNQQGQ-SASRSVFVK 88
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 436-480 1.08e-03

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


Pssm-ID: 409417  Cd Length: 95  Bit Score: 39.91  E-value: 1.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1804387592  436 HFQPEIQWYRNGVPLSPSKWVQTLWSGERaTLTFSHLNKEDEGLY 480
Cdd:cd05760     28 HPRPTYQWFRDGTPLSDGQGNYSVSSKER-TLTLRSAGPDDSGLY 71
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 1577-1665 1.20e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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: 409450  Cd Length: 89  Bit Score: 39.53  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1577 GLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDdhctLKFEAGktAYFAITGVSTDDSGKYGLVVKNKYGSET 1656
Cdd:cd05864      7 GMESLVEAKVGERVRIPVKYLGYPPPEIKWYKNGIPIESN----HTIKAG--HVLTIMEVTEKDAGNYTVVLTNPISKEK 80


                   ....*....
gi 1804387592 1657 SDFTISVFI 1665
Cdd:cd05864     81 QRHTFSLVV 89
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 439-500 1.21e-03

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 39.50  E-value: 1.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1804387592  439 PEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVR--MGEyyeqYSAYVFVR 500
Cdd:cd05748     22 PTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKnsAGE----KSATINVK 81
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 1162-1221 1.26e-03

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


Pssm-ID: 143223  Cd Length: 69  Bit Score: 39.09  E-value: 1.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1162 QMTPKSEFTWSKDYVSTEDSPRLEVESKGNktkMTFKDLGMDDLGLYSCDVIDTDGIASS 1221
Cdd:cd05746      8 QGDPEPTITWNKDGVQVTESGKFHISPEGY---LAIRDVGVADQGRYECVARNTIGYASV 64
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1155-1221 1.30e-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: 39.41  E-value: 1.30e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592  1155 SLNFECD-QMTPKSEFTWSKDYVST-EDSPRLEVESKGNKTKMTFKDLGMDDLGLYSCDVIDTDGIASS 1221
Cdd:smart00410   11 SVTLSCEaSGSPPPEVTWYKQGGKLlAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 283-369 1.33e-03

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: 39.48  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  283 LRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVPInVHANPGKyIIESRYGMHTLEINACDFEDTAQYRASAMNVKGELS 362
Cdd:cd20973      4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPI-VESRRFQ-IDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81


                   ....*..
gi 1804387592  363 AYASVVV 369
Cdd:cd20973     82 CSAELTV 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 292-369 1.35e-03

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: 39.30  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  292 ENVKLHCSVAGWPEPRVTWYKN--QVPInvhanpgkyiieSRYGM---HTLEINACDFEDTAQYRASAMNVKGELSAYAS 366
Cdd:cd05725     13 DSAEFQCEVGGDPVPTVRWRKEdgELPK------------GRYEIlddHSLKIRKVTAGDMGSYTCVAENMVGKIEASAT 80


                   ...
gi 1804387592  367 VVV 369
Cdd:cd05725     81 LTV 83
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 417-483 1.35e-03

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: 39.62  E-value: 1.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804387592  417 REGETMSLGCRVVITPeikhfQPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIR 483
Cdd:cd20949     12 KEGQSATILCEVKGEP-----QPNVTWHFNGQPISASVADMSKYRILADGLLINKVTQDDTGEYTCR 73
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 1580-1663 1.46e-03

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: 39.40  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1580 DVVTIQEGKALnLTCNVWGDPTPEVSWLKNEKALASDDHctlKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSDF 1659
Cdd:cd20952      8 NQTVAVGGTVV-LNCQATGEPVPTISWLKDGVPLLGKDE---RITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSA 83


                   ....
gi 1804387592 1660 TISV 1663
Cdd:cd20952     84 VLDV 87
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 292-369 1.64e-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: 39.53  E-value: 1.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  292 ENVKLHCSVAGWPEPRVTWYKNQVPINVHANpgKYIIEsrYGMHTLEINACDFEDTAQYRASAMNVKGELSAYASVVV 369
Cdd:cd05730     19 QSVTLACDADGFPEPTMTWTKDGEPIESGEE--KYSFN--EDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 1579-1661 1.66e-03

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: 39.10  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNV-WGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:pfam00047    3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82


                   ....
gi 1804387592 1658 DFTI 1661
Cdd:pfam00047   83 STSL 86
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 1583-1663 1.68e-03

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


Pssm-ID: 409567  Cd Length: 91  Bit Score: 39.38  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSDFTIS 1662
Cdd:cd20975     11 SVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQCEARLE 90


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gi 1804387592 1663 V 1663
Cdd:cd20975     91 V 91
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 292-369 1.70e-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: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  292 ENVKLHCSVA-GWPEPRVTWYKNQVPINVhANPGKYIIESrygmHTLEINACDFEDTAQYRASAMNVKGE-LSAYASVVV 369
Cdd:cd05724     13 EMAVLECSPPrGHPEPTVSWRKDGQPLNL-DNERVRIVDD----GNLLIAEARKSDEGTYKCVATNMVGErESRAARLSV 87
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 287-358 1.77e-03

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 39.12  E-value: 1.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  287 TVWEKENVKLHCSVAGWPEPRVTWYKNQVPIN------VHANPGKYIiesrygmhTLEINACDFEDTAQYrasAMNVK 358
Cdd:cd05891     12 TIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIElsehysVKLEQGKYA--------SLTIKGVTSEDSGKY---SINVK 78
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 417-482 1.95e-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: 39.10  E-value: 1.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804387592  417 REGETMSLGCRVVITPeikhfQPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTI 482
Cdd:cd20972     14 AEGSKVRLECRVTGNP-----TPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSC 74
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 292-359 2.07e-03

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 39.07  E-value: 2.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  292 ENVKLHCSVAGWPEPRVTWYKNQVPInvhanPGKYIIESRYGMhtLEINACDFEDTAQYRASAMNVKG 359
Cdd:cd04968     17 QTVTLECFALGNPVPQIKWRKVDGSP-----SSQWEITTSEPV--LEIPNVQFEDEGTYECEAENSRG 77
IgI_TrKABC_d5 cd04971
Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB, and TrkC; member of the I-set ...
 1579-1656 2.20e-03

Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB, and TrkC; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth domain of Trk receptors TrkA, TrkB, and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, TrkB, and TrkC mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. TrkA is recognized by NGF. TrkB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain, and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409360  Cd Length: 96  Bit Score: 38.92  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTC---NVWGDPTPEVSWLKNEKAL-ASDDHCTlKFEAGKTAYFAITGV------STDDSGKYGLVV 1648
Cdd:cd04971      2 PVIVRLEEPELRHHWCipfTVRGNPKPTLTWYHNGAVLnESDYIRT-EIHYEAATPTEYHGClkfdnpTHVNNGNYTLVA 80


                   ....*...
gi 1804387592 1649 KNKYGSET 1656
Cdd:cd04971     81 SNEYGQDS 88
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 1358-1444 2.24e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 39.02  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1358 PHFAEYL-SWEVTGECNVLLKCKVANIKKeTHIVWYKDEREISVDEKHDF---KDGICTLLITEFSKKDAGIYEVILKDD 1433
Cdd:cd05744      1 PHFLQAPgDLEVQEGRLCRFDCKVSGLPT-PDLFWQLNGKPVRPDSAHKMlvrENGRHSLIIEPVTKRDAGIYTCIARNR 79

                           90
                   ....*....|.
gi 1804387592 1434 RGKDKSRLKLV 1444
Cdd:cd05744     80 AGENSFNAELV 90
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 1587-1657 2.36e-03

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


Pssm-ID: 409563  Cd Length: 93  Bit Score: 38.99  E-value: 2.36e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1804387592 1587 GKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKFEAGKTAYFAITGVSTD-DSGKYGLVVKNKYGSETS 1657
Cdd:cd20971     16 QSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIASVTDdDATVYQVRATNQGGSVSG 87
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 417-494 2.36e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 38.53  E-value: 2.36e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  417 REGETMSLGCRVVITPEIKhfqpeIQWYRNGVPLSPSKwvqtlwsgeraTLTFSHLNKEDEGLYTIRVRMGEYYEQYS 494
Cdd:pfam13895   12 TEGEPVTLTCSAPGNPPPS-----YTWYKDGSAISSSP-----------NFFTLSVSAEDSGTYTCVARNGRGGKVSN 73
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 283-359 2.46e-03

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 38.93  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  283 LRSHTVWEKENVKLHCSVAGWPEPRVTWYKNQVP--------INVHANPGKYIIESRYGmhtleiNACDFEdtAQYRASA 354
Cdd:cd05733      8 PKDYIVDPRDNITIKCEAKGNPQPTFRWTKDGKFfdpakdprVSMRRRSGTLVIDNHNG------GPEDYQ--GEYQCYA 79


                   ....*
gi 1804387592  355 MNVKG 359
Cdd:cd05733     80 SNELG 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1373-1443 2.66e-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: 38.64  E-value: 2.66e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804387592  1373 NVLLKCKVANiKKETHIVWYKDEREIsVDEKHDFK----DGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKL 1443
Cdd:smart00410   11 SVTLSCEASG-SPPPEVTWYKQGGKL-LAESGRFSvsrsGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 418-481 3.41e-03

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: 38.32  E-value: 3.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804387592  418 EGETMSLGCRVVITPeikhfQPEIQWYRNGVPLSPSKWVQTLWSGE-RATLTFSHLNKEDEGLYT 481
Cdd:cd20973     11 EGSAARFDCKVEGYP-----DPEVKWMKDDNPIVESRRFQIDQDEDgLCSLIISDVCGDDSGKYT 70
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 1587-1663 3.52e-03

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 38.30  E-value: 3.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804387592 1587 GKALNLTCNVWGDPTPEVSWLKNEKALASDdhcTLKFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETSDFTISV 1663
Cdd:cd05856     19 GSSVRLKCVASGNPRPDITWLKDNKPLTPP---EIGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 294-369 3.91e-03

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: 38.25  E-value: 3.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804387592  294 VKLHCSVAGWPEPRVTWYKNQVPINVHaNPGKYIIESrygmHTLEINACDFEDTAQYRASAMNVKGELSAYASVVV 369
Cdd:cd20952     17 VVLNCQATGEPVPTISWLKDGVPLLGK-DERITTLEN----GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVLDV 87
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 1579-1657 4.14e-03

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


Pssm-ID: 409388  Cd Length: 84  Bit Score: 37.95  E-value: 4.14e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHctlkFEAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:cd05723      4 PSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPSDY----FKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQA 78
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 1582-1653 4.64e-03

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


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 38.27  E-value: 4.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804387592 1582 VTIQEGKALNLTCNVWGDPTPEVSWLK-------NEKALasDDHCTLKFEAGKTAyFAITGVSTDDSGKYGLVVKNKYG 1653
Cdd:cd05732     11 QTAVELEQITLTCEAEGDPIPEITWRRatrgisfEEGDL--DGRIVVRGHARVSS-LTLKDVQLTDAGRYDCEASNRIG 86
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 1579-1663 4.73e-03

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: 37.76  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1579 PDVVTIQEGKALNLTCNVWGDPTPEVSWLKNE------KALASDDHcTLKfeagktayfaITGVSTDDSGKYGLVVKNKY 1652
Cdd:cd05725      4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDgelpkgRYEILDDH-SLK----------IRKVTAGDMGSYTCVAENMV 72

                           90
                   ....*....|.
gi 1804387592 1653 GSETSDFTISV 1663
Cdd:cd05725     73 GKIEASATLTV 83
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 287-358 4.82e-03

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 37.96  E-value: 4.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  287 TVWEKENVKLHCSVAGWPEPRVTWYKNQVPI------NVHANPGKYIiesrygmhTLEINACDFEDTAQYrasAMNVK 358
Cdd:cd05737     12 TIMEGKTLNLTCNVWGDPPPEVSWLKNDQALafldhcNLKVEAGRTV--------YFTINGVSSEDSGKY---GLVVK 78
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 1583-1664 4.95e-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: 37.99  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592 1583 TIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHcTLKFEAGKTAyFAITGVSTDDSGKYGLVVKNKYGSETSDFTIS 1662
Cdd:cd05730     14 TANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSE-MTILDVDKLDEAEYTCIAENKAGEQEAEIHLK 91


                   ..
gi 1804387592 1663 VF 1664
Cdd:cd05730     92 VF 93
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 294-369 5.20e-03

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 37.92  E-value: 5.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804387592  294 VKLHCSVAGWPEPRVTWYKNQVPINVHAnpgkyIIESRYGMHTLEINACDFEDTAQYRASAMNVKGELSAYASVVV 369
Cdd:cd05856     22 VRLKCVASGNPRPDITWLKDNKPLTPPE-----IGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 292-359 5.69e-03

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 37.47  E-value: 5.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  292 ENVKLHCSVAGWPEPRVTWYKNQVPINVHAnpgKYIIESRYGMHTLEINACDFEDTAQYRASAMNVKG 359
Cdd:cd05743      2 ETVEFTCVATGVPTPIINWRLNWGHVPDSA---RVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
Ig1_Tyro3_like cd20961
First immunoglobulin (Ig)-like domain of Tyro3 receptor tyrosine kinase (RTK), and similar ...
 1582-1657 6.09e-03

First immunoglobulin (Ig)-like domain of Tyro3 receptor tyrosine kinase (RTK), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Tyro3 receptor tyrosine kinase (RTK). Tyro3 together with Axl and Mer form the Axl/Tyro3 family of receptor tyrosine kinases (RTKs). This family includes Axl (also known as Ark, Ufo, and Tyro7), Tyro3 (also known as Sky, Rse, Brt, Dtk, and Tif), and Mer (also known as Nyk, c-Eyk, and Tyro12). Axl/Tyro3 family receptors have an extracellular portion with two Ig-like domains followed by two fibronectin-types III (FNIII) domains, a membrane-spanning single helix, and a cytoplasmic tyrosine kinase domain. Axl, Tyro3 and Mer are widely expressed in adult tissues, though they show higher expression in the brain, in the lymphatic and vascular systems, and in the testis. Axl, Tyro3, and Mer bind the vitamin K dependent protein Gas6 with high affinity, and in doing so activate their tyrosine kinase activity. Axl/Gas6 signaling may play a part in cell adhesion processes, prevention of apoptosis, and cell proliferation.


Pssm-ID: 409553  Cd Length: 87  Bit Score: 37.43  E-value: 6.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804387592 1582 VTIQEGKALNLTCNVWGDPTPEVSWLKNEKALASDDHCTLKF-EAGKTAYFAITGVSTDDSGKYGLVVKNKYGSETS 1657
Cdd:cd20961      3 LTVSQGQPVKLNCSVEGMEEPDIQWVKDGAVVQNLDQLYIPVsEQHWIGFLSLKSVERSDAGRYWCQVEDGGETEIS 79
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 290-369 6.92e-03

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 36.84  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  290 EKENVKLHCSVAGWPEPRVTWYKNQVPINVHAnpgKYIIESRygmHTLEINACDFEDTAQYRASAMNVKGELSAYASVVV 369
Cdd:cd05745      1 EGQTVDFLCEAQGYPQPVIAWTKGGSQLSVDR---RHLVLSS---GTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 418-482 7.62e-03

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


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 37.40  E-value: 7.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804387592  418 EGETMSLGCRVVITPeikhfQPEIQWYRNGVPLSPSKWVQTLWSGERA---TLTFSHLNKEDEGLYTI 482
Cdd:cd20951     14 EKSDAKLRVEVQGKP-----DPEVKWYKNGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSA 76
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 282-369 9.80e-03

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: 37.11  E-value: 9.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804387592  282 KLRSHTVWEKENVKLHC-SVAGWPEPRVTWYKNQVPINvHANPGKYIIESRYGMHTLEINACDFEDTAQYRASAMNVKGE 360
Cdd:cd05750      5 EMKSQTVQEGSKLVLKCeATSENPSPRYRWFKDGKELN-RKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGK 83


                   ....*....
gi 1804387592  361 LSAYASVVV 369
Cdd:cd05750     84 DTVTGNVTV 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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