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Conserved domains on  [gi|387527984|ref|NP_001248348|]
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interleukin-1 receptor type 2 isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 136-230 7.16e-56

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


:

Pssm-ID: 409478  Cd Length: 95  Bit Score: 175.33  E-value: 7.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 136 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 215
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                         90
                 ....*....|....*
gi 387527984 216 QQYNITRSIELRIKK 230
Cdd:cd05897   81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 29-126 3.51e-47

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


:

Pssm-ID: 409414  Cd Length: 96  Bit Score: 153.35  E-value: 3.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  29 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 108
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78

                         90
                 ....*....|....*...
gi 387527984 109 TTRNASYCDKMSIELRVF 126
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 241-285 7.19e-04

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 pfam00047:

Pssm-ID: 472250  Cd Length: 86  Bit Score: 37.94  E-value: 7.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 387527984  241 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAY 285
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESLK 43
 
Name Accession Description Interval E-value
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 136-230 7.16e-56

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 175.33  E-value: 7.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 136 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 215
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                         90
                 ....*....|....*
gi 387527984 216 QQYNITRSIELRIKK 230
Cdd:cd05897   81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 29-126 3.51e-47

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409414  Cd Length: 96  Bit Score: 153.35  E-value: 3.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  29 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 108
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78

                         90
                 ....*....|....*...
gi 387527984 109 TTRNASYCDKMSIELRVF 126
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 6-282 4.19e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 150.17  E-value: 4.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984   6 VLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPywLWASVSPRINLTWHKN--DSARTVPGEEE 83
Cdd:PHA02785   4 LPVIFLPIFFYSSFVQTFNAPECIDKGQYFASFMELENEPVILPCPQIN--TLSSGYNILDILWEKRgaDNDRIIPIDNG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  84 TRMwaqdgaLWLLPAlQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKT 163
Cdd:PHA02785  82 SNM------LILNPT-QSDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 164 DVKIQWYKDSLLLDKDnekfLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKkeeTIPVIISPL 243
Cdd:PHA02785 155 NADIIWSGHRRLRNKR----LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLP 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 387527984 244 KTISASLGSRLTIPCKVFLgtgTPLTT--MLWWTANDTHIE 282
Cdd:PHA02785 228 EGVVTSIGSNLTIACRVSL---RPPTTdaDVFWISNGMYYE 265
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 42-125 4.78e-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: 49.81  E-value: 4.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984    42 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSAR-TVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS 120
Cdd:smart00410   8 EGESVTLSCE-------ASGSPPPEVTWYKQGGKLlAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 387527984   121 IELRV 125
Cdd:smart00410  81 TTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 41-112 5.51e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.01  E-value: 5.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387527984   41 LEGEPVALRCpqvpywlWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:pfam13927  14 REGETVTLTC-------EATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 149-228 2.33e-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: 39.41  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984   149 VLVCPdlsefTRDKTDVKIQWYKD--SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHegqqYNITRSIEL 226
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTL 83


                   ..
gi 387527984   227 RI 228
Cdd:smart00410  84 TV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 241-285 7.19e-04

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: 37.94  E-value: 7.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 387527984  241 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAY 285
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESLK 43
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 166-208 1.79e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.39  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 387527984  166 KIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCV 208
Cdd:pfam13927  32 TITWYKNgEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
PHA02633 PHA02633
hypothetical protein; Provisional
 95-125 5.67e-03

hypothetical protein; Provisional


Pssm-ID: 165016  Cd Length: 63  Bit Score: 34.57  E-value: 5.67e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 387527984  95 LLPALQEDSGTYVCTTRNASYCDKMSIELRV 125
Cdd:PHA02633  22 ILNPTQSDSGIYMCITKNETYSDMMKFDLCI 52
 
Name Accession Description Interval E-value
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 136-230 7.16e-56

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 175.33  E-value: 7.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 136 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 215
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                         90
                 ....*....|....*
gi 387527984 216 QQYNITRSIELRIKK 230
Cdd:cd05897   81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 29-126 3.51e-47

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409414  Cd Length: 96  Bit Score: 153.35  E-value: 3.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  29 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 108
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78

                         90
                 ....*....|....*...
gi 387527984 109 TTRNASYCDKMSIELRVF 126
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 6-282 4.19e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 150.17  E-value: 4.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984   6 VLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPywLWASVSPRINLTWHKN--DSARTVPGEEE 83
Cdd:PHA02785   4 LPVIFLPIFFYSSFVQTFNAPECIDKGQYFASFMELENEPVILPCPQIN--TLSSGYNILDILWEKRgaDNDRIIPIDNG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  84 TRMwaqdgaLWLLPAlQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKT 163
Cdd:PHA02785  82 SNM------LILNPT-QSDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 164 DVKIQWYKDSLLLDKDnekfLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKkeeTIPVIISPL 243
Cdd:PHA02785 155 NADIIWSGHRRLRNKR----LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLP 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 387527984 244 KTISASLGSRLTIPCKVFLgtgTPLTT--MLWWTANDTHIE 282
Cdd:PHA02785 228 EGVVTSIGSNLTIACRVSL---RPPTTdaDVFWISNGMYYE 265
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 136-229 3.30e-33

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 117.04  E-value: 3.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 136 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNeKFLSVRgtTHLLVHDVALEDAGYYRCVLTFAHEG 215
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDK-RFIPKG--SKLLIQNVTEEDAGNYTCKFTYTHNG 77

                         90
                 ....*....|....
gi 387527984 216 QQYNITRSIELRIK 229
Cdd:cd05757   78 KQYNVTRTISLTVT 91
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 138-229 7.07e-22

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409586  Cd Length: 94  Bit Score: 87.52  E-value: 7.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 138 YPQILTLSTSGVLVCPDLsEFTRDKTDV--KIQWYKDSLLLDKDNEKFLSVRGTthLLVHDVALEDAGYYRCVLTFAHEG 215
Cdd:cd20994    3 YKQKVPFTSGGRIVCPHL-DFFKDENNNlpKVQWYKDCKPLLLDDKRFAGLESD--LLIFNVTVQDQGNYTCHTSYTYMG 79

                         90
                 ....*....|....
gi 387527984 216 QQYNITRSIELRIK 229
Cdd:cd20994   80 KQYNISRTISLIVL 93
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 27-228 3.39e-13

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 67.63  E-value: 3.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  27 SCRFRGRHYKREFRLEGEPVALRCPQVPY----WLWASVSPRINLTWHKNDS--------ART-----VPGEEETRmwaq 89
Cdd:PHA02826  21 YCKYRGGDLTPVYAKFGDPMVLLCTGKHYkksiFFDKTFITSYNVTWSKTDSlafvrdsgARTkikkiTHNEIGDR---- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  90 DGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFlPFISypqiltlSTSGVLVCPDLSEFTRDKTDVKIQW 169
Cdd:PHA02826  97 SENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGTINY-QFNS-------GKDSKLHCYGTDGISSTFKDYTLTW 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 387527984 170 YKDSLLLDKDnEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRI 228
Cdd:PHA02826 169 YKNGNIVLYT-DRIQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 50-125 2.79e-12

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. IL-1 receptor antagonist (IL-1RA), a naturally occurring cytokine, is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409583  Cd Length: 91  Bit Score: 61.54  E-value: 2.79e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 387527984  50 CPQVPYwlwasvSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRV 125
Cdd:cd20991   21 CPLNPN------ESKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKITAKF 90
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 35-125 2.44e-10

First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. IL1RAPL is encoded by a gene on the X-chromosome, this gene is wholly or partially deleted in multiple cases of non-syndromic intellectual disability. This group also contains IL1RAPL-2 which is also encoded by a gene on the X-chromosome and is a candidate for another non-syndromic intellectual disability loci.


Pssm-ID: 409477  Cd Length: 105  Bit Score: 56.50  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  35 YKREFRLEGEPVALRCPQVPYWLWASV----SPRINLTWHKNDSARTVpgEE-----ETRMWAQDGALWLLPALQEDSGT 105
Cdd:cd05896    7 LKKYMVLAGEPVRIKCALFYGYIRTNYsmaqSAGLSLMWYKSSGPGDF--EEpiifdGVRMSKEEDSIWFRPAELQDSGL 84

                         90       100
                 ....*....|....*....|
gi 387527984 106 YVCTTRNASYCDKMSIELRV 125
Cdd:cd05896   85 YTCVLRNSTYCMKVSMSLTV 104
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 41-125 6.42e-09

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409584  Cd Length: 108  Bit Score: 52.62  E-value: 6.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  41 LEGEPVALRCPQVPYWL---WASV-SPRINLTWHKNDSARTVpgEE-------ETRMWAQDGALWLLPALQEDSGTYVCT 109
Cdd:cd20992   14 FEGEPARIKCPLFEHFLkynYSTAhSAGLTLIWYWTRQDRDL--EEpinfrlpDNRISKEKDVLWFRPTLLNDTGNYTCM 91

                         90
                 ....*....|....*.
gi 387527984 110 TRNASYCDKMSIELRV 125
Cdd:cd20992   92 LRNTTYCSKVAFPLEV 107
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 42-125 4.78e-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: 49.81  E-value: 4.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984    42 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSAR-TVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS 120
Cdd:smart00410   8 EGESVTLSCE-------ASGSPPPEVTWYKQGGKLlAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 387527984   121 IELRV 125
Cdd:smart00410  81 TTLTV 85
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 29-125 3.39e-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: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  29 RFRGRHYKREFRLEGEPVALRC------PQVPYWLWASVSPrinLTWHKNDSARTVPgeeetrmwaqDGALWLLPALQED 102
Cdd:cd20969    3 AIRDRKAQQVFVDEGHTVQFVCradgdpPPAILWLSPRKHL---VSAKSNGRLTVFP----------DGTLEVRYAQVQD 69

                         90       100
                 ....*....|....*....|...
gi 387527984 103 SGTYVCTTRNASYCDKMSIELRV 125
Cdd:cd20969   70 NGTYLCIAANAGGNDSMPAHLHV 92
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 139-228 3.67e-06

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409585  Cd Length: 93  Bit Score: 44.51  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 139 PQILTLSTSG-VLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKflsVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQ 217
Cdd:cd20993    4 PVIAYIEYGGrTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDR---VPKGDKLVIHVMLEHYQGNYTCVVTYETKGRT 80

                         90
                 ....*....|.
gi 387527984 218 YNITRSIELRI 228
Cdd:cd20993   81 IKLTRTVNVKV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 149-217 5.08e-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: 43.47  E-value: 5.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984 149 VLVCPdlsefTRDKTDVKIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQ 217
Cdd:cd00096    2 TLTCS-----ASGNPPPTITWYKNgKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 46-112 1.36e-05

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: 42.32  E-value: 1.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387527984  46 VALRCPqvpywlwASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:cd00096    1 VTLTCS-------ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 41-112 5.51e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.01  E-value: 5.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387527984   41 LEGEPVALRCpqvpywlWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:pfam13927  14 REGETVTLTC-------EATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 40-112 2.03e-04

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: 39.30  E-value: 2.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387527984  40 RLEGEPVALRCPqvpywlwASVSPRINLTWHKNdsARTVPGEEETRMWaQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:cd20978   13 VKGGQDVTLPCQ-------VTGVPQPKITWLHN--GKPLQGPMERATV-EDGTLTIINVQPEDTGYYGCVATN 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 149-228 2.33e-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: 39.41  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984   149 VLVCPdlsefTRDKTDVKIQWYKD--SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHegqqYNITRSIEL 226
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTL 83


                   ..
gi 387527984   227 RI 228
Cdd:smart00410  84 TV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 41-114 4.24e-04

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: 38.72  E-value: 4.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 387527984   41 LEGEPVALRCPQVPywlwasVSPRINLTWHKNDSaRTVPGEEETRMWAQDGA--LWLLPALQEDSGTYVCTTRNAS 114
Cdd:pfam00047   9 LEGDSATLTCSAST------GSPGPDVTWSKEGG-TLIESLKVKHDNGRTTQssLLISNVTKEDAGTYTCVVNNPG 77
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 41-125 4.40e-04

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: 38.77  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984  41 LEGEPVALRCPqvpywlwASVSPRINLTWHKNDSARTVPGEEETrMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS 120
Cdd:cd20976   14 VEGQDFVAQCS-------ARGKPVPRITWIRNAQPLQYAADRST-CEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCS 85


                 ....*
gi 387527984 121 IELRV 125
Cdd:cd20976   86 AWVTV 90
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 42-116 5.88e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 37.76  E-value: 5.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387527984   42 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSArtvpgeeetrmWAQDGALWLLPALQEDSGTYVCTTRNASYC 116
Cdd:pfam13895  13 EGEPVTLTCS-------APGNPPPSYTWYKDGSA-----------ISSSPNFFTLSVSAEDSGTYTCVARNGRGG 69
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 241-285 7.19e-04

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: 37.94  E-value: 7.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 387527984  241 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAY 285
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESLK 43
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 41-112 9.10e-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: 37.87  E-value: 9.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387527984  41 LEGEPVALRCPqvpywlwASVSPRINLTWHKNDSARTVPGE-EETRMWAQDgaLWLLPALQEDSGTYVCTTRN 112
Cdd:cd20970   15 REGENATFMCR-------AEGSPEPEISWTRNGNLIIEFNTrYIVRENGTT--LTIRNIRRSDMGIYLCIASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 166-208 1.79e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.39  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 387527984  166 KIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCV 208
Cdd:pfam13927  32 TITWYKNgEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 41-112 2.28e-03

Second 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 second 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 the 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, and 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, 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 Slit-2 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: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 36.61  E-value: 2.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387527984  41 LEGEPVALRC-PQVPYwlwasvsPRINLTWHKNDSarTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:cd05724   10 AVGEMAVLECsPPRGH-------PEPTVSWRKDGQ--PLNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATN 73
PHA02633 PHA02633
hypothetical protein; Provisional
 95-125 5.67e-03

hypothetical protein; Provisional


Pssm-ID: 165016  Cd Length: 63  Bit Score: 34.57  E-value: 5.67e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 387527984  95 LLPALQEDSGTYVCTTRNASYCDKMSIELRV 125
Cdd:PHA02633  22 ILNPTQSDSGIYMCITKNETYSDMMKFDLCI 52
I-set pfam07679
Immunoglobulin I-set domain;
42-125 8.93e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 34.93  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387527984   42 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSI 121
Cdd:pfam07679  14 EGESARFTCT-------VTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASA 86


                  ....
gi 387527984  122 ELRV 125
Cdd:pfam07679  87 ELTV 90
 
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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