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Conserved domains on  [gi|386766218|ref|NP_001247232|]
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uncharacterized protein Dmel_CG31431, isoform C [Drosophila melanogaster]

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 ...
 152-272 6.18e-10

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 cd04974:

Pssm-ID: 472250  Cd Length: 102  Bit Score: 55.89  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218 152 PEFVDSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFRRQTYVGTQSGgeassapttsnfsnhivrYNGRTYelLSTDPEK 231
Cdd:cd04974    1 PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYG------------------PDGLPY--VTVLKVA 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 386766218 232 MMAPQIYLSKLILDGVRLRDAGHYACVAISYRGHKIREAFL 272
Cdd:cd04974   61 GVNTTGEENTLTISNVTFDDAGEYICLAGNSIGLSFHSAWL 101
 
Name Accession Description Interval E-value
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 152-272 6.18e-10

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. 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: 409363  Cd Length: 102  Bit Score: 55.89  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218 152 PEFVDSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFRRQTYVGTQSGgeassapttsnfsnhivrYNGRTYelLSTDPEK 231
Cdd:cd04974    1 PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYG------------------PDGLPY--VTVLKVA 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 386766218 232 MMAPQIYLSKLILDGVRLRDAGHYACVAISYRGHKIREAFL 272
Cdd:cd04974   61 GVNTTGEENTLTISNVTFDDAGEYICLAGNSIGLSFHSAWL 101
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 152-259 1.87e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218  152 PEFVdSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFRrqtyvgtqSGGEASSAPTTSNFSNHIVryngrtyellstdpek 231
Cdd:pfam13927   2 PVIT-VSPSSVTVREGETVTLTCEATGSPPPTITWYK--------NGEPISSGSTRSRSLSGSN---------------- 56

                          90       100
                  ....*....|....*....|....*...
gi 386766218  232 mmapqiylSKLILDGVRLRDAGHYACVA 259
Cdd:pfam13927  57 --------STLTISNVTRSDAGTYTCVA 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 159-274 2.39e-06

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: 45.19  E-value: 2.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218   159 PNNKTTLVGSRVVFQCRVHSEEHPTIKWFRRQTYVGTQSGgeassapttsnfsnhivRYNGRTYELLSTdpekmmapqiy 238
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG-----------------RFSVSRSGSTST----------- 52

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 386766218   239 lskLILDGVRLRDAGHYACVAISYRGHKIREAFLDV 274
Cdd:smart00410  53 ---LTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 152-272 6.18e-10

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. 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: 409363  Cd Length: 102  Bit Score: 55.89  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218 152 PEFVDSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFRRQTYVGTQSGgeassapttsnfsnhivrYNGRTYelLSTDPEK 231
Cdd:cd04974    1 PILQAGLPANQTVVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKYG------------------PDGLPY--VTVLKVA 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 386766218 232 MMAPQIYLSKLILDGVRLRDAGHYACVAISYRGHKIREAFL 272
Cdd:cd04974   61 GVNTTGEENTLTISNVTFDDAGEYICLAGNSIGLSFHSAWL 101
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 159-275 2.56e-07

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. 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: 409444  Cd Length: 105  Bit Score: 48.42  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218 159 PNNKTTLVGSRVVFQCRVHSEEHPTIKWFRRQTYVGTQSGGEASSAPTTSnfsnhivryngRTYELLSTDPEkmmapqiy 238
Cdd:cd05858    8 PANTSVVVGTDAEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVEVL-----------KTAGVNTTDKE-------- 68

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 386766218 239 LSKLILDGVRLRDAGHYACVAISYRGHKIREAFLDVL 275
Cdd:cd05858   69 IEVLYLRNVTFEDAGEYTCLAGNSIGISHHSAWLTVL 105
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 152-274 1.56e-06

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: 45.85  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218 152 PEFVDSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFrrqtyvgtqsggeassapttsnfsnhivrYNGRTyelLSTDPEK 231
Cdd:cd20978    1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWL-----------------------------HNGKP---LQGPMER 48

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 386766218 232 MmapQIYLSKLILDGVRLRDAGHYACVAISYRGHKIREAFLDV 274
Cdd:cd20978   49 A---TVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 152-259 1.87e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 45.25  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218  152 PEFVdSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFRrqtyvgtqSGGEASSAPTTSNFSNHIVryngrtyellstdpek 231
Cdd:pfam13927   2 PVIT-VSPSSVTVREGETVTLTCEATGSPPPTITWYK--------NGEPISSGSTRSRSLSGSN---------------- 56

                          90       100
                  ....*....|....*....|....*...
gi 386766218  232 mmapqiylSKLILDGVRLRDAGHYACVA 259
Cdd:pfam13927  57 --------STLTISNVTRSDAGTYTCVA 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 159-274 2.39e-06

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: 45.19  E-value: 2.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218   159 PNNKTTLVGSRVVFQCRVHSEEHPTIKWFRRQTYVGTQSGgeassapttsnfsnhivRYNGRTYELLSTdpekmmapqiy 238
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG-----------------RFSVSRSGSTST----------- 52

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 386766218   239 lskLILDGVRLRDAGHYACVAISYRGHKIREAFLDV 274
Cdd:smart00410  53 ---LTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
152-259 3.64e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.86  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218  152 PEFVdSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFRrqtyvgtqsGGEassaPTTSNfSNHIVRYNGRTYellstdpek 231
Cdd:pfam07679   1 PKFT-QKPKDVEVQEGESARFTCTVTGTPDPEVSWFK---------DGQ----PLRSS-DRFKVTYEGGTY--------- 56

                          90       100
                  ....*....|....*....|....*...
gi 386766218  232 mmapqiylsKLILDGVRLRDAGHYACVA 259
Cdd:pfam07679  57 ---------TLTISNVQPDDSGKYTCVA 75
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 155-259 4.29e-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: 41.72  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766218 155 VDSYPNNKTTLVGSRVVFQCRVHSEEHPTIKWFRRQTYVGTQSggeassapttsnfSNHIVRYNGRTYELLStdpekmma 234
Cdd:cd20970    5 TPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFN-------------TRYIVRENGTTLTIRN-------- 63

                         90       100
                 ....*....|....*....|....*
gi 386766218 235 pqiylsklildgVRLRDAGHYACVA 259
Cdd:cd20970   64 ------------IRRSDMGIYLCIA 76
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 159-188 5.02e-05

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: 41.23  E-value: 5.02e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 386766218 159 PNNKTTLVGSRVVFQCRVHSEEHPTIKWFR 188
Cdd:cd05725    4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRK 33
 
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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