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Conserved domains on  [gi|11225607|ref|NP_059112|]
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X-linked interleukin-1 receptor accessory protein-like 2 precursor [Homo sapiens]

Protein Classification

Ig2_IL1R-like and IG_like domain-containing protein( domain architecture ID 11666199)

protein containing domains Ig, Ig2_IL1R-like, IG_like, and TIR

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 ...
 32-134 4.49e-66

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: 212.50  E-value: 4.49e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  32 IDWSVDLKTYMALAGEPVRVKCALFYSYIRTNYSTAQSTGLRLMWYKNKG--DLEEPIIFSEVRMSKEEDSIWFHSAEAQ 109
Cdd:cd05896   1 TDWSVDLKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGpgDFEEPIIFDGVRMSKEEDSIWFRPAELQ 80

                        90       100
                ....*....|....*....|....*
gi 11225607 110 DSGFYTCVLRNSTYCMKVSMSLTVA 134
Cdd:cd05896  81 DSGLYTCVLRNSTYCMKVSMSLTVA 105
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 146-237 1.98e-30

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: 114.73  E-value: 1.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607 146 IRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRR 225
Cdd:cd05757   1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                        90
                ....*....|..
gi 11225607 226 TTELKVTALLTD 237
Cdd:cd05757  81 NVTRTISLTVTE 92
TIR super family cl23801
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 402-563 1.44e-24

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: 100.52  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   402 YDAYLSYTKVDqdtldcdnpEEEQFALEVLPDVleKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLR 481
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   482 RGWSIFELESRLHNMLVSGeIKVILIECTELKGKVNCQE---VESLKRSIKLLS---LIKWKG----------SKSSKLN 545
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFYEVDPSDVRKQTgsfGKAFKKHKKVLTeekVLKWRGalnevaniwhSKSVSDE 147

                         170
                  ....*....|....*...
gi 11225607   546 SKFWKHLVYEMPIKKKEM 563
Cdd:pfam01582 148 SKFWKKIAYDISNKLNGT 165
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 250-347 3.55e-07

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: 48.27  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607    250 PSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMK-GEKFIeelaghIREGEIRLLKEHLgekevELALIFDSVVEADLAN 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEVTWYKqGGKLL------AESGRFSVSRSGS-----TSTLTISNVTPEDSGT 65

                           90
                   ....*....|....*....
gi 11225607    329 YTCHVENRNGRKHASVLLR 347
Cdd:smart00410  66 YTCAATNSSGSASSGTTLT 84
 
Name Accession Description Interval E-value
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 32-134 4.49e-66

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: 212.50  E-value: 4.49e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  32 IDWSVDLKTYMALAGEPVRVKCALFYSYIRTNYSTAQSTGLRLMWYKNKG--DLEEPIIFSEVRMSKEEDSIWFHSAEAQ 109
Cdd:cd05896   1 TDWSVDLKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGpgDFEEPIIFDGVRMSKEEDSIWFRPAELQ 80

                        90       100
                ....*....|....*....|....*
gi 11225607 110 DSGFYTCVLRNSTYCMKVSMSLTVA 134
Cdd:cd05896  81 DSGLYTCVLRNSTYCMKVSMSLTVA 105
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 146-237 1.98e-30

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: 114.73  E-value: 1.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607 146 IRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRR 225
Cdd:cd05757   1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                        90
                ....*....|..
gi 11225607 226 TTELKVTALLTD 237
Cdd:cd05757  81 NVTRTISLTVTE 92
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 402-563 1.44e-24

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: 100.52  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   402 YDAYLSYTKVDqdtldcdnpEEEQFALEVLPDVleKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLR 481
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   482 RGWSIFELESRLHNMLVSGeIKVILIECTELKGKVNCQE---VESLKRSIKLLS---LIKWKG----------SKSSKLN 545
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFYEVDPSDVRKQTgsfGKAFKKHKKVLTeekVLKWRGalnevaniwhSKSVSDE 147

                         170
                  ....*....|....*...
gi 11225607   546 SKFWKHLVYEMPIKKKEM 563
Cdd:pfam01582 148 SKFWKKIAYDISNKLNGT 165
TIR smart00255
Toll - interleukin 1 - resistance;
401-559 4.53e-24

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 98.16  E-value: 4.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607    401 EYDAYLSYtkvdqdtldcdnPEEEQFALEVLPDVLEKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiL 480
Cdd:smart00255   1 EYDVFISY------------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNY-A 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607    481 RRGWSIFELESRLHNMLVSGEIKVILIECTELKgkvncQEVESLKRSIKLL---SLIKWKGSKSsklnSKFWKHLVYEMP 557
Cdd:smart00255  68 ESEWCLDELVAALENALEEGGLRVIPIFYEVIP-----SDVRKQPGKFRKVfkkNYLKWPEDEK----EQFWKKALYAVP 138


                   ..
gi 11225607    558 IK 559
Cdd:smart00255 139 SK 140
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 31-290 6.89e-16

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 79.29  E-value: 6.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   31 CIDWSVDLKTYMALAGEPVRVKCAlfysyiRTNYSTAQSTGLRLMWYKNKGDLEEPIIFSEvrmskeEDSIWFHSAEAQD 110
Cdd:PHA02785  26 CIDKGQYFASFMELENEPVILPCP------QINTLSSGYNILDILWEKRGADNDRIIPIDN------GSNMLILNPTQSD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  111 SGFYTCVLRNSTYCMKVSMSLT-VAENESGLcynSRIRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKEckPKMWR 189
Cdd:PHA02785  94 SGIYICITKNETYCDMMSLNLTiVSVSESNI---DLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGH--RRLRN 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  190 SIIIQKGNALL-IQEVQEEDGGNYTCELKYegklVRRTTELKVTALLTDKPPKPLFPMENQ-PSVIDVQLGKPLNIPCKA 267
Cdd:PHA02785 169 KRLKQRTPGIItIEDVRKNDAGYYTCVLKY----IYGDKTYNVTRIVKLEVRDRIIPPTMQlPEGVVTSIGSNLTIACRV 244

                        250       260
                 ....*....|....*....|...
gi 11225607  268 FFGfSGESGPMIYWMKGEKFIEE 290
Cdd:PHA02785 245 SLR-PPTTDADVFWISNGMYYEE 266
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 250-347 3.55e-07

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: 48.27  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607    250 PSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMK-GEKFIeelaghIREGEIRLLKEHLgekevELALIFDSVVEADLAN 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEVTWYKqGGKLL------AESGRFSVSRSGS-----TSTLTISNVTPEDSGT 65

                           90
                   ....*....|....*....
gi 11225607    329 YTCHVENRNGRKHASVLLR 347
Cdd:smart00410  66 YTCAATNSSGSASSGTTLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 39-133 2.87e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607     39 KTYMALAGEPVRVKCalfysyirtnySTAQSTGLRLMWYKNKGdleEPIIFS---EVRMSKEEDSIWFHSAEAQDSGFYT 115
Cdd:smart00410   2 PSVTVKEGESVTLSC-----------EASGSPPPEVTWYKQGG---KLLAESgrfSVSRSGSTSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*...
gi 11225607    116 CVLRNSTYCMKVSMSLTV 133
Cdd:smart00410  68 CAATNSSGSASSGTTLTV 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 171-231 2.08e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.15  E-value: 2.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11225607   171 SDQEPDVVWYKECKPkmwrsiIIQKGNaLLIQEVQEEDGGNYTCELKYE-GKLVRRTTELKV 231
Cdd:pfam13895  25 GNPPPSYTWYKDGSA------ISSSPN-FFTLSVSAEDSGTYTCVARNGrGGKVSNPVELTV 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 249-335 3.55e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   249 QPSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELALIFDSVVEADLAN 328
Cdd:pfam13927   7 SPSSVTVREGETVTLTCEA----TGSPPPTITWYKNGEPISSGSTRSRS-----------LSGSNSTLTISNVTRSDAGT 71


                  ....*..
gi 11225607   329 YTCHVEN 335
Cdd:pfam13927  72 YTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 159-231 3.87e-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: 42.49  E-value: 3.87e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11225607    159 EISCPdmddfKKSDQEPDVVWYKE-CKPKMWRSIIIQKGNA----LLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 231
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQgGKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 272-338 9.39e-04

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 39.07  E-value: 9.39e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11225607 272 SGESGPMIYWMK-GEKFIEElagHiREGEIRLLKEHLgekevelALIFDSVVEADLANYTCHVENRNG 338
Cdd:cd05857  29 AGNPTPTMRWLKnGKEFKQE---H-RIGGYKVRNQHW-------SLIMESVVPSDKGNYTCVVENEYG 85
 
Name Accession Description Interval E-value
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 32-134 4.49e-66

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: 212.50  E-value: 4.49e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  32 IDWSVDLKTYMALAGEPVRVKCALFYSYIRTNYSTAQSTGLRLMWYKNKG--DLEEPIIFSEVRMSKEEDSIWFHSAEAQ 109
Cdd:cd05896   1 TDWSVDLKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGpgDFEEPIIFDGVRMSKEEDSIWFRPAELQ 80

                        90       100
                ....*....|....*....|....*
gi 11225607 110 DSGFYTCVLRNSTYCMKVSMSLTVA 134
Cdd:cd05896  81 DSGLYTCVLRNSTYCMKVSMSLTVA 105
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 33-133 1.82e-31

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: 117.91  E-value: 1.82e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  33 DWSVDLKTYMALAGEPVRVKCALFYSYirtnysTAQSTGLRLMWYKNkgDLEEPIIFS-EVRMSKEEDSIWFHSAEAQDS 111
Cdd:cd05756   2 EWGEDIKILVVLEGEPDVIKCPLFPNF------LAQSAGLNLTWYKN--DSETPISFEpDSRIHQEKDKLWFVPALLEDS 73

                        90       100
                ....*....|....*....|..
gi 11225607 112 GFYTCVLRNSTYCMKVSMSLTV 133
Cdd:cd05756  74 GNYYCVVRNSTYCSKVSISLEV 95
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 146-237 1.98e-30

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: 114.73  E-value: 1.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607 146 IRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRR 225
Cdd:cd05757   1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                        90
                ....*....|..
gi 11225607 226 TTELKVTALLTD 237
Cdd:cd05757  81 NVTRTISLTVTE 92
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 33-133 5.11e-28

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: 108.48  E-value: 5.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  33 DWSVD-LKTYMALAGEPVRVKCALFYSYIRTNYSTAQSTGLRLMWYKNKG--DLEEPIIFS--EVRMSKEEDSIWFHSAE 107
Cdd:cd20992   2 DWGLDtMRQIQVFEGEPARIKCPLFEHFLKYNYSTAHSAGLTLIWYWTRQdrDLEEPINFRlpDNRISKEKDVLWFRPTL 81

                        90       100
                ....*....|....*....|....*.
gi 11225607 108 AQDSGFYTCVLRNSTYCMKVSMSLTV 133
Cdd:cd20992  82 LNDTGNYTCMLRNTTYCSKVAFPLEV 107
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 402-563 1.44e-24

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: 100.52  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   402 YDAYLSYTKVDqdtldcdnpEEEQFALEVLPDVleKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLR 481
Cdd:pfam01582   1 YDVFLSFRGSD---------TREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNY-AS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   482 RGWSIFELESRLHNMLVSGeIKVILIECTELKGKVNCQE---VESLKRSIKLLS---LIKWKG----------SKSSKLN 545
Cdd:pfam01582  69 SGWCLDELVKILECALDLG-QKVIPIFYEVDPSDVRKQTgsfGKAFKKHKKVLTeekVLKWRGalnevaniwhSKSVSDE 147

                         170
                  ....*....|....*...
gi 11225607   546 SKFWKHLVYEMPIKKKEM 563
Cdd:pfam01582 148 SKFWKKIAYDISNKLNGT 165
TIR smart00255
Toll - interleukin 1 - resistance;
401-559 4.53e-24

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 98.16  E-value: 4.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607    401 EYDAYLSYtkvdqdtldcdnPEEEQFALEVLPDVLEKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiL 480
Cdd:smart00255   1 EYDVFISY------------SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNY-A 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607    481 RRGWSIFELESRLHNMLVSGEIKVILIECTELKgkvncQEVESLKRSIKLL---SLIKWKGSKSsklnSKFWKHLVYEMP 557
Cdd:smart00255  68 ESEWCLDELVAALENALEEGGLRVIPIFYEVIP-----SDVRKQPGKFRKVfkkNYLKWPEDEK----EQFWKKALYAVP 138


                   ..
gi 11225607    558 IK 559
Cdd:smart00255 139 SK 140
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 31-290 6.89e-16

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 79.29  E-value: 6.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   31 CIDWSVDLKTYMALAGEPVRVKCAlfysyiRTNYSTAQSTGLRLMWYKNKGDLEEPIIFSEvrmskeEDSIWFHSAEAQD 110
Cdd:PHA02785  26 CIDKGQYFASFMELENEPVILPCP------QINTLSSGYNILDILWEKRGADNDRIIPIDN------GSNMLILNPTQSD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  111 SGFYTCVLRNSTYCMKVSMSLT-VAENESGLcynSRIRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKEckPKMWR 189
Cdd:PHA02785  94 SGIYICITKNETYCDMMSLNLTiVSVSESNI---DLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGH--RRLRN 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  190 SIIIQKGNALL-IQEVQEEDGGNYTCELKYegklVRRTTELKVTALLTDKPPKPLFPMENQ-PSVIDVQLGKPLNIPCKA 267
Cdd:PHA02785 169 KRLKQRTPGIItIEDVRKNDAGYYTCVLKY----IYGDKTYNVTRIVKLEVRDRIIPPTMQlPEGVVTSIGSNLTIACRV 244

                        250       260
                 ....*....|....*....|...
gi 11225607  268 FFGfSGESGPMIYWMKGEKFIEE 290
Cdd:PHA02785 245 SLR-PPTTDADVFWISNGMYYEE 266
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 148-231 1.35e-12

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: 64.02  E-value: 1.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607 148 YLEKSEVTKRKEISCPDMDDFKKSDQE-PDVVWYKECKPKMWRSIIIQ-KGNALLIQEVQEEDGGNYTCELKYE--GKL- 222
Cdd:cd20994   3 YKQKVPFTSGGRIVCPHLDFFKDENNNlPKVQWYKDCKPLLLDDKRFAgLESDLLIFNVTVQDQGNYTCHTSYTymGKQy 82

                        90
                ....*....|
gi 11225607 223 -VRRTTELKV 231
Cdd:cd20994  83 nISRTISLIV 92
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 158-234 9.73e-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: 56.06  E-value: 9.73e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11225607 158 KEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYE--GKLVRRTTELKVTAL 234
Cdd:cd20993  14 RTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYEtkGRTIKLTRTVNVKVV 92
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 74-130 1.89e-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. 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: 54.99  E-value: 1.89e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 11225607  74 LMWYKNkgDLEEPIIFSE-VRMSKEEDSIWFHSAEAQDSGFYTCVLRNSTYCMKVSMS 130
Cdd:cd20991  32 ITWYKN--DSKTPISMEQdSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKIT 87
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 405-513 3.29e-09

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 55.01  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   405 YLSYTKVDQDtldcdnpeeeqFALEVLpDVLEKHyGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYiLRRGW 484
Cdd:pfam13676   2 FISYAGEDRA-----------WAEWLA-DALEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNY-LESPW 67

                          90       100       110
                  ....*....|....*....|....*....|.
gi 11225607   485 SIFELESRLHnmLVSGEIKVI--LIECTELK 513
Cdd:pfam13676  68 CRAEWEAALA--DPEGRKRLIpvRLECDLEL 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 250-347 3.55e-07

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: 48.27  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607    250 PSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMK-GEKFIeelaghIREGEIRLLKEHLgekevELALIFDSVVEADLAN 328
Cdd:smart00410   1 PPSVTVKEGESVTLSCEA----SGSPPPEVTWYKqGGKLL------AESGRFSVSRSGS-----TSTLTISNVTPEDSGT 65

                           90
                   ....*....|....*....
gi 11225607    329 YTCHVENRNGRKHASVLLR 347
Cdd:smart00410  66 YTCAATNSSGSASSGTTLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 39-133 2.87e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.96  E-value: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607     39 KTYMALAGEPVRVKCalfysyirtnySTAQSTGLRLMWYKNKGdleEPIIFS---EVRMSKEEDSIWFHSAEAQDSGFYT 115
Cdd:smart00410   2 PSVTVKEGESVTLSC-----------EASGSPPPEVTWYKQGG---KLLAESgrfSVSRSGSTSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*...
gi 11225607    116 CVLRNSTYCMKVSMSLTV 133
Cdd:smart00410  68 CAATNSSGSASSGTTLTV 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 171-231 2.08e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.15  E-value: 2.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11225607   171 SDQEPDVVWYKECKPkmwrsiIIQKGNaLLIQEVQEEDGGNYTCELKYE-GKLVRRTTELKV 231
Cdd:pfam13895  25 GNPPPSYTWYKDGSA------ISSSPN-FFTLSVSAEDSGTYTCVARNGrGGKVSNPVELTV 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 249-335 3.55e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   249 QPSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELALIFDSVVEADLAN 328
Cdd:pfam13927   7 SPSSVTVREGETVTLTCEA----TGSPPPTITWYKNGEPISSGSTRSRS-----------LSGSNSTLTISNVTRSDAGT 71


                  ....*..
gi 11225607   329 YTCHVEN 335
Cdd:pfam13927  72 YTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 159-231 3.87e-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: 42.49  E-value: 3.87e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11225607    159 EISCPdmddfKKSDQEPDVVWYKE-CKPKMWRSIIIQKGNA----LLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 231
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQgGKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 170-215 1.30e-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: 1.30e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 11225607 170 KSDQEPDVVWYKECKP---KMWRSIIIQKGNA-LLIQEVQEEDGGNYTCE 215
Cdd:cd00096   8 SGNPPPTITWYKNGKPlppSSRDSRRSELGNGtLTISNVTLEDSGTYTCV 57
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 160-231 1.32e-04

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: 41.28  E-value: 1.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11225607 160 ISCPDMDDFKKSDQEPDVVWYKECK--PKMWRSIIIQKGNA-LLIQEVQEEDGGNYTCELK--YEGK--LVRRTTELKV 231
Cdd:cd05897  15 LVCPDLSEFTINRTDVEIQWYKDSLllDKDNEKFLSVKGSThLLIHDVSLNDSGYYTCKLTftHEGKkyNITRSIELRI 93
IgI_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member ...
 175-216 3.16e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group 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: 409365  Cd Length: 90  Bit Score: 40.28  E-value: 3.16e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 11225607 175 PDVVWYKECKPkMWRSIIIQKGNALLIQEVQEEDGGNYTCEL 216
Cdd:cd04976  33 PEVVWYKDGLP-LTEKARYLTRHSLIIKEVTEEDTGNYTILL 73
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 76-121 5.89e-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: 38.85  E-value: 5.89e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 11225607  76 WYKNKGDLEEPIIFSeVRMSKEEDSIWFHSAEAQDSGFYTCVLRNS 121
Cdd:cd00096  17 WYKNGKPLPPSSRDS-RRSELGNGTLTISNVTLEDSGTYTCVASNS 61
I-set pfam07679
Immunoglobulin I-set domain;
249-346 9.19e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.78  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   249 QPSVIDVQLGKPLNIPCKAffgfSGESGPMIYWMKGEKfieelagHIREGEIRLLKEhlgeKEVELALIFDSVVEADLAN 328
Cdd:pfam07679   6 KPKDVEVQEGESARFTCTV----TGTPDPEVSWFKDGQ-------PLRSSDRFKVTY----EGGTYTLTISNVQPDDSGK 70

                          90
                  ....*....|....*...
gi 11225607   329 YTCHVENRNGRKHASVLL 346
Cdd:pfam07679  71 YTCVATNSAGEAEASAEL 88
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 272-338 9.39e-04

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 39.07  E-value: 9.39e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11225607 272 SGESGPMIYWMK-GEKFIEElagHiREGEIRLLKEHLgekevelALIFDSVVEADLANYTCHVENRNG 338
Cdd:cd05857  29 AGNPTPTMRWLKnGKEFKQE---H-RIGGYKVRNQHW-------SLIMESVVPSDKGNYTCVVENEYG 85
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 46-218 9.74e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 41.44  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607   46 GEPVRVKCAL-------FY--SYIrTNYSTAQSTGLRLMWYKNKGDLEE--PIIFSEVrmSKEEDSIWFHSAEAQDSGFY 114
Cdd:PHA02826  37 GDPMVLLCTGkhykksiFFdkTFI-TSYNVTWSKTDSLAFVRDSGARTKikKITHNEI--GDRSENLWIGNVINIDEGIY 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607  115 TCVLRNSTYCMKVSMSLTVAENESGLCYNSriryleksevTKRKEISCPDMDDFKKSDQEPDVVWYKEcKPKMWRSIIIQ 194
Cdd:PHA02826 114 ICTISSGNICEESTIRLTFDSGTINYQFNS----------GKDSKLHCYGTDGISSTFKDYTLTWYKN-GNIVLYTDRIQ 182

                        170       180
                 ....*....|....*....|....*..
gi 11225607  195 KGN---ALLIQEVQEEDGGNYTCELKY 218
Cdd:PHA02826 183 LRNnnsTLVIKSATHDDSGIYTCNLRF 209
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
 272-347 1.03e-03

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: 38.67  E-value: 1.03e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11225607 272 SGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELA-LIFDSVVEADLANYTCHVENRNGRKHASVLLR 347
Cdd:cd05894  20 SGEPAPTVTWSRGDKAFTATEGRVRV-----------ESYKDLSsFVIEGAEREDEGVYTITVTNPVGEDHASLFVK 85
IgI_VEGFR-2 cd05864
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); ...
 174-213 1.67e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 2 (VEGFR-2). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-2 (KDR/Flk-1) is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGF-A also interacts with VEGFR-1, which it binds more strongly than VEGFR-2. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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: 409450  Cd Length: 89  Bit Score: 37.99  E-value: 1.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 11225607 174 EPDVVWYKECKPKMWRsIIIQKGNALLIQEVQEEDGGNYT 213
Cdd:cd05864  31 PPEIKWYKNGIPIESN-HTIKAGHVLTIMEVTEKDAGNYT 69
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 261-343 2.60e-03

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: 36.92  E-value: 2.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607 261 LNIPCKAffgfSGESGPMIYWMKGEKFIEELAGHIREgeirllkehlgEKEVELALIFDSVVEADLANYTCHVENRNGRK 340
Cdd:cd00096   1 VTLTCSA----SGNPPPTITWYKNGKPLPPSSRDSRR-----------SELGNGTLTISNVTLEDSGTYTCVASNSAGGS 65


                ...
gi 11225607 341 HAS 343
Cdd:cd00096  66 ASA 68
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 149-233 4.18e-03

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


Pssm-ID: 409368  Cd Length: 88  Bit Score: 37.05  E-value: 4.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11225607 149 LEKSEVTKRKE---ISCpdmddFKKSDQEPdVVWY---KECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELkyeGKL 222
Cdd:cd04979   2 SFKQISVKEGDtviLSC-----SVKSNNAP-VTWIhngKKVPRYRSPRLVLKTERGLLIRSAQEADAGVYECHS---GER 72

                        90
                ....*....|.
gi 11225607 223 VRRTTELKVTA 233
Cdd:cd04979  73 VLGSTLRSVTL 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 171-215 4.38e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.39  E-value: 4.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 11225607   171 SDQEPDVVWYK---ECKPKMWRSIIIQKGNALL-IQEVQEEDGGNYTCE 215
Cdd:pfam13927  27 GSPPPTITWYKngePISSGSTRSRSLSGSNSTLtISNVTRSDAGTYTCV 75
I-set pfam07679
Immunoglobulin I-set domain;
172-231 5.94e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.47  E-value: 5.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11225607   172 DQEPDVVWYKECKP-KMWRSIIIQK--GNA-LLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 231
Cdd:pfam07679  27 TPDPEVSWFKDGQPlRSSDRFKVTYegGTYtLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 175-231 6.28e-03

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: 36.43  E-value: 6.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11225607 175 PDVVWYKECKPKMWRSII-----IQKGNALLIQEVQEEDGGNYTCELKYEGKLVRRTTELKV 231
Cdd:cd05729  34 PNITWLKDGKEFKKEHRIggtkvEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
 175-213 6.84e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1). VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-1 binds VEGF-A strongly; VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-1 may play an inhibitory role in the function of VEGFR-2 by binding VEGF-A and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis and may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. 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: 409499  Cd Length: 92  Bit Score: 36.39  E-value: 6.84e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 11225607 175 PDVVWYKECKPKMWRSI-IIQKGNALLIQEVQEEDGGNYT 213
Cdd:cd07702  33 PEVIWLKDGLPATEKCArYLTRGYSLIIKDVTEEDAGNYT 72
 
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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