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 168480100  293 PYLVKHPESRV-REAGQNVTFCCKASGTPMPKkYSWFHNGTLLDRR------QQGSgphLELQGLHQAQAGEYHCKAWNE 365
Cdd:cd20978     1 PKFIQKPEKNVvVKGGQDVTLPCQVTGVPQPK-ITWLHNGKPLQGPmeratvEDGT---LTIINVQPEDTGYYGCVATNE 76

                          90
                  ....*....|
gi 168480100  366 AGTVRSRAAL 375
Cdd:cd20978    77 IGDIYTETLL 86

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  512 IEVPPatERLVVTFVDPSGDFVDSVRVLPFDPRGAGvyhEIRALRKAAAVLldAERGGEIPLGSTEEAPALGELVLPPGT 591
Cdd:COG3321   795 LEVGP--GPVLTGLVRQCLAAAGDAVVLPSLRRGED---ELAQLLTALAQL--WVAGVPVDWSALYPGRGRRRVPLPTYP 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  592 FHHPDGRPYTGPVEARVTFVDPRDLASASAASSDLRFLDSAGELAPLRTYGMFAVDLRAPGSTEQLHVARADVHVDADHV 671
Cdd:COG3321   868 FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAA 947

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  672 RMPGHAEALALWSLDPETGLWEEEGSEQGSGGFRRETAAARVRREERAFLVGALTMRERRLFNLDVPERRRCFVKVR--- 748
Cdd:COG3321   948 AAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALaal 1027

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  749 -AYGTDRFAPAEQVQGVVVTLLNLEPAPGFTANPRAWGRFDSAVTGPNGACVPAFCDAEKPDAYTAFVTAALGGEELEAA 827
Cdd:COG3321  1028 lAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALL 1107

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  828 PSRPRATAAVVGVAQPYLERLGYQRTDHDDPALKRTGFRLNLARPRAGHESEAHGPVYPWRRLRDCEDAPVTDSHFRFSR 907
Cdd:COG3321  1108 LLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAA 1187

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  908 VEADKYEYDVVPFHEGAPASWTGDLLAWWPNPQEFRACFLKVRLQGPQEYMVRSHNAGGTHEATRGRLYGLRDTRSVRHP 987
Cdd:COG3321  1188 ALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAA 1267

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168480100  988 ERPGASAACVEFK--CGGMLFDQRQVDRTLVTVTPQGSCRRVAVNTLLQDYLARHPPLAAADDPAAFAMLAPLDALG 1062
Cdd:COG3321  1268 AAGLAALAAAAAAaaAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALA 1344

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  293 PYLVKHPESRV-REAGQNVTFCCKASGTPMPKkYSWFHNGTLLDRR------QQGSgphLELQGLHQAQAGEYHCKAWNE 365
Cdd:cd20978     1 PKFIQKPEKNVvVKGGQDVTLPCQVTGVPQPK-ITWLHNGKPLQGPmeratvEDGT---LTIINVQPEDTGYYGCVATNE 76

                          90
                  ....*....|
gi 168480100  366 AGTVRSRAAL 375
Cdd:cd20978    77 IGDIYTETLL 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 168480100    299 PESRVREAGQNVTFCCKASGTPMPKkYSWFHNGTLL----DR---RQQGSGPHLELQGLHQAQAGEYHCKAWNEAGTVRS 371
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPE-VTWYKQGGKLlaesGRfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....
gi 168480100    372 RAAL 375
Cdd:smart00410   80 GTTL 83

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  512 IEVPPatERLVVTFVDPSGDFVDSVRVLPFDPRGAGvyhEIRALRKAAAVLldAERGGEIPLGSTEEAPALGELVLPPGT 591
Cdd:COG3321   795 LEVGP--GPVLTGLVRQCLAAAGDAVVLPSLRRGED---ELAQLLTALAQL--WVAGVPVDWSALYPGRGRRRVPLPTYP 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  592 FHHPDGRPYTGPVEARVTFVDPRDLASASAASSDLRFLDSAGELAPLRTYGMFAVDLRAPGSTEQLHVARADVHVDADHV 671
Cdd:COG3321   868 FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAA 947

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  672 RMPGHAEALALWSLDPETGLWEEEGSEQGSGGFRRETAAARVRREERAFLVGALTMRERRLFNLDVPERRRCFVKVR--- 748
Cdd:COG3321   948 AAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALaal 1027

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  749 -AYGTDRFAPAEQVQGVVVTLLNLEPAPGFTANPRAWGRFDSAVTGPNGACVPAFCDAEKPDAYTAFVTAALGGEELEAA 827
Cdd:COG3321  1028 lAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALL 1107

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  828 PSRPRATAAVVGVAQPYLERLGYQRTDHDDPALKRTGFRLNLARPRAGHESEAHGPVYPWRRLRDCEDAPVTDSHFRFSR 907
Cdd:COG3321  1108 LLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAA 1187

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  908 VEADKYEYDVVPFHEGAPASWTGDLLAWWPNPQEFRACFLKVRLQGPQEYMVRSHNAGGTHEATRGRLYGLRDTRSVRHP 987
Cdd:COG3321  1188 ALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAA 1267

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168480100  988 ERPGASAACVEFK--CGGMLFDQRQVDRTLVTVTPQGSCRRVAVNTLLQDYLARHPPLAAADDPAAFAMLAPLDALG 1062
Cdd:COG3321  1268 AAGLAALAAAAAAaaAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALA 1344

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  293 PYLVKHPESRV-REAGQNVTFCCKASGTPMPKkYSWFHNGTLLDRR------QQGSgphLELQGLHQAQAGEYHCKAWNE 365
Cdd:cd20978     1 PKFIQKPEKNVvVKGGQDVTLPCQVTGVPQPK-ITWLHNGKPLQGPmeratvEDGT---LTIINVQPEDTGYYGCVATNE 76

                          90
                  ....*....|
gi 168480100  366 AGTVRSRAAL 375
Cdd:cd20978    77 IGDIYTETLL 86

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100   293 PYLVKHPESRVREAGQNVTFCCKASGTPMPKkYSWFHNGTLL--DRR----QQGSGPHLELQGLHQAQAGEYHCKAWNEA 366
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPE-VSWFKDGQPLrsSDRfkvtYEGGTYTLTISNVQPDDSGKYTCVATNSA 79

                   ....*....
gi 168480100   367 GTVRSRAAL 375
Cdd:pfam07679   80 GEAEASAEL 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 168480100  310 VTFCCKASGTPMPKkYSWFHNGTLL------DRRQQGSGPHLELQGLHQAQAGEYHCKAWNEAGTVRSRAA 374
Cdd:cd00096     1 VTLTCSASGNPPPT-ITWYKNGKPLppssrdSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70

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 168480100  293 PYLVKHPESRVREAGQNVTFCCKASGTPMPkKYSWFHNGTLL------DRRQQGSGPH-LELQGLHQAQAGEYHCKAWNE 365
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTP-DLFWQLNGKPVrpdsahKMLVRENGRHsLIIEPVTKRDAGIYTCIARNR 79

                          90
                  ....*....|
gi 168480100  366 AGTVRSRAAL 375
Cdd:cd05744    80 AGENSFNAEL 89

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 168480100  303 VREaGQNVTFCCKASGTPMPkKYSWFHNGTLLDRRQQG-----SGPHLELQGLHQAQAGEYHCKAWNEA-GTVRSRAAL 375
Cdd:cd20970    14 ARE-GENATFMCRAEGSPEP-EISWTRNGNLIIEFNTRyivreNGTTLTIRNIRRSDMGIYLCIASNGVpGSVEKRITL 90

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100   292 KPYLVKHPeSRVREaGQNVTFCCKASGTPMPKkYSWFHNGTLLDRRQQGSGPHLELQglhqaQAGEYHCKAWNEAGTVRS 371
Cdd:pfam13895    1 KPVLTPSP-TVVTE-GEPVTLTCSAPGNPPPS-YTWYKDGSAISSSPNFFTLSVSAE-----DSGTYTCVARNGRGGKVS 72

                   ....*..
gi 168480100   372 RAALLTI 378
Cdd:pfam13895   73 NPVELTV 79

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  295 LVKHPESRVREAGQNVTFCCKASGTPMPKkYSWFHNGTLL---DRR----QQGSgphLELQGLHQAQAGEYHCKAWNEAG 367
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPT-ISWLKDGVPLlgkDERittlENGS---LQIKGAEKSDTGEYTCVALNLSG 77

                  ....*...
gi 168480100  368 TVRSRAAL 375
Cdd:cd20952    78 EATWSAVL 85

Second immunoglobulin (Ig)-like domain of Axl/Tyro3 family receptor tyrosine kinases (RTKs); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in 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, lymphatic and vascular systems, and 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  294 YLVKHPESRVREAGQNVTFCCKASGTPMPKKYSWFHNGTLLDRRQQGSGPHLELQGLHQAQAgeYHCKAWNEAGTVRSRA 373
Cdd:cd05749     1 HFTVEPEDLAVTANTPFNLTCQAVGPPEPVEILWWQGGSPLGGPPAPSPSVLNVPGLNETTK--FSCEAHNAKGLTSSRT 78

                  ....
gi 168480100  374 ALLT 377
Cdd:cd05749    79 ATVT 82

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 168480100  307 GQNVTFCCKASGTPMPkKYSWFHNGTLL--DRRQQ--GSGPhLELQGLHQAQAGEYHCKAWNEAGTVRSRAAL 375
Cdd:cd05745     2 GQTVDFLCEAQGYPQP-VIAWTKGGSQLsvDRRHLvlSSGT-LRISRVALHDQGQYECQAVNIVGSQRTVAQL 72

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 168480100  310 VTFCCKASGTPMPKkYSWFHNGTLLD-----RRQQGSGPHLELQGLHQAQAGEYHCKAWNEAGTVRSRAALL 376
Cdd:cd04967    22 VALNCRARANPVPS-YRWLMNGTEIDlesdyRYSLVDGTLVISNPSKAKDAGHYQCLATNTVGSVLSREATL 92

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 168480100  307 GQNVTFCCKASGTPMPKkYSWFHNGTLL----DRRQQGSG-PHLELQGLHQAQAGEYHCKAWNEAGTVRSRAAL 375
Cdd:cd20976    16 GQDFVAQCSARGKPVPR-ITWIRNAQPLqyaaDRSTCEAGvGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWV 88

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 168480100  308 QNVTFCCKASGTPMPKkYSWFHNGTLLD-----RRQQGSGPHLELQGLHQAQAGEYHCKAWNEAGTVRSRAALL 376
Cdd:cd05848    20 KKVILNCEARGNPVPT-YRWLRNGTEIDtesdyRYSLIDGNLIISNPSEVKDSGRYQCLATNSIGSILSREALL 92

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  294 YLVKHPESRVREAGQNVTFCCKASGTPMPkKYSWFHNGTLL-----DRRQQGSGPHLELQGLHQAQAGEYHCKAWNEAGT 368
Cdd:cd05868     1 YWITAPTNLVLSPGEDGTLICRANGNPKP-SISWLTNGVPIeiaptDPSRKVDGDTIIFSKVQERSSAVYQCNASNEYGY 79

                  ....*
gi 168480100  369 VRSRA 373
Cdd:cd05868    80 LLANA 84

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  298 HPESRVREAGQNVTFCCKASGTP-MPKKYSWFHNGTLLD--------RRQQG--SGPHLELQGLHQAQAGEYHCKAWNEA 366
Cdd:cd04970     8 APSNADITVGENATLQCHASHDPtLDLTFTWSFNGVPIDlekieghyRRRYGkdSNGDLEIVNAQLKHAGRYTCTAQTVV 87

                          90
                  ....*....|....*
gi 168480100  367 GTVRSrAALLTILAP 381
Cdd:cd04970    88 DSDSA-SATLVVRGP 101

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  299 PESRVREAGQNVTFCCKASGTPmPKKYSWFHNGTLldrrqQGSGPHLELQGLHQAQAGEYHCKAWNEAGT 368
Cdd:cd20948     2 PSDTYYLSGENLNLSCHAASNP-PAQYSWTINGTF-----QTSSQELFLPAITENNEGTYTCSAHNSLTG 65

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 168480100  307 GQNVTFCCKASGTPMPKKYSWFHNGTLLdrrqQGSGPHLELQGLHQAQAGEYHCKA 362
Cdd:cd05752    15 GEKVTLTCQGFYSPEQNSTQWYHNGTLI----SSTSSSYRIVAATVNDSGEYRCQT 66

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  306 AGQNVTFCCKASGTPMpKKYSWFHNGTLL--DRRQQ----GSgphLELQGLHQAQ-AGEYHCKAWNEAGTVRSRAALLTI 378
Cdd:cd20958    14 AGQTLRLHCPVAGYPI-SSITWEKDGRRLplNHRQRvfpnGT---LVIENVQRSSdEGEYTCTARNQQGQSASRSVFVKV 89

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  294 YLVKHPESRVREAGQNVTFCCKASGTPMPkKYSWFHNGTLL-----DRRQQGSGPHLELQGLHQAQAGEYHCKAWNEAGT 368
Cdd:cd04978     1 YWIIEPPSLVLSPGETGELICEAEGNPQP-TITWRLNGVPIepapeDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGY 79

                  ....*..
gi 168480100  369 VRSRAAL 375
Cdd:cd04978    80 LLANAFL 86

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  512 IEVPPatERLVVTFVDPSGDFVDSVRVLPFDPRGAGvyhEIRALRKAAAVLldAERGGEIPLGSTEEAPALGELVLPPGT 591
Cdd:COG3321   795 LEVGP--GPVLTGLVRQCLAAAGDAVVLPSLRRGED---ELAQLLTALAQL--WVAGVPVDWSALYPGRGRRRVPLPTYP 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  592 FHHPDGRPYTGPVEARVTFVDPRDLASASAASSDLRFLDSAGELAPLRTYGMFAVDLRAPGSTEQLHVARADVHVDADHV 671
Cdd:COG3321   868 FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAA 947

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  672 RMPGHAEALALWSLDPETGLWEEEGSEQGSGGFRRETAAARVRREERAFLVGALTMRERRLFNLDVPERRRCFVKVR--- 748
Cdd:COG3321   948 AAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALaal 1027

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  749 -AYGTDRFAPAEQVQGVVVTLLNLEPAPGFTANPRAWGRFDSAVTGPNGACVPAFCDAEKPDAYTAFVTAALGGEELEAA 827
Cdd:COG3321  1028 lAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALL 1107

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  828 PSRPRATAAVVGVAQPYLERLGYQRTDHDDPALKRTGFRLNLARPRAGHESEAHGPVYPWRRLRDCEDAPVTDSHFRFSR 907
Cdd:COG3321  1108 LLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAA 1187

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168480100  908 VEADKYEYDVVPFHEGAPASWTGDLLAWWPNPQEFRACFLKVRLQGPQEYMVRSHNAGGTHEATRGRLYGLRDTRSVRHP 987
Cdd:COG3321  1188 ALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAA 1267

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 168480100  988 ERPGASAACVEFK--CGGMLFDQRQVDRTLVTVTPQGSCRRVAVNTLLQDYLARHPPLAAADDPAAFAMLAPLDALG 1062
Cdd:COG3321  1268 AAGLAALAAAAAAaaAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALA 1344