Immunoglobulin Domain C1 of human cardiac Myosin Binding Protein C and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain C1 of human cardiac Myosin Binding Protein C (MyBP-C). MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. 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 C1 domain of the MyBP-C 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  160 LFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTG 239
Cdd:cd20962      1 LFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFAG 80

                           90       100
                   ....*....|....*....|.
gi 1825953459  240 GYRCEVSTKDKFDCSNFNLTV 260
Cdd:cd20962     81 GYRCEVSTKDKFDCSNFNLTV 101

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. 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 Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  371 KKLEPAYQVSKGHKIRLTVELADPDAEVRWLKNGQEIQMSgSKYIFESIGAKRTLTISQCSLADDAAYQCVVGGEKCSTE 450
Cdd:cd20967      1 KKAQPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSS-SKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFE 79

                   ...
gi 1825953459  451 LFV 453
Cdd:cd20967     80 LFV 82

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  986 TIQKKVREPVNLLIPFQGKPRPQVTWTKEGQPLAG-EEVSVRNSPTDTILFIRAARRAHSGTYQVTVRIENMEDEATLVL 1064
Cdd:cd05748      1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                   ..
gi 1825953459 1065 QV 1066
Cdd:cd05748     81 KV 82

Tri-helix bundle domain; This domain can be found in the myosin-binding motif (m-domain) region present in myosin-binding protein C (MyBP-C). MyBP-C is a sarcomeric assembly protein necessary for the regulation of sarcomere structure and function. The MyBP-C family of proteins consists mainly of modules with immunoglobulin (Ig) or fibronectin folds. This domain exhibits a three-helix bundle fold and there is a known actin-binding motif, LK(R/K)XK positioned in the third helix (alpha3), similar to that found in villin and related proteins.

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1825953459  324 DVWEILRQAPPSEYERIAFQYGVTDLRGMLKRLK 357
Cdd:pfam18362    1 DVWEILSNAPPKDYEKIAFQYGITDLRGMLKKLK 34

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459   12 FSKKPRSVEVAAGSPVVFEVETERAGV-KVRWQRGGSDIGASSKYGLATEGTRHTLTVREVGPADQGSYAVIA----GSS 86
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGEA 82

                   ....*...
gi 1825953459   87 KVKFDLKV 94
Cdd:pfam07679   83 EASAELTV 90

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1825953459  557 DLTVGAKDQAVFKCEVS---DENVrgVWLKNGKELLPDSRIKVSHIGRVHKLTIDDVTPADEADYSFV 621
Cdd:pfam07679    9 DVEVQEGESARFTCTVTgtpDPEV--SWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV 74

Immunoglobulin Domain C1 of human cardiac Myosin Binding Protein C and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain C1 of human cardiac Myosin Binding Protein C (MyBP-C). MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. 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 C1 domain of the MyBP-C 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  160 LFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTG 239
Cdd:cd20962      1 LFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFAG 80

                           90       100
                   ....*....|....*....|.
gi 1825953459  240 GYRCEVSTKDKFDCSNFNLTV 260
Cdd:cd20962     81 GYRCEVSTKDKFDCSNFNLTV 101

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. 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 Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  371 KKLEPAYQVSKGHKIRLTVELADPDAEVRWLKNGQEIQMSgSKYIFESIGAKRTLTISQCSLADDAAYQCVVGGEKCSTE 450
Cdd:cd20967      1 KKAQPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSS-SKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFE 79

                   ...
gi 1825953459  451 LFV 453
Cdd:cd20967     80 LFV 82

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  986 TIQKKVREPVNLLIPFQGKPRPQVTWTKEGQPLAG-EEVSVRNSPTDTILFIRAARRAHSGTYQVTVRIENMEDEATLVL 1064
Cdd:cd05748      1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKEtGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                   ..
gi 1825953459 1065 QV 1066
Cdd:cd05748     81 KV 82

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  776 PDAPAAPKVSNVGEDSCTVQWEPPAYDGGqPVLGYILERKKKKSYRWMRLNFDLIQELSHEARRMIEGVVYEMRVYAVNA 855
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|.
gi 1825953459  856 IGMSRPSPASQ 866
Cdd:cd00063     80 GGESPPSESVT 90

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459 1188 TQPLVNRSVIAGYTTMLCCAVRGSPKPKISWFKNGLDLGEDARFRM-FSKQGVLTLEIRKPCPFDGGIYVCRATNLQGEA 1266
Cdd:cd20973      1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                   ....*...
gi 1825953459 1267 QCECRLEV 1274
Cdd:cd20973     81 TCSAELTV 88

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  1193 NRSVIAGYTTMLCCAVRGSPKPKISWFKNGLD-LGEDARFRMFSKQGVLTLEIRKPCPFDGGIYVCRATNLQGEAQCECR 1271
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                    ...
gi 1825953459  1272 LEV 1274
Cdd:smart00410   83 LTV 85

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459   12 FSKKPRSVEVAAGSPVVFEVETERAGV-KVRWQRGGSDIGASSKYGLATEGTRHTLTVREVGPADQGSYAVIA----GSS 86
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaGEA 82

                   ....*...
gi 1825953459   87 KVKFDLKV 94
Cdd:pfam07679   83 EASAELTV 90

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  1070 PSPPQDLRVTEAWGLNVALEWKPPQDDGNTELW-GYTVQKADKKTmEWFTVLEHYRRTHCVVPELIIGNGYYFRVFSQNM 1148
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvGYRVEYREEGS-EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                    ....
gi 1825953459  1149 VGSS 1152
Cdd:smart00060   80 AGEG 83

Fibronectin type III domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  875 SEPTHLAVEDVSDTTVSLKWRPPErVGAGGLDGYSVEYCPEGCSEWVTALRGLTEHTSILVKDLPTGARLLFRVRAHNMA 954
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ....*
gi 1825953459  955 GPGAP 959
Cdd:pfam00041   80 GEGPP 84

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  369 FQKKLEPAyQVSKGHKIRLTVEL-ADPDAEVRWLKNGQEIQmSGSKYIFESIGAKRTLTISQCSLADDAAYQCVV----G 443
Cdd:pfam07679    3 FTQKPKDV-EVQEGESARFTCTVtGTPDPEVSWFKDGQPLR-SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnsaG 80

                           90
                   ....*....|
gi 1825953459  444 GEKCSTELFV 453
Cdd:pfam07679   81 EAEASAELTV 90

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  980 PRHLRQTIQKKVRE--PVNLLIPFQGKPRPQVTWTKEGQPLA-GEEVSVRNSPTDTILFIRAARRAHSGTYqvTVRIENM 1056
Cdd:pfam07679    1 PKFTQKPKDVEVQEgeSARFTCTVTGTPDPEVSWFKDGQPLRsSDRFKVTYEGGTYTLTISNVQPDDSGKY--TCVATNS 78

                           90
                   ....*....|..
gi 1825953459 1057 --EDEATLVLQV 1066
Cdd:pfam07679   79 agEAEASAELTV 90

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459   165 PQDGEVTVGGSITFSARVAGASllkPPVVKWFKGKWVDLSSKvgQHLQLHDSYDRASkvylfeLHITDAQPAFTGGYRCE 244
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSP---PPEVTWYKQGGKLLAES--GRFSVSRSGSTST------LTISNVTPEDSGTYTCA 69

                            90
                    ....*....|....*.
gi 1825953459   245 VSTKDKFDCSNFNLTV 260
Cdd:smart00410   70 ATNSSGSASSGTTLTV 85

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

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1825953459   557 DLTVGAKDQAVFKCEVS-DENVRGVWLKNGKELL-PDSRIKVSHIGRVHKLTIDDVTPADEADY 618
Cdd:smart00410    3 SVTVKEGESVTLSCEASgSPPPEVTWYKQGGKLLaESGRFSVSRSGSTSTLTISNVTPEDSGTY 66

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459   465 EDQLVMVGQRVEFECEVS-EEGAQVKWLKDGVELTREETfKYRFKKDGRRHRLIINEATLEDTGHY--ALRTSGGQ--AL 539
Cdd:smart00410    2 PSVTVKEGESVTLSCEASgSPPPEVTWYKQGGKLLAESG-RFSVSRSGSTSTLTISNVTPEDSGTYtcAATNSSGSasSG 80

                    ....*
gi 1825953459   540 AELIV 544
Cdd:smart00410   81 TTLTV 85

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  161 FVMRPQDGEVTVGGSITFSARVAGASllkPPVVKWFKGkwvDLSSKVGQHLQLHDSYDRASkvylfeLHITDAQPAFTGG 240
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTP---DPEVSWFKD---GQPLRSSDRFKVTYEGGTYT------LTISNVQPDDSGK 70

                           90       100
                   ....*....|....*....|
gi 1825953459  241 YRCEVSTKDKFDCSNFNLTV 260
Cdd:pfam07679   71 YTCVATNSAGEAEASAELTV 90

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1825953459  566 AVFKCEVS-DENVRGVWLKNGKELLPDSRIKVSHIGRVHKLTIDDVTPADEADYS 619
Cdd:cd00096      1 VTLTCSASgNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYT 55

Immunoglobulin Domain C1 of human cardiac Myosin Binding Protein C and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain C1 of human cardiac Myosin Binding Protein C (MyBP-C). MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. 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 C1 domain of the MyBP-C 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  160 LFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTG 239
Cdd:cd20962      1 LFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFAG 80

                           90       100
                   ....*....|....*....|.
gi 1825953459  240 GYRCEVSTKDKFDCSNFNLTV 260
Cdd:cd20962     81 GYRCEVSTKDKFDCSNFNLTV 101

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. 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 Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  371 KKLEPAYQVSKGHKIRLTVELADPDAEVRWLKNGQEIQMSgSKYIFESIGAKRTLTISQCSLADDAAYQCVVGGEKCSTE 450
Cdd:cd20967      1 KKAQPAVQVSKGHKIRLTVELADPDAEVKWYKDGQELQSS-SKVIFESIGAKRTLTVQQASLADAGEYQCVAGGEKCSFE 79

                   ...
gi 1825953459  451 LFV 453
Cdd:cd20967     80 LFV 82

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459 1185 PSFTQPLVNRSVIAGYTTMLCCAVRGSPKPKISWFKNGLDLGEDARFRMFSKQGVLTLEIRKPCPFDGGIYVCRATNLQG 1264
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAG 80

                           90
                   ....*....|
gi 1825953459 1265 EAQCECRLEV 1274
Cdd:pfam07679   81 EAEASAELTV 90

Fibronectin type 3 domain [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  753 YTVTVKNPVGEDRVNLTVKVIDVPDAPAAP---KVSNVGEDSCTVQWEPPAYDGgqpVLGYILERKKKKSYRWMRLNFdl 829
Cdd:COG3401    207 YRVAATDTGGESAPSNEVSVTTPTTPPSAPtglTATADTPGSVTLSWDPVTESD---ATGYRVYRSNSGDGPFTKVAT-- 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  830 IQELSHEARRMIEGVVYEMRVYAVNAIG-MSRPSPASQPFMPIGPPSEPTHLAVEDVSDTTVSLKWRPperVGAGGLDGY 908
Cdd:COG3401    282 VTTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTA---SSDADVTGY 358

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1825953459  909 SVEYCPEGCSEWVTALRGLTEhTSILVKDLPTGARLLFRVRAHNMAG----PGAPVT-TTEPVTVQEILQRP 975
Cdd:COG3401    359 NVYRSTSGGGTYTKIAETVTT-TSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSaTTASAASGESLTAS 429

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  874 PSEPTHLAVEDVSDTTVSLKWRPPERVGaGGLDGYSVEYCPEGCSEWVTALRGLTEHTSILVKDLPTGARLLFRVRAHNM 953
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|....
gi 1825953459  954 AGPGAPVTTTEPVT 967
Cdd:cd00063     80 GGESPPSESVTVTT 93

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459 1188 TQPLVNRSVIAGYTTMLCCAVRGSPKPKISWFKNGLDLGEDARFRM-FSKQGVLTLEIRKPCPFDGGIYVCRATNLQGEA 1266
Cdd:cd20973      1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                   ....*...
gi 1825953459 1267 QCECRLEV 1274
Cdd:cd20973     81 TCSAELTV 88

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1825953459 1204 LCCAVRGSPKPKISWFKNGLDLGEDARFRMFSKQGVLTLEIRKPCPFDGGIYVCRATNLQGEAQ 1267
Cdd:cd00096      3 LTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459  460 ITRPLEDQLVMVGQRVEFECEVSEEGA-QVKWLKDGVELTreETFKYRFKKDGRRHRLIINEATLEDTGHYALRT--SGG 536
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDpEVSWFKDGQPLR--SSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVAtnSAG 80

                   ....*....
gi 1825953459  537 QALAELIVQ 545
Cdd:pfam07679   81 EAEASAELT 89

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459 1185 PSFTQPLVNRSVIAGYTTMLCCAVRGSPKPKISWFKNGLDLGEDARFRMFSKQ-GVLTLEIRKPCPFDGGIYVCRATNLQ 1263
Cdd:cd05744      1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVREnGRHSLIIEPVTKRDAGIYTCIARNRA 80

                           90
                   ....*....|.
gi 1825953459 1264 GEAQCECRLEV 1274
Cdd:cd05744     81 GENSFNAELVV 91

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825953459   776 PDAPAAPKVSNVGEDSCTVQWEPPAYDGGQ-PVLGYILERKKKKSyRWMRLNFDlIQELSHEARRMIEGVVYEMRVYAVN 854
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGS-EWKEVNVT-PSSTSYTLTGLKPGTEYEFRVRAVN 78