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Conserved domains on  [gi|151301230|ref|NP_766488|]
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sialic acid-binding Ig-like lectin 10 isoform 1 precursor [Mus musculus]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 34076)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 22-134 6.70e-38

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


The actual alignment was detected with superfamily member cd05712:

Pssm-ID: 472250  Cd Length: 119  Bit Score: 136.75  E-value: 6.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  22 YFLQVQRIVKAQEGLCIFVPCSFSSPEGKWLNRsPLYGYWFKGIRKPSLSFPVATNNKDKVLEWEARGRFQLLGDISKKN 101
Cdd:cd05712    1 WGLQMPKSVTVQEGLCVLIPCSFSYPADYWVSN-PVHGYWYRGGPYPKYRPPVATNNRTREVHESTQGRFRLLGDPGKKN 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 151301230 102 CSLLIKDVQWGDSTNYFFRMERGFE-RFSFKEEF 134
Cdd:cd05712   80 CSLSISDARPEDSGKYFFRVERGDSnKYSYLSNQ 113
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 145-230 5.37e-21

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


The actual alignment was detected with superfamily member cd20987:

Pssm-ID: 472250  Cd Length: 94  Bit Score: 88.01  E-value: 5.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 145 PDIFIPEVLEPGEPVTVVCLFSWtfnQCPA--PSFSWMGDAVS-------FQESRPHTSNYSVLSFIPGLQHHDTELTCQ 215
Cdd:cd20987    1 PNIHVPEELEAGQEVTLTCSVPD---NCPAlsPEFSWLGAALTplppvlgRLEEEGTTTHSSVLTFTPRPEDHGTNLTCQ 77

                         90
                 ....*....|....*..
gi 151301230 216 LDFSR--MSTQRTVRLR 230
Cdd:cd20987   78 VKFPGatVTTERTIQLN 94
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 366-439 2.45e-12

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


The actual alignment was detected with superfamily member cd20948:

Pssm-ID: 472250  Cd Length: 76  Bit Score: 62.51  E-value: 2.45e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151301230 366 LEGQSLCLVCVTYSNPPANVSWAWvtqTLIPIQSSEpgVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSVHY 439
Cdd:cd20948    8 LSGENLNLSCHAASNPPAQYSWTI---NGTFQTSSQ--ELFLPAITENNEGTYTCSAHNSLTGKNISLVLSVTV 76
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 256-335 4.31e-12

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


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSS-----PVGSRTLaLELPWVKAGDSGHYTCQAENRLGSQQHT 330
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDrfkvtYEGGTYT-LTISNVQPDDSGKYTCVATNSAGEAEAS 85


                  ....*
gi 151301230  331 LDLSV 335
Cdd:pfam07679  86 AELTV 90
 
Name Accession Description Interval E-value
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 22-134 6.70e-38

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 136.75  E-value: 6.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  22 YFLQVQRIVKAQEGLCIFVPCSFSSPEGKWLNRsPLYGYWFKGIRKPSLSFPVATNNKDKVLEWEARGRFQLLGDISKKN 101
Cdd:cd05712    1 WGLQMPKSVTVQEGLCVLIPCSFSYPADYWVSN-PVHGYWYRGGPYPKYRPPVATNNRTREVHESTQGRFRLLGDPGKKN 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 151301230 102 CSLLIKDVQWGDSTNYFFRMERGFE-RFSFKEEF 134
Cdd:cd05712   80 CSLSISDARPEDSGKYFFRVERGDSnKYSYLSNQ 113
IgC2_CD33_d2_like cd20987
Second immunoglobulin domain of Cluster of Differentiation (CD) 33 and related Siglecs; member ...
 145-230 5.37e-21

Second immunoglobulin domain of Cluster of Differentiation (CD) 33 and related Siglecs; member of the C2-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 33 (also known as sialic-acid binding immunoglobulin type-lectin 3 (Siglec-3)) and related Siglecs. CD33, a Siglec family member, is a well-known immunotherapeutic target in acute myeloid leukemia (AML). It is an inhibitory sialoadhesin expressed in human leukocytes of the myeloid lineage and some lymphoid subsets, including natural killer (NK) cells. Siglecs are primarily expressed on immune cells and recognize sialic acid-containing glycan ligands. Siglecs are organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4, myelin-associated glycoprotein), the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11. CD33 (Siglec-3) is the smallest Siglec member. It preferentially binds to alpha2-6- and alpha2-3-sialylated glycans and strongly binds to sialylated ligands on leukemic cell lines. 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. This group includes CD33-related Siglecs which belong to the C2-set of IgSF domains. Unlike the C1-set, the C2-set structures do not have a D strand.


Pssm-ID: 409579  Cd Length: 94  Bit Score: 88.01  E-value: 5.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 145 PDIFIPEVLEPGEPVTVVCLFSWtfnQCPA--PSFSWMGDAVS-------FQESRPHTSNYSVLSFIPGLQHHDTELTCQ 215
Cdd:cd20987    1 PNIHVPEELEAGQEVTLTCSVPD---NCPAlsPEFSWLGAALTplppvlgRLEEEGTTTHSSVLTFTPRPEDHGTNLTCQ 77

                         90
                 ....*....|....*..
gi 151301230 216 LDFSR--MSTQRTVRLR 230
Cdd:cd20987   78 VKFPGatVTTERTIQLN 94
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 366-439 2.45e-12

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.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 62.51  E-value: 2.45e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151301230 366 LEGQSLCLVCVTYSNPPANVSWAWvtqTLIPIQSSEpgVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSVHY 439
Cdd:cd20948    8 LSGENLNLSCHAASNPPAQYSWTI---NGTFQTSSQ--ELFLPAITENNEGTYTCSAHNSLTGKNISLVLSVTV 76
I-set pfam07679
Immunoglobulin I-set domain;
256-335 4.31e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSS-----PVGSRTLaLELPWVKAGDSGHYTCQAENRLGSQQHT 330
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDrfkvtYEGGTYT-LTISNVQPDDSGKYTCVATNSAGEAEAS 85


                  ....*
gi 151301230  331 LDLSV 335
Cdd:pfam07679  86 AELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 256-335 4.87e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.44  E-value: 4.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230   256 PSHLEVQQGQSLRLLCTADSQPPATLSW-------VLEDQVLSWSSPvgSRTLALELPWVKAGDSGHYTCQAENRLGSQQ 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWykqggklLAESGRFSVSRS--GSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78


                   ....*..
gi 151301230   329 HTLDLSV 335
Cdd:smart00410  79 SGTTLTV 85
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 256-337 1.22e-09

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.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 55.20  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWvledqvlSWSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd20948    2 PSDTYYLSGENLNLSCHAASNPPAQYSW-------TINGTFQTSSQELFLPAITENNEGTYTCSAHNSLTGKNISLVLSV 74


                 ..
gi 151301230 336 LY 337
Cdd:cd20948   75 TV 76
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 25-138 2.98e-09

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 55.16  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230   25 QVQRIVKAQEGLCIFVPCSFSSpegkWLNRSPLYGYWFKGIRKPSLSFPVATNNKDKVLEwEARGRFQLLGDISKKNCSL 104
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSS----SMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEG-VKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 151301230  105 LIKDVQWGDSTNYFFRMeRGFERFSFKEEFRLQV 138
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 362-437 1.99e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.74  E-value: 1.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230   362 SLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIP-------IQSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLS 434
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAesgrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82


                   ...
gi 151301230   435 LSV 437
Cdd:smart00410  83 LTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 355-424 1.07e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.79  E-value: 1.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301230  355 EILRNAISLPVLEGQSLCLVCVTYSNPPANVSW------AWVTQTLIPIQSSEPGVLELPLVQREHEGEFTCAAQN 424
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWykngepISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
 
Name Accession Description Interval E-value
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 22-134 6.70e-38

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 136.75  E-value: 6.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  22 YFLQVQRIVKAQEGLCIFVPCSFSSPEGKWLNRsPLYGYWFKGIRKPSLSFPVATNNKDKVLEWEARGRFQLLGDISKKN 101
Cdd:cd05712    1 WGLQMPKSVTVQEGLCVLIPCSFSYPADYWVSN-PVHGYWYRGGPYPKYRPPVATNNRTREVHESTQGRFRLLGDPGKKN 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 151301230 102 CSLLIKDVQWGDSTNYFFRMERGFE-RFSFKEEF 134
Cdd:cd05712   80 CSLSISDARPEDSGKYFFRVERGDSnKYSYLSNQ 113
IgC2_CD33_d2_like cd20987
Second immunoglobulin domain of Cluster of Differentiation (CD) 33 and related Siglecs; member ...
 145-230 5.37e-21

Second immunoglobulin domain of Cluster of Differentiation (CD) 33 and related Siglecs; member of the C2-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 33 (also known as sialic-acid binding immunoglobulin type-lectin 3 (Siglec-3)) and related Siglecs. CD33, a Siglec family member, is a well-known immunotherapeutic target in acute myeloid leukemia (AML). It is an inhibitory sialoadhesin expressed in human leukocytes of the myeloid lineage and some lymphoid subsets, including natural killer (NK) cells. Siglecs are primarily expressed on immune cells and recognize sialic acid-containing glycan ligands. Siglecs are organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4, myelin-associated glycoprotein), the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11. CD33 (Siglec-3) is the smallest Siglec member. It preferentially binds to alpha2-6- and alpha2-3-sialylated glycans and strongly binds to sialylated ligands on leukemic cell lines. 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. This group includes CD33-related Siglecs which belong to the C2-set of IgSF domains. Unlike the C1-set, the C2-set structures do not have a D strand.


Pssm-ID: 409579  Cd Length: 94  Bit Score: 88.01  E-value: 5.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 145 PDIFIPEVLEPGEPVTVVCLFSWtfnQCPA--PSFSWMGDAVS-------FQESRPHTSNYSVLSFIPGLQHHDTELTCQ 215
Cdd:cd20987    1 PNIHVPEELEAGQEVTLTCSVPD---NCPAlsPEFSWLGAALTplppvlgRLEEEGTTTHSSVLTFTPRPEDHGTNLTCQ 77

                         90
                 ....*....|....*..
gi 151301230 216 LDFSR--MSTQRTVRLR 230
Cdd:cd20987   78 VKFPGatVTTERTIQLN 94
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 366-439 2.45e-12

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.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 62.51  E-value: 2.45e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151301230 366 LEGQSLCLVCVTYSNPPANVSWAWvtqTLIPIQSSEpgVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSVHY 439
Cdd:cd20948    8 LSGENLNLSCHAASNPPAQYSWTI---NGTFQTSSQ--ELFLPAITENNEGTYTCSAHNSLTGKNISLVLSVTV 76
I-set pfam07679
Immunoglobulin I-set domain;
256-335 4.31e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 62.27  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSS-----PVGSRTLaLELPWVKAGDSGHYTCQAENRLGSQQHT 330
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDrfkvtYEGGTYT-LTISNVQPDDSGKYTCVATNSAGEAEAS 85


                  ....*
gi 151301230  331 LDLSV 335
Cdd:pfam07679  86 AELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 256-335 4.87e-11

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 59.44  E-value: 4.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230   256 PSHLEVQQGQSLRLLCTADSQPPATLSW-------VLEDQVLSWSSPvgSRTLALELPWVKAGDSGHYTCQAENRLGSQQ 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWykqggklLAESGRFSVSRS--GSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78


                   ....*..
gi 151301230   329 HTLDLSV 335
Cdd:smart00410  79 SGTTLTV 85
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 256-337 1.22e-09

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.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 55.20  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWvledqvlSWSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd20948    2 PSDTYYLSGENLNLSCHAASNPPAQYSW-------TINGTFQTSSQELFLPAITENNEGTYTCSAHNSLTGKNISLVLSV 74


                 ..
gi 151301230 336 LY 337
Cdd:cd20948   75 TV 76
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 25-138 2.98e-09

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 55.16  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230   25 QVQRIVKAQEGLCIFVPCSFSSpegkWLNRSPLYGYWFKGIRKPSLSFPVATNNKDKVLEwEARGRFQLLGDISKKNCSL 104
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSS----SMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEG-VKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 151301230  105 LIKDVQWGDSTNYFFRMeRGFERFSFKEEFRLQV 138
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTV 108
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 255-322 8.68e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.57  E-value: 8.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 151301230  255 NPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSS----PVGSRTLALELPWVKAGDSGHYTCQAEN 322
Cdd:pfam13927   7 SPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGStrsrSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 254-335 1.60e-08

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


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 52.33  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 254 ENPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSR----TLALELPWVKAGDSGHYTCQAENRLGSQQH 329
Cdd:cd20949    4 ENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKyrilADGLLINKVTQDDTGEYTCRAYQVNSIASD 83


                 ....*.
gi 151301230 330 TLDLSV 335
Cdd:cd20949   84 MQERTV 89
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 362-437 1.99e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.74  E-value: 1.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230   362 SLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIP-------IQSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLS 434
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAesgrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82


                   ...
gi 151301230   435 LSV 437
Cdd:smart00410  83 LTV 85
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 262-335 3.11e-08

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


Pssm-ID: 409551  Cd Length: 94  Bit Score: 51.72  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 262 QQGQSLRLLCT-ADSQPPATLSWVLEDQVLS-----WSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd20959   15 QVGMRAQLHCGvPGGDLPLNIRWTLDGQPISddlgiTVSRLGRRSSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 256-334 7.34e-08

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


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 50.43  E-value: 7.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTL----ALELPWVKAGDSGHYTCQAENRLGSQQHTL 331
Cdd:cd05747   10 PRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTeyksTFEISKVQMSDEGNYTVVVENSEGKQEAQF 89


                 ...
gi 151301230 332 DLS 334
Cdd:cd05747   90 TLT 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 267-330 1.04e-07

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.25  E-value: 1.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151301230 267 LRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTLA----LELPWVKAGDSGHYTCQAENRLGSQQHT 330
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELgngtLTISNVTLEDSGTYTCVASNSAGGSASA 68
IgV_CD22_d1 cd20929
First immunoglobulin domain of Cluster of Differentiation (CD) 22; member of the V-set of IgSF ...
 32-128 1.19e-07

First immunoglobulin domain of Cluster of Differentiation (CD) 22; member of the V-set of IgSF domains; The members here are composed of the first immunoglobulin domain in Cluster of Differentiation (CD) 22 (also known as Siglec-2). CD22, a sialic-acid binding immunoglobulin type-lectin (Siglec) family member, is an inhibitory co-receptor of the B-cell receptor (BCR). The inhibitory function of CD22 and its restricted expression on B cells makes CD22 an attractive target against dysregulated B cells that cause autoimmune diseases and B-cell-derived cancers. CD22 plays a vital role in establishing a baseline level of B-cell inhibition, and thus is an important determinant of homeostasis in humoral immunity. Siglecs are primarily expressed on immune cells and recognize sialic acid-containing glycan ligands. Siglecs are organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4, myelin-associated glycoprotein), the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11. 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 V-set of IgSF domains.


Pssm-ID: 409523  Cd Length: 114  Bit Score: 50.77  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  32 AQEGLCIFVPCSFSSPEGKWLNRSPLYGYWFKGIRKPSLSFPVATNNKDKVLEWEARgRFQLLGDiSKKNCSLLIKDVQW 111
Cdd:cd20929   11 AWEGACVWIPCTYRALDGDLESFILFHNPEYNKATSKFDGTRLYESTKDGKVPSEQK-RVQFLGD-KNKNCTLSIHPVHL 88

                         90
                 ....*....|....*..
gi 151301230 112 GDSTNYFFRMERGFERF 128
Cdd:cd20929   89 NDSGQLGLRMESKTEKW 105
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 257-335 1.35e-07

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 49.52  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 257 SHLEVQQGQSLRLLCTADSQPPATLSWV-LEDQVLSWSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05876    3 SSLVALRGQSLVLECIAEGLPTPTVKWLrPSGPLPPDRVKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 255-335 3.14e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.16  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  255 NPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTLALElpwvkagDSGHYTCQAENRLGSQQ-HTLDL 333
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPNFFTLSVSAE-------DSGTYTCVARNGRGGKVsNPVEL 77


                  ..
gi 151301230  334 SV 335
Cdd:pfam13895  78 TV 79
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 256-335 5.19e-07

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


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 47.78  E-value: 5.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLswssPVG-SRTLA---LELPWVKAGDSGHYTCQAENRLGSQQHTL 331
Cdd:cd05725    4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGEL----PKGrYEILDdhsLKIRKVTAGDMGSYTCVAENMVGKIEASA 79


                 ....
gi 151301230 332 DLSV 335
Cdd:cd05725   80 TLTV 83
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 362-438 8.14e-07

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 47.54  E-value: 8.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151301230 362 SLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIP--IQSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSVH 438
Cdd:cd04968   10 DTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSSqwEITTSEPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRIIVQ 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 355-424 1.07e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.79  E-value: 1.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301230  355 EILRNAISLPVLEGQSLCLVCVTYSNPPANVSW------AWVTQTLIPIQSSEPGVLELPLVQREHEGEFTCAAQN 424
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWykngepISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 250-335 2.98e-06

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 46.09  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 250 PDLHENPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWS---SPVGSRTLALELPWVKAGDSGHYTCQAENRLGS 326
Cdd:cd20976    2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAadrSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQ 81


                 ....*....
gi 151301230 327 QQHTLDLSV 335
Cdd:cd20976   82 VSCSAWVTV 90
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 261-335 3.74e-06

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 45.48  E-value: 3.74e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301230 261 VQQGQSLRLLCTADSQPPATLSWV-LEDQVLSWSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05731    7 VLRGGVLLLECIAEGLPTPDIRWIkLGGELPKGRTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 264-335 4.61e-06

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 45.67  E-value: 4.61e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151301230 264 GQSLRLLCTADSQPPATLSWvLEDQVLSWSSPVGSRTLALELPW------VKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05729   19 ANKVRLECGAGGNPMPNITW-LKDGKEFKKEHRIGGTKVEEKGWsliierAIPRDKGKYTCIVENEYGSINHTYDVDV 95
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 373-430 7.05e-06

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.24  E-value: 7.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151301230 373 LVCVTYSNPPANVSWAWVTQTLIPIQSSEP------GVLELPLVQREHEGEFTCAAQNPLGAQR 430
Cdd:cd00096    3 LTCSASGNPPPTITWYKNGKPLPPSSRDSRrselgnGTLTISNVTLEDSGTYTCVASNSAGGSA 66
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 259-328 7.10e-06

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 44.88  E-value: 7.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301230  259 LEVQQGQSLRLLCTA-DSQPPATLSWVLEDQVLSWSSPV-----GSRTLALELPWVKAGDSGHYTCQAENRLGSQQ 328
Cdd:pfam00047   6 VTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVkhdngRTTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 261-335 7.85e-06

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


Pssm-ID: 409561  Cd Length: 92  Bit Score: 44.69  E-value: 7.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151301230 261 VQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTL----ALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd20969   14 VDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVfpdgTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
IgC_CRIg cd16082
Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin ...
 261-330 9.01e-06

Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4)) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. 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 such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409504  Cd Length: 86  Bit Score: 44.36  E-value: 9.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 261 VQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTLALELPWVKAgDSGHYTCQAENRLGSQQHT 330
Cdd:cd16082   10 VPQGMRISLQCQAWGSPPISYVWYKEQTNNQEPIKVAALSTLLFKPAVVA-DSGSYFCTAKGRVGSEQRS 78
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 355-427 1.38e-05

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 43.77  E-value: 1.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151301230 355 EILRNAISLPVLEGQSLCLVCVTYSNPPANVSWAwVTQTLIP----IQSSEPGVLELPLVQREHEGEFTCAAQNPLG 427
Cdd:cd20968    1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWI-KGDDLIKennrIAVLESGSLRIHNVQKEDAGQYRCVAKNSLG 76
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 250-335 1.73e-05

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


Pssm-ID: 409582  Cd Length: 91  Bit Score: 43.94  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 250 PDLHENPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSP-------VGSRTLALELpwVKAGDSGHYTCQAEN 322
Cdd:cd20990    1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAhkmlvreNGVHSLIIEP--VTSRDAGIYTCIATN 78

                         90
                 ....*....|...
gi 151301230 323 RLGSQQHTLDLSV 335
Cdd:cd20990   79 RAGQNSFNLELVV 91
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 264-335 2.73e-05

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 43.31  E-value: 2.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151301230 264 GQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSR--TLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05856   19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKkkKWTLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 250-335 3.14e-05

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 42.83  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 250 PDLHENP--SHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSS-----PVGSrtlaLELPWVKAGDSGHYTCQAEN 322
Cdd:cd04969    1 PDFELNPvkKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSricilPDGS----LKIKNVTKSDEGKYTCFAVN 76

                         90
                 ....*....|...
gi 151301230 323 RLGSQQHTLDLSV 335
Cdd:cd04969   77 FFGKANSTGSLSV 89
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 256-335 4.10e-05

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


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 42.87  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPV-------GSRTLALELpwVKAGDSGHYTCQAENRLGSQQ 328
Cdd:cd05744    7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHkmlvrenGRHSLIIEP--VTKRDAGIYTCIARNRAGENS 84


                 ....*..
gi 151301230 329 HTLDLSV 335
Cdd:cd05744   85 FNAELVV 91
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 258-335 5.61e-05

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


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 42.08  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 258 HLEVQQGQSLRLLCTADSQPPATLSWVL-EDQVLSWSSpvgsRTLA-----LELPWVKAGDSGHYTCQAENRLGSQQHTL 331
Cdd:cd05764    9 ELRVLEGQRATLRCKARGDPEPAIHWISpEGKLISNSS----RTLVydngtLDILITTVKDTGAFTCIASNPAGEATARV 84


                 ....
gi 151301230 332 DLSV 335
Cdd:cd05764   85 ELHI 88
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 255-325 7.93e-05

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 41.67  E-value: 7.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151301230 255 NPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTL---ALELPWVKAGDSGHYTCQAENRLG 325
Cdd:cd04978    5 EPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVdgrTLIFSNLQPNDTAVYQCNASNVHG 78
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 256-335 9.11e-05

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.81  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPV-----GSRTLALELPWVKAGDSGHYTCQAENRLGSQQHT 330
Cdd:cd05737    8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCnlkveAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSD 87


                 ....*
gi 151301230 331 LDLSV 335
Cdd:cd05737   88 VTVSV 92
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 261-335 1.20e-04

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 41.38  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 261 VQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGS-----RTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05857   16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGykvrnQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 95
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 264-335 1.41e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 41.46  E-value: 1.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151301230 264 GQSLRLLCTADSQPPATLSWV-----LEDQVLSWS-SPVGSRTLALElpwVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05730   18 GQSVTLACDADGFPEPTMTWTkdgepIESGEEKYSfNEDGSEMTILD---VDKLDEAEYTCIAENKAGEQEAEIHLKV 92
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 368-437 2.63e-04

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


Pssm-ID: 409551  Cd Length: 94  Bit Score: 40.55  E-value: 2.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151301230 368 GQSLCLVC-VTYSNPPANVSWAWVTQTLIP---IQSSEPG----VLELPLVQREHEGEFTCAAQNPLGAQRISLSLSV 437
Cdd:cd20959   17 GMRAQLHCgVPGGDLPLNIRWTLDGQPISDdlgITVSRLGrrssILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 362-437 3.19e-04

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


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 39.89  E-value: 3.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151301230 362 SLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIP---IQSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSV 437
Cdd:cd05876    4 SLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPdrvKYQNHNKTLQLLNVGESDDGEYVCLAENSLGSARHAYYVTV 82
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 263-335 3.24e-04

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 39.54  E-value: 3.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151301230 263 QGQSLRLLCTADSQPPATLSWVLEDQVLswssPVGSRTL-----ALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05745    1 EGQTVDFLCEAQGYPQPVIAWTKGGSQL----SVDRRHLvlssgTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 362-437 3.48e-04

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 40.14  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 362 SLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIpiQSS-----EPGVLELPLVQREHEGEFTCAAQNPLGAQRISLSLS 436
Cdd:cd04969   11 KILAAKGGDVIIECKPKASPKPTISWSKGTELLT--NSSricilPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLS 88


                 .
gi 151301230 437 V 437
Cdd:cd04969   89 V 89
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
 354-438 3.71e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF; VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity.


Pssm-ID: 409404  Cd Length: 102  Bit Score: 40.22  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 354 LEILRNAISLPVLEGQSLCLVCVTYSNPPANVSWAW-----------VTQTLIPIQSSEPG----VLELPLVQREHEGEF 418
Cdd:cd05742    3 LELSPNAEPTVLPQGETLVLNCTANVNLNEVVDFQWtypsekegklaLLKPDIKVDWSEPGefvsTLTIPEATLKDSGTY 82

                         90       100
                 ....*....|....*....|
gi 151301230 419 TCAAQNPLGAQRISLSLSVH 438
Cdd:cd05742   83 TCAARSGVMKKEKQTSVSVH 102
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 250-335 3.94e-04

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


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 39.84  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 250 PDLHENPSHLEVQQGQSLRLLCTADSQPPATLSWVL-----EDQVLSWSSPVGSRTLA----LELPWVKAGDSGHYTCQA 320
Cdd:cd05765    1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvpgkENLIMRPNHVRGNVVVTnigqLVIYNAQPQDAGLYTCTA 80

                         90
                 ....*....|....*
gi 151301230 321 ENRLGSQQHTLDLSV 335
Cdd:cd05765   81 RNSGGLLRANFPLSV 95
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 245-335 5.23e-04

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 39.41  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 245 DNVSVPdlhENPSHLEVQQGQSLRLLCTADSQPPATLSWVLED---QVLSWSSPVGSRTLALELPWVKAGDSGHYTCQAE 321
Cdd:cd20970    1 PVISTP---QPSFTVTAREGENATFMCRAEGSPEPEISWTRNGnliIEFNTRYIVRENGTTLTIRNIRRSDMGIYLCIAS 77

                         90
                 ....*....|....*
gi 151301230 322 NRL-GSQQHTLDLSV 335
Cdd:cd20970   78 NGVpGSVEKRITLQV 92
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 250-326 5.54e-04

First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module by contacts between IG domains 1 and 4, and domains 2 and 3. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409437 [Multi-domain]  Cd Length: 97  Bit Score: 39.52  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 250 PDLHENPSHLEVQQG---QSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTLALEL----PwVKAGDSGHYTCQAEN 322
Cdd:cd05850    3 PVFEEQPSSTLFPEGsaeEKVTLACRARASPPATYRWKMNGTELKMEPDSRYRLVAGNLvisnP-VKAKDAGSYQCLASN 81


                 ....
gi 151301230 323 RLGS 326
Cdd:cd05850   82 RRGT 85
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 256-326 6.06e-04

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


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 39.60  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSW-------------VLEDQVLSwSSPVGSrtlaLELPWVKAGDSGHYTCQAEN 322
Cdd:cd20954    8 PVDANVAAGQDVMLHCQADGFPTPTVTWkkatgstpgeykdLLYDPNVR-ILPNGT----LVFGHVQKENEGHYLCEAKN 82


                 ....
gi 151301230 323 RLGS 326
Cdd:cd20954   83 GIGS 86
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 259-335 6.16e-04

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


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 39.09  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 259 LEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPV-----GSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDL 333
Cdd:cd20973    7 KEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFqidqdEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86


                 ..
gi 151301230 334 SV 335
Cdd:cd20973   87 TV 88
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 365-437 8.06e-04

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 39.12  E-value: 8.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 365 VLEGQSLCLVCVTYSNPPANVSWAWVTQTL-------IPIQSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSV 437
Cdd:cd05891   13 IMEGKTLNLTCTVFGNPDPEVIWFKNDQDIelsehysVKLEQGKYASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
I-set pfam07679
Immunoglobulin I-set domain;
365-437 8.28e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.78  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  365 VLEGQSLCLVCVTYSNPPANVSWawvTQTLIPIQSSEPGV---------LELPLVQREHEGEFTCAAQNPLGAQRISLSL 435
Cdd:pfam07679  12 VQEGESARFTCTVTGTPDPEVSW---FKDGQPLRSSDRFKvtyeggtytLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88


                  ..
gi 151301230  436 SV 437
Cdd:pfam07679  89 TV 90
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 256-326 8.44e-04

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 38.76  E-value: 8.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGS-RTLALELPWVKAGDSGHYTCQAENRLGS 326
Cdd:cd20968    6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVlESGSLRIHNVQKEDAGQYRCVAKNSLGI 77
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 365-437 1.20e-03

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 38.73  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 365 VLEGQSLCLVCVTYSNPPANVSWAWVTQtliPIQSSEPGVLELPL----------VQREHEGEFTCAAQNPLGAQRISLS 434
Cdd:cd05737   13 IMEGKTLNLTCNVWGDPPPEVSWLKNDQ---ALAFLDHCNLKVEAgrtvyftingVSSEDSGKYGLVVKNKYGSETSDVT 89


                 ...
gi 151301230 435 LSV 437
Cdd:cd05737   90 VSV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 260-335 1.62e-03

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


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 38.26  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 260 EVQQGQSLRLLCTADSQPPA-TLSWVLEDQVLSWSSPV------GSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLD 332
Cdd:cd05750   10 TVQEGSKLVLKCEATSENPSpRYRWFKDGKELNRKRPKnikirnKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGN 89


                 ...
gi 151301230 333 LSV 335
Cdd:cd05750   90 VTV 92
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 256-335 1.84e-03

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 37.96  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd05728    6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 261-335 2.07e-03

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 37.76  E-value: 2.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151301230 261 VQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSP---VGSRTLALELpwVKAGDSGHYTCQAENRLGSQQHTLDLSV 335
Cdd:cd20978   13 VKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMEratVEDGTLTIIN--VQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgV_TIM-3_like cd20982
Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3) ...
 30-122 2.11e-03

Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and similar domains; The members here are composed of the immunoglobulin variable (IgV) domain of T cell immunoglobulin domain and mucin domain 3 (Tim-3; also known as Hepatitis A virus cellular receptor 2 (HAVcr-2) and Cluster of Differentiation 366 (CD366)) and similar proteins. TIM-3 is a checkpoint inhibitor in immune responses to tumors, as well as involved in chronic viral infections. Thus, Tim-3 has emerged as one of most promising immune checkpoint targets for cancer immunotherapy. Tim-3 is highly expressed on Th1 lymphocytes and CD11b(+) macrophages and is upregulated on activated T and myeloid cells. TIM-3 regulates macrophage, activation and inhibits Th1 mediated immune responses to promote immunological tolerance. There are three TIM family members in humans (TIM-1, TIM-3, and TIM-4) and eight members in mice (TIM-1 to TIM-8). The IgV domain of human TIM-3 has been shown to bind ligands such as carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1), high mobility group protein B1 (HMGB1)and galectin-9 (GAL9). The binding of GAL9 to TIM-3 can negatively regulate Th1 immune response, enhance immune tolerance and inhibit anti#tumor immunity. Dysregulation of the TIM-3/GAL9 pathway is implicated in numerous chronic autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus.


Pssm-ID: 409574  Cd Length: 107  Bit Score: 38.21  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  30 VKAQEGLCIFVPCSFSSPEGKWLnrSPLYgyWFKGIRKPS--LSFPVATNNKDkvLEWEARGRFQLLGDISKKNCSLLIK 107
Cdd:cd20982    3 YRAEVGHNAYLPCSYTTAAPGNL--VPVC--WGKGACPVSycGNVLLRTDERD--VTYQKSSRYQLKGDFSKGDVSLTIE 76

                         90
                 ....*....|....*
gi 151301230 108 DVQWGDSTNYFFRME 122
Cdd:cd20982   77 NVTLADSGIYCCRIQ 91
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 256-326 2.78e-03

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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 37.48  E-value: 2.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPvGSRTL---ALELPWVKAGDSGHYTCQAENRLGS 326
Cdd:cd20952    6 PQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDE-RITTLengSLQIKGAEKSDTGEYTCVALNLSGE 78
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 254-335 3.12e-03

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


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 37.50  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 254 ENPSHLEVQQgqsLRLLCTADSQPPATLSWVLEDQVLSWS--SPVG-------SRTLALELPWVKAGDSGHYTCQAENRL 324
Cdd:cd05732    9 ENQTAVELEQ---ITLTCEAEGDPIPEITWRRATRGISFEegDLDGrivvrghARVSSLTLKDVQLTDAGRYDCEASNRI 85

                         90
                 ....*....|.
gi 151301230 325 GSQQHTLDLSV 335
Cdd:cd05732   86 GGDQQSMYLEV 96
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 256-335 3.19e-03

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 37.20  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWS-----SPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQqhT 330
Cdd:cd05891    8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSehysvKLEQGKYASLTIKGVTSEDSGKYSINVKNKYGGE--T 85


                 ....*
gi 151301230 331 LDLSV 335
Cdd:cd05891   86 VDVTV 90
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 367-437 3.23e-03

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 36.84  E-value: 3.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151301230 367 EGQSLCLVCVTYSNPPANVSWAWVTQTLiPI----QSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSV 437
Cdd:cd05745    1 EGQTVDFLCEAQGYPQPVIAWTKGGSQL-SVdrrhLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 362-435 4.27e-03

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 36.79  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230  362 SLPVLEGQSLCLVC-VTYSNPPANVSWaWVTQTlIPIQSSEPG---------VLELPLVQREHEGEFTCAAQNPLGAQRI 431
Cdd:pfam00047   5 TVTVLEGDSATLTCsASTGSPGPDVTW-SKEGG-TLIESLKVKhdngrttqsSLLISNVTKEDAGTYTCVVNNPGGSATL 82


                  ....
gi 151301230  432 SLSL 435
Cdd:pfam00047  83 STSL 86
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 365-437 4.48e-03

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 36.62  E-value: 4.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301230 365 VLEGQSLCLVCVTYSNPPANVSWAWVTQTLIPIQSSEPG---VLELPLVQREHEGEFTCAAQNPLGAQRISLSLSV 437
Cdd:cd05731    7 VLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKFENfnkTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 356-435 4.95e-03

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


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 36.68  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301230 356 ILRNAISLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIPIQSS----EPGVLELPLVQREHEGEFTCAAQNPLG--AQ 429
Cdd:cd05764    3 ITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRtlvyDNGTLDILITTVKDTGAFTCIASNPAGeaTA 82


                 ....*.
gi 151301230 430 RISLSL 435
Cdd:cd05764   83 RVELHI 88
IgC2_CD22_d3 cd20937
Third immunoglobulin domain in Cluster of Differentiation (CD) 22; member of the Constant 2 ...
 256-328 8.03e-03

Third immunoglobulin domain in Cluster of Differentiation (CD) 22; member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain in Cluster of Differentiation (CD) 22 (also known as Siglec-2). CD22, a sialic-acid binding immunoglobulin type-lectin (Siglec) family member, is an inhibitory co-receptor of the B-cell receptor (BCR). The inhibitory function of CD22 and its restricted expression on B cells makes CD22 an attractive target against dysregulated B cells that cause autoimmune diseases and B-cell-derived cancers. CD22 plays a vital role in establishing a baseline level of B-cell inhibition, and thus is an important determinant of homeostasis in humoral immunity. Siglecs are primarily expressed on immune cells and recognize sialic acid-containing glycan ligands. Siglecs are organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4, myelin-associated glycoprotein), the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11. 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.


Pssm-ID: 409531  Cd Length: 88  Bit Score: 36.32  E-value: 8.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151301230 256 PSHLEVQQGQSLRLLCTADSQPP--ATLSWVLEDQVLSwsspvGSRTLALELPWVKAGDSGHYTCQAENRLGSQQ 328
Cdd:cd20937    9 PSDAIVREGDSVTMTCEVSSSNPeyTTVSWLKDGTSLK-----KQNTFTLNLREVTKDQSGKYCCQVSNDVGPGR 78
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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