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 6093459  190 TYIRQVGESVNLQIPFQGKPKPQASWTHNGHALD-SQRVNVRSGDQDSILFIRSAQRSDSGRYELTVRLEGLEAKAAIDI 268
Cdd:cd05748   1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                ..
gi 6093459  269 LV 270
Cdd:cd05748  81 KV 82

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 6093459      78 PSAPLQLTLEDVSHSSLTVSWEPPEDLGSWGSRAMCWSSVREGASEWVPVNPRPVmVTQQTVRNLALGDKFFLRVTAVNS 157
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 6093459     158 AGAG 161
Cdd:smart00060  80 AGEG 83

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6093459      5 ATPEASVSTSEGTAPEPAKVPTPEPSGQVAASESTGQEQAPEPQKQPQAQDPAAHEAPATPATTKPEAPSEDVPSAPLQ 83
Cdd:PRK12270   40 STAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

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 6093459  190 TYIRQVGESVNLQIPFQGKPKPQASWTHNGHALD-SQRVNVRSGDQDSILFIRSAQRSDSGRYELTVRLEGLEAKAAIDI 268
Cdd:cd05748   1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                ..
gi 6093459  269 LV 270
Cdd:cd05748  81 KV 82

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 6093459  392 TQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQGDPKYRAV-SEQGVCTLEIRKPSPFDSGVYTCKAINVLGEP 470
Cdd:cd20973   1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                ....*...
gi 6093459  471 AVDCRLEV 478
Cdd:cd20973  81 TCSAELTV 88

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 6093459      78 PSAPLQLTLEDVSHSSLTVSWEPPEDLGSWGSRAMCWSSVREGASEWVPVNPRPVmVTQQTVRNLALGDKFFLRVTAVNS 157
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPS-STSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 6093459     158 AGAG 161
Cdd:smart00060  80 AGEG 83

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 6093459  274 PGPPSSIKLLDVWGCNAALEWMPPQDTGnTELLGYTVQKADKKTGQWFTVLERYHPTT-CTVSDLIIGNSYSFRVFSENL 352
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEVTPGSETsYTLTGLKPGTEYEFRVRAVNG 79

                        90
                ....*....|
gi 6093459  353 CGLSDLATTT 362
Cdd:cd00063  80 GGESPPSESV 89

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 6093459     274 PGPPSSIKLLDVWGCNAALEWMPPQDTGNTE-LLGYTVQKaDKKTGQWFTVLERYHPTTCTVSDLIIGNSYSFRVFSENL 352
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEY-REEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 6093459     353 CGLS 356
Cdd:smart00060  80 AGEG 83

Fibronectin type III domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459     79 SAPLQLTLEDVSHSSLTVSWEPPEDLGS--WGSRAMCWSSVREGASEWVPVNPRPVMVtqqTVRNLALGDKFFLRVTAVN 156
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpiTGYEVEYRPKNSGEPWNEITVPGTTTSV---TLTGLKPGTEYEVRVQAVN 77

                  ....*..
gi 6093459    157 SAGAGPP 163
Cdd:pfam00041  78 GGGEGPP 84

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6093459      5 ATPEASVSTSEGTAPEPAKVPTPEPSGQVAASESTGQEQAPEPQKQPQAQDPAAHEAPATPATTKPEAPSEDVPSAPLQ 83
Cdd:PRK12270   40 STAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459      3 GKATPEASVSTSEGTAPEPAKVPTPEPsgQVAASESTGQEQAPEPQKQPQAQDPAAHEAPATPATtkPEAPSEDVPSAPL 82
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA--AALPPAASPAGPL 2828

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459     83 QLTLEDVSHSSLTVSWEPPEDLGSWGSRAMCWSSVREGASEWVPvnPRPVMVTQQTVRNLAlgdkfflrvtavnsAGAGP 162
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPA--AKPAAPARPPVRRLA--------------RPAVS 2892

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6093459    163 PAVLDQPVHIQEITEAPKIRVPRHLRQTYIRQVGESVNLQIPFQGKPKPQAS 214
Cdd:PHA03247 2893 RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944

Uncharacterized membrane protein [Function unknown];

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6093459   15 EGTAPEPAKVPTPEPSGQVAASEST-GQEQAPEPQKQPQAQDPAAHEAPATPATTKPEAPSEdVPSAPLQLT 85
Cdd:COG5373  38 AEAAEAASAPAEPEPEAAAAATAAApEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEAEPAA-APAAASSFE 108

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 6093459  190 TYIRQVGESVNLQIPFQGKPKPQASWTHNGHALD-SQRVNVRSGDQDSILFIRSAQRSDSGRYELTVRLEGLEAKAAIDI 268
Cdd:cd05748   1 TIVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKeTGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80

                ..
gi 6093459  269 LV 270
Cdd:cd05748  81 KV 82

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 6093459  392 TQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQGDPKYRAV-SEQGVCTLEIRKPSPFDSGVYTCKAINVLGEP 470
Cdd:cd20973   1 IQTLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDqDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEA 80

                ....*...
gi 6093459  471 AVDCRLEV 478
Cdd:cd20973  81 TCSAELTV 88

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6093459    388 PPSFTQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQGDPKYRAVSEQGVCTLEIRKPSPFDSGVYTCKAIN 465
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6093459    194 QVGESVNLQIPFQGKPKPQASWTHNGHAL-DSQRVNVRSGDQDSILFIRSAQRSDSGRYELTVRLEGLEAKAAI 266
Cdd:pfam07679  13 QEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASA 86

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459     189 QTYIRQVGESVNLQIPFQGKPKPQASWTHNGHAL--DSQRVNVRSGDQDSILFIRSAQRSDSGRYELTVRLEGLEAKAAI 266
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 6093459     267 DILV 270
Cdd:smart00410  82 TLTV 85

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 6093459  389 PSFTQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQGDPKY-RAVSEQGVCTLEIRKPSPFDSGVYTCKAINVL 467
Cdd:cd05744   1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHkMLVRENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                        90
                ....*....|.
gi 6093459  468 GEPAVDCRLEV 478
Cdd:cd05744  81 GENSFNAELVV 91

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 6093459  274 PGPPSSIKLLDVWGCNAALEWMPPQDTGnTELLGYTVQKADKKTGQWFTVLERYHPTT-CTVSDLIIGNSYSFRVFSENL 352
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKGSGDWKEVEVTPGSETsYTLTGLKPGTEYEFRVRAVNG 79

                        90
                ....*....|
gi 6093459  353 CGLSDLATTT 362
Cdd:cd00063  80 GGESPPSESV 89

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 6093459     274 PGPPSSIKLLDVWGCNAALEWMPPQDTGNTE-LLGYTVQKaDKKTGQWFTVLERYHPTTCTVSDLIIGNSYSFRVFSENL 352
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEY-REEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

                   ....
gi 6093459     353 CGLS 356
Cdd:smart00060  80 AGEG 83

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459  388 PPSFTQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQGDPKYRAVSEQGVCTLEIRKPSPFDSGVYTCKAINVL 467
Cdd:cd20972   1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                .
gi 6093459  468 G 468
Cdd:cd20972  81 G 81

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6093459    179 PKIRVPRhlrQTYIRQVGESVNLQIPFQGKPKPQASWTHNGHALDSQRVNVRSGDQD-SILFIRSAQRSDSGRYELTVR 256
Cdd:pfam13927   2 PVITVSP---SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSnSTLTISNVTRSDAGTYTCVAS 77

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6093459  196 GESVNLQIPFQGKPKPQASWTHNGHAL--DSQRVNVRSGDQDSILFIRSAQRSDSGRYELTVRLEGLEAKAAIDILV 270
Cdd:cd05894  10 GNKLRLDVPISGEPAPTVTWSRGDKAFtaTEGRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86

Fibronectin type III domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6093459    275 GPPSSIKLLDVWGCNAALEWMPPqDTGNTELLGYTVQKADKKTGQ-WFTVLERYHPTTCTVSDLIIGNSYSFRVFSEN 351
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

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 6093459  199 VNLQIPFQGKPKPQASWTHNGHALD-SQRVNVRSGDQDSILFIRSAQRSDSGRYELTVR 256
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPpSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59

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

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459  391 FTQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQG-DPKYRAVsEQGvcTLEIRKPSPFDSGVYTCKAINVLGE 469
Cdd:cd20952   2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGkDERITTL-ENG--SLQIKGAEKSDTGEYTCVALNLSGE 78

                ....*....
gi 6093459  470 PAVDCRLEV 478
Cdd:cd20952  79 ATWSAVLDV 87

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459  390 SFTQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQ-GDPKYRaVSEQGVcTLEIRKPSPFDSGVYTCKAINVLG 468
Cdd:cd20970   4 STPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIeFNTRYI-VRENGT-TLTIRNIRRSDMGIYLCIASNGVP 81

                        90
                ....*....|.
gi 6093459  469 ePAVDCRLEVK 479
Cdd:cd20970  82 -GSVEKRITLQ 91

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

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                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6093459  410 CSVRASPKPKIIWMKNKMSIQGDPKYrAVSEQGvcTLEIRKPSPFDSGVYTCKAINVLG 468
Cdd:cd04969  24 CKPKASPKPTISWSKGTELLTNSSRI-CILPDG--SLKIKNVTKSDEGKYTCFAVNFFG 79

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459  390 SFTQPVADRTSTPGYSTQLFCSVRASPKPKIIWMKN----KMSIQGDPKYRAVSEqgvcTLEIRKPSPFDSGVYTCKAIN 465
Cdd:cd20949   1 TFTENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNgqpiSASVADMSKYRILAD----GLLINKVTQDDTGEYTCRAYQ 76

                ...
gi 6093459  466 VLG 468
Cdd:cd20949  77 VNS 79

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.

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gi 6093459  399 TSTPGYSTQLFCSVRASPKPKIIWMKNKMSIQGDPKYRAVSEQGVcTLEIRKPSPFDSGVYTCKAINVLG 468
Cdd:cd04978  10 VLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGR-TLIFSNLQPNDTAVYQCNASNVHG 78

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093459  407 QLFCSVRASPKPKIIWMKNKMSIQGDPKYRaVSEQGvcTLEIRKPSPFDSGVYTCKAINVLGEPAVDCRL 476
Cdd:cd05746   2 QIPCSAQGDPEPTITWNKDGVQVTESGKFH-ISPEG--YLAIRDVGVADQGRYECVARNTIGYASVSMVL 68

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.