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Conserved domains on  [gi|1267063758|ref|NP_001344020|]
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B-lymphocyte antigen CD19 isoform 2 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CD19_protodomain_1_2 cd23999
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 1 ...
 24-115 1.01e-49

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 1 and 2; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding. This group contains the protodomains 1 and 2 of the CD19 double Ig domain.


:

Pssm-ID: 467826  Cd Length: 92  Bit Score: 166.06  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758  24 LLVEVEEGGNVVLPCLPDSSPVSSEKLAWYRGNQSTPFLELSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQKRPPF 103
Cdd:cd23999     1 LLVEVEEGDNAVLPCLIGPSDGPPEQLTWSRGGQLEPFLQLSLGSPGLGAQVGPLGIWLFIFNVSEQMGGFYLCELGPPS 80

                          90
                  ....*....|..
gi 1267063758 104 KDIWQPAWTVNV 115
Cdd:cd23999    81 KQAWQPGWTVSV 92
CD19_double_Ig super family cl49627
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, ...
 183-272 7.20e-43

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding.


The actual alignment was detected with superfamily member cd23998:

Pssm-ID: 483967  Cd Length: 95  Bit Score: 148.02  E-value: 7.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 183 QDLTVAPGSTLWLSCGVPPVPVAKGSISWTHVHPRRPNVSLLSLSLGGEHPVREMWV-----WGSLLLLPQATALDEGTY 257
Cdd:cd23998     1 QDLTVAPGSTLWLSCGVPPDSGTRGPISWTHVHPKPSNTSLLSLELKEDRPAREKWVlgtlrGGALLLLPRATAQDAGIY 80

                          90
                  ....*....|....*
gi 1267063758 258 YCLRGNLTIERHVKV 272
Cdd:cd23998    81 HCHLGNRTISMELTV 95
 
Name Accession Description Interval E-value
CD19_protodomain_1_2 cd23999
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 1 ...
 24-115 1.01e-49

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 1 and 2; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding. This group contains the protodomains 1 and 2 of the CD19 double Ig domain.


Pssm-ID: 467826  Cd Length: 92  Bit Score: 166.06  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758  24 LLVEVEEGGNVVLPCLPDSSPVSSEKLAWYRGNQSTPFLELSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQKRPPF 103
Cdd:cd23999     1 LLVEVEEGDNAVLPCLIGPSDGPPEQLTWSRGGQLEPFLQLSLGSPGLGAQVGPLGIWLFIFNVSEQMGGFYLCELGPPS 80

                          90
                  ....*....|..
gi 1267063758 104 KDIWQPAWTVNV 115
Cdd:cd23999    81 KQAWQPGWTVSV 92
CD19_protodomain_3_4 cd23998
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 3 ...
 183-272 7.20e-43

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 3 and 4; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding. This group contains the protodomains 3 and 4 of the CD19 double Ig domain.


Pssm-ID: 467825  Cd Length: 95  Bit Score: 148.02  E-value: 7.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 183 QDLTVAPGSTLWLSCGVPPVPVAKGSISWTHVHPRRPNVSLLSLSLGGEHPVREMWV-----WGSLLLLPQATALDEGTY 257
Cdd:cd23998     1 QDLTVAPGSTLWLSCGVPPDSGTRGPISWTHVHPKPSNTSLLSLELKEDRPAREKWVlgtlrGGALLLLPRATAQDAGIY 80

                          90
                  ....*....|....*
gi 1267063758 258 YCLRGNLTIERHVKV 272
Cdd:cd23998    81 HCHLGNRTISMELTV 95
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 26-115 1.61e-04

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: 40.57  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758   26 VEVEEGGNVVLPCLPDSSPVSSekLAWYRGNqstpfLELSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQKRPPFKD 105
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPE--VTWYKQG-----GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS 76

                           90
                   ....*....|
gi 1267063758  106 IWQPAwTVNV 115
Cdd:smart00410  77 ASSGT-TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 183-263 5.96e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.03  E-value: 5.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758  183 QDLTVAPGSTLWLSCGVPPVPVAkgSISWthvhpRRPNVSLLSlslggeHPVREMWVWGSL---LLLPQATALDEGTYYC 259
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPP--EVTW-----YKQGGKLLA------ESGRFSVSRSGStstLTISNVTPEDSGTYTC 68


                   ....
gi 1267063758  260 LRGN 263
Cdd:smart00410  69 AATN 72
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 26-98 1.33e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 1.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267063758  26 VEVEEGGNVVLPCLPDSSPvsSEKLAWYRGNQstpfleLSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQ 98
Cdd:pfam13927  11 VTVREGETVTLTCEATGSP--PPTITWYKNGE------PISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 182-259 5.47e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.00  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 182 NQDLTVAPGSTLWLSCGV--PPVPvakgSISWTHVHPRRPNVSLLSLSLGGEhpvremwvwGSLLLLPQATALDEGTYYC 259
Cdd:pfam13927   8 PSSVTVREGETVTLTCEAtgSPPP----TITWYKNGEPISSGSTRSRSLSGS---------NSTLTISNVTRSDAGTYTC 74
 
Name Accession Description Interval E-value
CD19_protodomain_1_2 cd23999
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 1 ...
 24-115 1.01e-49

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 1 and 2; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding. This group contains the protodomains 1 and 2 of the CD19 double Ig domain.


Pssm-ID: 467826  Cd Length: 92  Bit Score: 166.06  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758  24 LLVEVEEGGNVVLPCLPDSSPVSSEKLAWYRGNQSTPFLELSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQKRPPF 103
Cdd:cd23999     1 LLVEVEEGDNAVLPCLIGPSDGPPEQLTWSRGGQLEPFLQLSLGSPGLGAQVGPLGIWLFIFNVSEQMGGFYLCELGPPS 80

                          90
                  ....*....|..
gi 1267063758 104 KDIWQPAWTVNV 115
Cdd:cd23999    81 KQAWQPGWTVSV 92
CD19_protodomain_3_4 cd23998
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 3 ...
 183-272 7.20e-43

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold protodomain 3 and 4; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding. This group contains the protodomains 3 and 4 of the CD19 double Ig domain.


Pssm-ID: 467825  Cd Length: 95  Bit Score: 148.02  E-value: 7.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 183 QDLTVAPGSTLWLSCGVPPVPVAKGSISWTHVHPRRPNVSLLSLSLGGEHPVREMWV-----WGSLLLLPQATALDEGTY 257
Cdd:cd23998     1 QDLTVAPGSTLWLSCGVPPDSGTRGPISWTHVHPKPSNTSLLSLELKEDRPAREKWVlgtlrGGALLLLPRATAQDAGIY 80

                          90
                  ....*....|....*
gi 1267063758 258 YCLRGNLTIERHVKV 272
Cdd:cd23998    81 HCHLGNRTISMELTV 95
CD19_double_Ig cd23997
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, ...
 24-115 2.18e-34

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding.


Pssm-ID: 467824  Cd Length: 89  Bit Score: 124.76  E-value: 2.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758  24 LLVEVEEGGNVVLPCLPDSSPVSSEKLAWYRGNQSTPFLELSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQKRPPF 103
Cdd:cd23997     1 LDVTVAEGSTLWLPCLVPPSDGPRGPLTWSRGHPKTPLLSLELGSPGLWVLVGPLGILLLLPNVSAQMGGFYLCELGNLS 80

                          90
                  ....*....|..
gi 1267063758 104 kdiWQPAWTVNV 115
Cdd:cd23997    81 ---WTIGWTVSV 89
CD19_double_Ig cd23997
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, ...
 183-272 1.79e-22

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding.


Pssm-ID: 467824  Cd Length: 89  Bit Score: 91.63  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 183 QDLTVAPGSTLWLSCGVPPVPVAKGSISWTHVHPRrpnVSLLSLSLGGehpvREMWV----WGSLLLLPQATALDEGTYY 258
Cdd:cd23997     1 LDVTVAEGSTLWLPCLVPPSDGPRGPLTWSRGHPK---TPLLSLELGS----PGLWVlvgpLGILLLLPNVSAQMGGFYL 73

                          90
                  ....*....|....*.
gi 1267063758 259 CLRGNL--TIERHVKV 272
Cdd:cd23997    74 CELGNLswTIGWTVSV 89
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 185-267 4.39e-09

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 53.62  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 185 LTVAPGSTLWLSCGVPPvpvAKGSISWTHVHPRRPnvsllslslgGEHPVREMWVWGSLLLLPQATALDEGTYYCLRGNL 264
Cdd:cd04979     6 ISVKEGDTVILSCSVKS---NNAPVTWIHNGKKVP----------RYRSPRLVLKTERGLLIRSAQEADAGVYECHSGER 72


                  ...
gi 1267063758 265 TIE 267
Cdd:cd04979    73 VLG 75
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 20-97 1.27e-05

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: 44.04  E-value: 1.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267063758  20 PQKSLLVEVEEGGNVVLPCLPDSSPvsSEKLAWYR-GNQSTPFLElspgspglGLHVGSLGILLVIVNVSDHMGGFYLC 97
Cdd:cd20970     6 PQPSFTVTAREGENATFMCRAEGSP--EPEISWTRnGNLIIEFNT--------RYIVRENGTTLTIRNIRRSDMGIYLC 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 26-115 1.61e-04

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: 40.57  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758   26 VEVEEGGNVVLPCLPDSSPVSSekLAWYRGNqstpfLELSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQKRPPFKD 105
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPPE--VTWYKQG-----GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS 76

                           90
                   ....*....|
gi 1267063758  106 IWQPAwTVNV 115
Cdd:smart00410  77 ASSGT-TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 183-263 5.96e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.03  E-value: 5.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758  183 QDLTVAPGSTLWLSCGVPPVPVAkgSISWthvhpRRPNVSLLSlslggeHPVREMWVWGSL---LLLPQATALDEGTYYC 259
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPP--EVTW-----YKQGGKLLA------ESGRFSVSRSGStstLTISNVTPEDSGTYTC 68


                   ....
gi 1267063758  260 LRGN 263
Cdd:smart00410  69 AATN 72
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 26-98 1.33e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 1.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267063758  26 VEVEEGGNVVLPCLPDSSPvsSEKLAWYRGNQstpfleLSPGSPGLGLHVGSLGILLVIVNVSDHMGGFYLCQ 98
Cdd:pfam13927  11 VTVREGETVTLTCEATGSP--PPTITWYKNGE------PISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 182-259 5.47e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.00  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 182 NQDLTVAPGSTLWLSCGV--PPVPvakgSISWTHVHPRRPNVSLLSLSLGGEhpvremwvwGSLLLLPQATALDEGTYYC 259
Cdd:pfam13927   8 PSSVTVREGETVTLTCEAtgSPPP----TITWYKNGEPISSGSTRSRSLSGS---------NSTLTISNVTRSDAGTYTC 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 180-259 5.67e-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: 36.02  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267063758 180 LINQDLTVAPGSTLWLSCGVPPVPVAkGSISWthvhpRRPNVSLLSLSLGGEHPVREMwvwGSLLLLPQATALDEGTYYC 259
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPG-PDVTW-----SKEGGTLIESLKVKHDNGRTT---QSSLLISNVTKEDAGTYTC 71
 
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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