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Conserved domains on  [gi|217272826|ref|NP_001136054|]
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interleukin-1 receptor accessory protein-like 1-B precursor [Danio rerio]

Protein Classification

immunoglobulin domain-containing protein( domain architecture ID 10959197)

immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and pattern recognition; similar to Drosophila melanogaster DIP/Dpr cell recognition proteins, which are members of the Wirin family of IgSF proteins with neuronal wiring functions, and human IgLON proteins, a family of cell adhesion molecules

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 ...
32-136 2.57e-57

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 cd05896:

Pssm-ID: 472250  Cd Length: 105  Bit Score: 189.39  E-value: 2.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  32 TDWSVDYLRYRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQ 111
Cdd:cd05896    1 TDWSVDLKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGPGDFEEPIIFDGVRMSKEEDSIWFRPAELQ 80
                         90       100
                 ....*....|....*....|....*
gi 217272826 112 DSGHYSCVLRNSSYCMKVSMALTVA 136
Cdd:cd05896   81 DSGLYTCVLRNSTYCMKVSMSLTVA 105
TIR super family cl23801
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
405-559 2.12e-22

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


The actual alignment was detected with superfamily member pfam01582:

Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 94.35  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  405 YDAYVSYTKVDpdqwsqetrEEEHFALEILPDMleKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYvVR 484
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  485 RGWSIFELETRLRNMLVSGeIKVILIE-CSD------LRGIMnyqeVEALKHTIKLLT---VIRWPGPG----------S 544
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFyEVDpsdvrkQTGSF----GKAFKKHKKVLTeekVLKWRGALnevaniwhskS 143
                         170
                  ....*....|....*
gi 217272826  545 SKPNSRFWKQLQYEM 559
Cdd:pfam01582 144 VSDESKFWKKIAYDI 158
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
148-234 5.33e-19

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 cd05757:

Pssm-ID: 472250  Cd Length: 92  Bit Score: 82.37  E-value: 5.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 148 MRRLEKAELSKSKDILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQF---GR-F 223
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYthnGKqY 80
                         90
                 ....*....|.
gi 217272826 224 LVRRTTELTVT 234
Cdd:cd05757   81 NVTRTISLTVT 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
241-338 2.24e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.89  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  241 PPKILQPPehklSVMELQLGGPVNLTCRAffgySGDVSPLIYWMKGEKFIEDLDETRIRESEikmvrehlgeqeVSVSLT 320
Cdd:pfam13927   1 KPVITVSP----SSVTVREGETVTLTCEA----TGSPPPTITWYKNGEPISSGSTRSRSLSG------------SNSTLT 60
                          90
                  ....*....|....*...
gi 217272826  321 IDSLQEEDLGNYSCYVEN 338
Cdd:pfam13927  61 ISNVTRSDAGTYTCVASN 78
 
Name Accession Description Interval E-value
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
32-136 2.57e-57

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: 189.39  E-value: 2.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  32 TDWSVDYLRYRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQ 111
Cdd:cd05896    1 TDWSVDLKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGPGDFEEPIIFDGVRMSKEEDSIWFRPAELQ 80
                         90       100
                 ....*....|....*....|....*
gi 217272826 112 DSGHYSCVLRNSSYCMKVSMALTVA 136
Cdd:cd05896   81 DSGLYTCVLRNSTYCMKVSMSLTVA 105
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
405-559 2.12e-22

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 94.35  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  405 YDAYVSYTKVDpdqwsqetrEEEHFALEILPDMleKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYvVR 484
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  485 RGWSIFELETRLRNMLVSGeIKVILIE-CSD------LRGIMnyqeVEALKHTIKLLT---VIRWPGPG----------S 544
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFyEVDpsdvrkQTGSF----GKAFKKHKKVLTeekVLKWRGALnevaniwhskS 143
                         170
                  ....*....|....*
gi 217272826  545 SKPNSRFWKQLQYEM 559
Cdd:pfam01582 144 VSDESKFWKKIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
405-560 8.55e-21

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 88.92  E-value: 8.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826   405 YDAYVSYtkvdpdqwsqetREEEHFALEILPDMLEKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYvVR 484
Cdd:smart00255   2 YDVFISY------------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNY-AE 68
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 217272826   485 RGWSIFELETRLRNMLVSGEIKVILIECSdlrgiMNYQEVEALKHTIKLL---TVIRWPGPGSskpnSRFWKQLQYEMP 560
Cdd:smart00255  69 SEWCLDELVAALENALEEGGLRVIPIFYE-----VIPSDVRKQPGKFRKVfkkNYLKWPEDEK----EQFWKKALYAVP 138
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
148-234 5.33e-19

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: 82.37  E-value: 5.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 148 MRRLEKAELSKSKDILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQF---GR-F 223
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYthnGKqY 80
                         90
                 ....*....|.
gi 217272826 224 LVRRTTELTVT 234
Cdd:cd05757   81 NVTRTISLTVT 91
PHA02785 PHA02785
IL-beta-binding protein; Provisional
7-334 1.27e-15

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 78.52  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826   7 LQILLYAAVIRSLKVVSkrgsvdgCTDWSVDYLRYRVLLGEPVRIKCAlfygyiRANYTHAQSAGLSLMWYRSATHTDHE 86
Cdd:PHA02785   9 LPIFFYSSFVQTFNAPE-------CIDKGQYFASFMELENEPVILPCP------QINTLSSGYNILDILWEKRGADNDRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  87 EPITlDGTrtlkeeDALWFRPAQlQDSGHYSCVLRNSSYCMKVSMALTVAENSSglcynSKMRRLEKAELSKSK---DIL 163
Cdd:PHA02785  76 IPID-NGS------NMLILNPTQ-SDSGIYICITKNETYCDMMSLNLTIVSVSE-----SNIDLISYPQIVNERstgEMV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 164 CPDIQDYTPAGSEPHVTW--YKECRPKQWRSsiiRTADLLSIRDVREDDIGNYTCEIQF----GRFLVRRTTELTVTAPL 237
Cdd:PHA02785 143 CPNINAFIASNVNADIIWsgHRRLRNKRLKQ---RTPGIITIEDVRKNDAGYYTCVLKYiygdKTYNVTRIVKLEVRDRI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 238 TdkpPKILQPPEhklsVMELQLGGPVNLTCRAFFgYSGDVSPLIYWM-KGEKFIEDLDETRIRESEIKMVREHLGEQEVS 316
Cdd:PHA02785 220 I---PPTMQLPE----GVVTSIGSNLTIACRVSL-RPPTTDADVFWIsNGMYYEEDDEDGDGRISVANKIYTTDKRRVIT 291
                        330
                 ....*....|....*...
gi 217272826 317 VSLTIDSLQEEDLGNYSC 334
Cdd:PHA02785 292 SRLNINPVKEEDATTFTC 309
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
241-338 2.24e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.89  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  241 PPKILQPPehklSVMELQLGGPVNLTCRAffgySGDVSPLIYWMKGEKFIEDLDETRIRESEikmvrehlgeqeVSVSLT 320
Cdd:pfam13927   1 KPVITVSP----SSVTVREGETVTLTCEA----TGSPPPTITWYKNGEPISSGSTRSRSLSG------------SNSTLT 60
                          90
                  ....*....|....*...
gi 217272826  321 IDSLQEEDLGNYSCYVEN 338
Cdd:pfam13927  61 ISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
253-350 4.24e-10

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: 56.74  E-value: 4.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826   253 SVMELQLGGPVNLTCRAffgySGDVSPLIYWMKgEKFIEDLDETRIRESEikmvrehlgeQEVSVSLTIDSLQEEDLGNY 332
Cdd:smart00410   2 PSVTVKEGESVTLSCEA----SGSPPPEVTWYK-QGGKLLAESGRFSVSR----------SGSTSTLTISNVTPEDSGTY 66
                           90
                   ....*....|....*...
gi 217272826   333 SCYVENGHGRRHAIIQLS 350
Cdd:smart00410  67 TCAATNSSGSASSGTTLT 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
242-342 1.47e-08

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: 52.39  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 242 PKILQPPEhklSVMELQLGGPVNLTCRAffgySGDVSPLIYWMKGEKFIEdldetriRESEIKMVREHlgeqevsvSLTI 321
Cdd:cd20978    1 PKFIQKPE---KNVVVKGGQDVTLPCQV----TGVPQPKITWLHNGKPLQ-------GPMERATVEDG--------TLTI 58
                         90       100
                 ....*....|....*....|.
gi 217272826 322 DSLQEEDLGNYSCYVENGHGR 342
Cdd:cd20978   59 INVQPEDTGYYGCVATNEIGD 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
175-233 1.14e-05

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: 44.03  E-value: 1.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272826   175 SEPHVTWYKEcrPKQW-----RSSIIRTADL--LSIRDVREDDIGNYTCEIQFGRFLVRRTTELTV 233
Cdd:smart00410  22 PPPEVTWYKQ--GGKLlaesgRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
41-135 1.73e-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: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826    41 YRVLLGEPVRIKCALFyGYIRANYThaqsaglslmWYRsathtDHEEPITLDGTRTLKEED---ALWFRPAQLQDSGHYS 117
Cdd:smart00410   4 VTVKEGESVTLSCEAS-GSPPPEVT----------WYK-----QGGKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYT 67
                           90
                   ....*....|....*...
gi 217272826   118 CVLRNSSYCMKVSMALTV 135
Cdd:smart00410  68 CAATNSSGSASSGTTLTV 85
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
76-146 7.73e-04

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 40.09  E-value: 7.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272826   76 WYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQDSGHYSCVLRNSSY-----CMKvsMALTVAENSSGLCYNS 146
Cdd:pfam18452  48 WYWQPKNGDPLEAITESSPHIIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLK--IILEVQPKTNASCSGS 121
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
173-217 8.86e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.70  E-value: 8.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 217272826  173 AGSEPHVTWYKECRPKQWRSSIIRTAD----LLSIRDVREDDIGNYTCE 217
Cdd:pfam13927  27 GSPPPTITWYKNGEPISSGSTRSRSLSgsnsTLTISNVTRSDAGTYTCV 75
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
103-221 7.94e-03

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 38.36  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 103 LWFRPAQLQDSGHYSCVLRNSSYCMKVSMALTVAENSSGLCYNSkmrrlekaelSKSKDILCPDIQDYTPAGSEPHVTWY 182
Cdd:PHA02826 100 LWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGTINYQFNS----------GKDSKLHCYGTDGISSTFKDYTLTWY 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 217272826 183 KECR--PKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQFG 221
Cdd:PHA02826 170 KNGNivLYTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRFN 210
 
Name Accession Description Interval E-value
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
32-136 2.57e-57

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: 189.39  E-value: 2.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  32 TDWSVDYLRYRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQ 111
Cdd:cd05896    1 TDWSVDLKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGPGDFEEPIIFDGVRMSKEEDSIWFRPAELQ 80
                         90       100
                 ....*....|....*....|....*
gi 217272826 112 DSGHYSCVLRNSSYCMKVSMALTVA 136
Cdd:cd05896   81 DSGLYTCVLRNSTYCMKVSMSLTVA 105
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
32-135 7.05e-35

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: 127.54  E-value: 7.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  32 TDWSVDYLRYRVLLGEPVRIKCALFYGYIranythAQSAGLSLMWYRSathtDHEEPITLD-GTRTLKEEDALWFRPAQL 110
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL------AQSAGLNLTWYKN----DSETPISFEpDSRIHQEKDKLWFVPALL 70
                         90       100
                 ....*....|....*....|....*
gi 217272826 111 QDSGHYSCVLRNSSYCMKVSMALTV 135
Cdd:cd05756   71 EDSGNYYCVVRNSTYCSKVSISLEV 95
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
33-135 4.66e-30

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: 114.25  E-value: 4.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  33 DWSVDYLR-YRVLLGEPVRIKCALFYGYIRANYTHAQSAGLSLMWYRSATHTDHEEPIT--LDGTRTLKEEDALWFRPAQ 109
Cdd:cd20992    2 DWGLDTMRqIQVFEGEPARIKCPLFEHFLKYNYSTAHSAGLTLIWYWTRQDRDLEEPINfrLPDNRISKEKDVLWFRPTL 81
                         90       100
                 ....*....|....*....|....*.
gi 217272826 110 LQDSGHYSCVLRNSSYCMKVSMALTV 135
Cdd:cd20992   82 LNDTGNYTCMLRNTTYCSKVAFPLEV 107
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
405-559 2.12e-22

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 94.35  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  405 YDAYVSYTKVDpdqwsqetrEEEHFALEILPDMleKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYvVR 484
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  485 RGWSIFELETRLRNMLVSGeIKVILIE-CSD------LRGIMnyqeVEALKHTIKLLT---VIRWPGPG----------S 544
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFyEVDpsdvrkQTGSF----GKAFKKHKKVLTeekVLKWRGALnevaniwhskS 143
                         170
                  ....*....|....*
gi 217272826  545 SKPNSRFWKQLQYEM 559
Cdd:pfam01582 144 VSDESKFWKKIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
405-560 8.55e-21

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 88.92  E-value: 8.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826   405 YDAYVSYtkvdpdqwsqetREEEHFALEILPDMLEKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYvVR 484
Cdd:smart00255   2 YDVFISY------------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNY-AE 68
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 217272826   485 RGWSIFELETRLRNMLVSGEIKVILIECSdlrgiMNYQEVEALKHTIKLL---TVIRWPGPGSskpnSRFWKQLQYEMP 560
Cdd:smart00255  69 SEWCLDELVAALENALEEGGLRVIPIFYE-----VIPSDVRKQPGKFRKVfkkNYLKWPEDEK----EQFWKKALYAVP 138
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
148-234 5.33e-19

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: 82.37  E-value: 5.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 148 MRRLEKAELSKSKDILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQF---GR-F 223
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYthnGKqY 80
                         90
                 ....*....|.
gi 217272826 224 LVRRTTELTVT 234
Cdd:cd05757   81 NVTRTISLTVT 91
PHA02785 PHA02785
IL-beta-binding protein; Provisional
7-334 1.27e-15

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 78.52  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826   7 LQILLYAAVIRSLKVVSkrgsvdgCTDWSVDYLRYRVLLGEPVRIKCAlfygyiRANYTHAQSAGLSLMWYRSATHTDHE 86
Cdd:PHA02785   9 LPIFFYSSFVQTFNAPE-------CIDKGQYFASFMELENEPVILPCP------QINTLSSGYNILDILWEKRGADNDRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  87 EPITlDGTrtlkeeDALWFRPAQlQDSGHYSCVLRNSSYCMKVSMALTVAENSSglcynSKMRRLEKAELSKSK---DIL 163
Cdd:PHA02785  76 IPID-NGS------NMLILNPTQ-SDSGIYICITKNETYCDMMSLNLTIVSVSE-----SNIDLISYPQIVNERstgEMV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 164 CPDIQDYTPAGSEPHVTW--YKECRPKQWRSsiiRTADLLSIRDVREDDIGNYTCEIQF----GRFLVRRTTELTVTAPL 237
Cdd:PHA02785 143 CPNINAFIASNVNADIIWsgHRRLRNKRLKQ---RTPGIITIEDVRKNDAGYYTCVLKYiygdKTYNVTRIVKLEVRDRI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 238 TdkpPKILQPPEhklsVMELQLGGPVNLTCRAFFgYSGDVSPLIYWM-KGEKFIEDLDETRIRESEIKMVREHLGEQEVS 316
Cdd:PHA02785 220 I---PPTMQLPE----GVVTSIGSNLTIACRVSL-RPPTTDADVFWIsNGMYYEEDDEDGDGRISVANKIYTTDKRRVIT 291
                        330
                 ....*....|....*...
gi 217272826 317 VSLTIDSLQEEDLGNYSC 334
Cdd:PHA02785 292 SRLNINPVKEEDATTFTC 309
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
73-129 2.50e-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: 63.08  E-value: 2.50e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 217272826  73 SLMWYRSathtDHEEPITLD-GTRTLKEEDALWFRPAQLQDSGHYSCVLRNSSYCMKV 129
Cdd:cd20991   31 TITWYKN----DSKTPISMEqDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKI 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
241-338 2.24e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.89  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  241 PPKILQPPehklSVMELQLGGPVNLTCRAffgySGDVSPLIYWMKGEKFIEDLDETRIRESEikmvrehlgeqeVSVSLT 320
Cdd:pfam13927   1 KPVITVSP----SSVTVREGETVTLTCEA----TGSPPPTITWYKNGEPISSGSTRSRSLSG------------SNSTLT 60
                          90
                  ....*....|....*...
gi 217272826  321 IDSLQEEDLGNYSCYVEN 338
Cdd:pfam13927  61 ISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
242-349 2.05e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 57.65  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  242 PKILQPPehklSVMELQLGGPVNLTCRAffgySGDVSPLIYWMKGEKfiedldetRIRES-EIKMVREhlgeqEVSVSLT 320
Cdd:pfam07679   1 PKFTQKP----KDVEVQEGESARFTCTV----TGTPDPEVSWFKDGQ--------PLRSSdRFKVTYE-----GGTYTLT 59
                          90       100
                  ....*....|....*....|....*....
gi 217272826  321 IDSLQEEDLGNYSCYVENGHGRRHAIIQL 349
Cdd:pfam07679  60 ISNVQPDDSGKYTCVATNSAGEAEASAEL 88
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
162-233 3.24e-10

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: 57.22  E-value: 3.24e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272826 162 ILCPDIQDYTPAGSEPHVTWYKECRPKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQF---GR-FLVRRTTELTV 233
Cdd:cd20993   16 ITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYetkGRtIKLTRTVNVKV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
253-350 4.24e-10

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: 56.74  E-value: 4.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826   253 SVMELQLGGPVNLTCRAffgySGDVSPLIYWMKgEKFIEDLDETRIRESEikmvrehlgeQEVSVSLTIDSLQEEDLGNY 332
Cdd:smart00410   2 PSVTVKEGESVTLSCEA----SGSPPPEVTWYK-QGGKLLAESGRFSVSR----------SGSTSTLTISNVTPEDSGTY 66
                           90
                   ....*....|....*...
gi 217272826   333 SCYVENGHGRRHAIIQLS 350
Cdd:smart00410  67 TCAATNSSGSASSGTTLT 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
242-342 1.47e-08

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: 52.39  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 242 PKILQPPEhklSVMELQLGGPVNLTCRAffgySGDVSPLIYWMKGEKFIEdldetriRESEIKMVREHlgeqevsvSLTI 321
Cdd:cd20978    1 PKFIQKPE---KNVVVKGGQDVTLPCQV----TGVPQPKITWLHNGKPLQ-------GPMERATVEDG--------TLTI 58
                         90       100
                 ....*....|....*....|.
gi 217272826 322 DSLQEEDLGNYSCYVENGHGR 342
Cdd:cd20978   59 INVQPEDTGYYGCVATNEIGD 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
263-343 2.15e-08

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: 51.56  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 263 VNLTCRAffgySGDVSPLIYWMKGEKFIEDLDETRIREseikmvrehlgeQEVSVSLTIDSLQEEDLGNYSCYVENGHGR 342
Cdd:cd00096    1 VTLTCSA----SGNPPPTITWYKNGKPLPPSSRDSRRS------------ELGNGTLTISNVTLEDSGTYTCVASNSAGG 64

                 .
gi 217272826 343 R 343
Cdd:cd00096   65 S 65
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
242-345 7.96e-08

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 50.63  E-value: 7.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 242 PKILQPPEHKLSVMELQLGGPVNLTCRAffgySGDVSPLIYWMKgekfiedlDETRireseikMVREHLGEQ-EVSVSLT 320
Cdd:cd05856    1 PRFTQPAKMRRRVIARPVGSSVRLKCVA----SGNPRPDITWLK--------DNKP-------LTPPEIGENkKKKWTLS 61
                         90       100
                 ....*....|....*....|....*
gi 217272826 321 IDSLQEEDLGNYSCYVENGHGRRHA 345
Cdd:cd05856   62 LKNLKPEDSGKYTCHVSNRAGEINA 86
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
423-514 2.02e-07

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 50.01  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  423 TREEEHFALEILPDmLEKHyGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYvVRRGWSIFELETRLRnmLVS 502
Cdd:pfam13676   6 AGEDRAWAEWLADA-LEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNY-LESPWCRAEWEAALA--DPE 80
                          90
                  ....*....|....
gi 217272826  503 GEIKVI--LIECSD 514
Cdd:pfam13676  81 GRKRLIpvRLECDL 94
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
254-341 3.45e-06

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 45.66  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 254 VMELQLGGPVNLTCRAFfgysGDVSPLIYWMKGEKFIEDLDETRIREseikmvrehlgEQEVSVSLTIDSLQEEDLGNYS 333
Cdd:cd05737   10 VVTIMEGKTLNLTCNVW----GDPPPEVSWLKNDQALAFLDHCNLKV-----------EAGRTVYFTINGVSSEDSGKYG 74

                 ....*...
gi 217272826 334 CYVENGHG 341
Cdd:cd05737   75 LVVKNKYG 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
256-341 4.44e-06

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.26  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  256 ELQLGGPVNLTCRAFFGYSGdvsPLIYWMKGEKFIEDLDETRIRESEIKmvrehlgeqevSVSLTIDSLQEEDLGNYSCY 335
Cdd:pfam00047   7 TVLEGDSATLTCSASTGSPG---PDVTWSKEGGTLIESLKVKHDNGRTT-----------QSSLLISNVTKEDAGTYTCV 72

                  ....*.
gi 217272826  336 VENGHG 341
Cdd:pfam00047  73 VNNPGG 78
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
162-233 9.71e-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: 409586  Cd Length: 94  Bit Score: 44.38  E-value: 9.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 162 ILCPDIQDYTPAGSE-PHVTWYKECRP---KQWRSSIIRTAdlLSIRDVREDDIGNYTCEIQF----GRFLVRRTTELTV 233
Cdd:cd20994   15 IVCPHLDFFKDENNNlPKVQWYKDCKPlllDDKRFAGLESD--LLIFNVTVQDQGNYTCHTSYtymgKQYNISRTISLIV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
175-233 1.14e-05

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: 44.03  E-value: 1.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272826   175 SEPHVTWYKEcrPKQW-----RSSIIRTADL--LSIRDVREDDIGNYTCEIQFGRFLVRRTTELTV 233
Cdd:smart00410  22 PPPEVTWYKQ--GGKLlaesgRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
252-341 3.08e-05

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


Pssm-ID: 143299  Cd Length: 92  Bit Score: 42.97  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 252 LSVMElqlGGPVNLTCRAFfgysGDVSPLIYWMKGEKFIEDLDETRIREseikmvrehlgEQEVSVSLTIDSLQEEDLGN 331
Cdd:cd05891   11 VTIME---GKTLNLTCTVF----GNPDPEVIWFKNDQDIELSEHYSVKL-----------EQGKYASLTIKGVTSEDSGK 72
                         90
                 ....*....|
gi 217272826 332 YSCYVENGHG 341
Cdd:cd05891   73 YSINVKNKYG 82
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
241-350 3.23e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 43.40  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 241 PPKILQPPEHklsvMELQLGGPVNLTCRaffgYSGDVSPLIYWMKGEKfiedldetRIRESE-IKMVrehlgEQEVSVSL 319
Cdd:cd05762    1 PPQIIQFPED----MKVRAGESVELFCK----VTGTQPITCTWMKFRK--------QIQEGEgIKIE-----NTENSSKL 59
                         90       100       110
                 ....*....|....*....|....*....|.
gi 217272826 320 TIDSLQEEDLGNYSCYVENGHGRRHAIIQLS 350
Cdd:cd05762   60 TITEGQQEHCGCYTLEVENKLGSRQAQVNLT 90
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
177-233 1.15e-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: 41.47  E-value: 1.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 177 PHVTWYKECRPKQW---RSSIIRTADLLSIRDVREDDIGNYTCEIQFGRFLVRRTTELTV 233
Cdd:cd20976   31 PRITWIRNAQPLQYaadRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
176-217 1.40e-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.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 40.78  E-value: 1.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 217272826 176 EPHVTWYKECRPKQWRSSIIRTADL----LSIRDVREDDIGNYTCE 217
Cdd:cd00096   12 PPTITWYKNGKPLPPSSRDSRRSELgngtLTISNVTLEDSGTYTCV 57
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
41-135 1.73e-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: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826    41 YRVLLGEPVRIKCALFyGYIRANYThaqsaglslmWYRsathtDHEEPITLDGTRTLKEED---ALWFRPAQLQDSGHYS 117
Cdd:smart00410   4 VTVKEGESVTLSCEAS-GSPPPEVT----------WYK-----QGGKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYT 67
                           90
                   ....*....|....*...
gi 217272826   118 CVLRNSSYCMKVSMALTV 135
Cdd:smart00410  68 CAATNSSGSASSGTTLTV 85
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
262-341 2.24e-04

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 40.67  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 262 PVNLTCRAFFGYSGDVSPLIYWMKGEKfiEDLDETRIRESEIKmvrehlgeqEVSVSLTIDSLQEEDLGNYSCYVENGHG 341
Cdd:cd05729   17 PAANKVRLECGAGGNPMPNITWLKDGK--EFKKEHRIGGTKVE---------EKGWSLIIERAIPRDKGKYTCIVENEYG 85
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
274-349 5.32e-04

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475  Cd Length: 86  Bit Score: 39.44  E-value: 5.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217272826 274 SGDVSPLIYWMKGEKFIEDlDETRIR-ESeikmvrehlgeQEVSVSLTIDSLQEEDLGNYSCYVENGHGRRHAIIQL 349
Cdd:cd05894   20 SGEPAPTVTWSRGDKAFTA-TEGRVRvES-----------YKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFV 84
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
76-146 7.73e-04

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 40.09  E-value: 7.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272826   76 WYRSATHTDHEEPITLDGTRTLKEEDALWFRPAQLQDSGHYSCVLRNSSY-----CMKvsMALTVAENSSGLCYNS 146
Cdd:pfam18452  48 WYWQPKNGDPLEAITESSPHIIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLK--IILEVQPKTNASCSGS 121
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
173-217 8.86e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.70  E-value: 8.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 217272826  173 AGSEPHVTWYKECRPKQWRSSIIRTAD----LLSIRDVREDDIGNYTCE 217
Cdd:pfam13927  27 GSPPPTITWYKNGEPISSGSTRSRSLSgsnsTLTISNVTRSDAGTYTCV 75
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
156-233 1.12e-03

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: 38.59  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 156 LSKSKDILCPDIQDYTPAGSEPHVTWYKECR---PKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQFG----RFLVRRT 228
Cdd:cd05897    9 TSTSGKLVCPDLSEFTINRTDVEIQWYKDSLlldKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFThegkKYNITRS 88

                 ....*
gi 217272826 229 TELTV 233
Cdd:cd05897   89 IELRI 93
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
247-298 2.71e-03

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 37.19  E-value: 2.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 217272826 247 PPEHKlsvmELQLGGPVNLTCRAFfgysGDVSPLIYWMKGEKFIEDLDETRI 298
Cdd:cd05739    3 PPSNH----EVMPGGSVNLTCVAV----GAPMPYVKWMKGGEELTKEDEMPV 46
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
260-347 7.91e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 36.03  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 260 GGPVNLtcraFFGYSGDVSPLIYWMKGEKFIEDLDETRIRESEikmvrehlgeqeVSVSLTIDSLQEEDLGNYSCYVENG 339
Cdd:cd05748    7 GESLRL----DIPIKGRPTPTVTWSKDGQPLKETGRVQIETTA------------SSTSLVIKNAKRSDSGKYTLTLKNS 70

                 ....*...
gi 217272826 340 HGRRHAII 347
Cdd:cd05748   71 AGEKSATI 78
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
103-221 7.94e-03

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 38.36  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826 103 LWFRPAQLQDSGHYSCVLRNSSYCMKVSMALTVAENSSGLCYNSkmrrlekaelSKSKDILCPDIQDYTPAGSEPHVTWY 182
Cdd:PHA02826 100 LWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGTINYQFNS----------GKDSKLHCYGTDGISSTFKDYTLTWY 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 217272826 183 KECR--PKQWRSSIIRTADLLSIRDVREDDIGNYTCEIQFG 221
Cdd:PHA02826 170 KNGNivLYTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRFN 210
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
253-350 7.96e-03

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 36.67  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  253 SVMELQLGGPVNLTCRaFFGYSGDVSPLIYWMKG----EKFIEDLDETRIRESEIKMVREHLGEQEV--SVSLTIDSLQE 326
Cdd:pfam07686   4 REVTVALGGSVTLPCT-YSSSMSEASTSVYWYRQppgkGPTFLIAYYSNGSEEGVKKGRFSGRGDPSngDGSLTIQNLTL 82
                          90       100
                  ....*....|....*....|....*
gi 217272826  327 EDLGNYSCYV-ENGHGRRHAIIQLS 350
Cdd:pfam07686  83 SDSGTYTCAViPSGEGVFGKGTRLT 107
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
172-233 8.59e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 35.83  E-value: 8.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 217272826  172 PAGSEPHVTWYKECRPKQWRSSIIRTAdllsirdVREDDIGNYTCEIQFGR-FLVRRTTELTV 233
Cdd:pfam13895  24 PGNPPPSYTWYKDGSAISSSPNFFTLS-------VSAEDSGTYTCVARNGRgGKVSNPVELTV 79
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
260-341 8.94e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 35.83  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272826  260 GGPVNLTCRAffgySGDVSPLIYWMKGEKFIEDLDEtrireseikmvrehlgeqevsvsLTIDSLQEEDLGNYSCYVENG 339
Cdd:pfam13895  14 GEPVTLTCSA----PGNPPPSYTWYKDGSAISSSPN-----------------------FFTLSVSAEDSGTYTCVARNG 66

                  ..
gi 217272826  340 HG 341
Cdd:pfam13895  67 RG 68
 
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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