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Conserved domains on  [gi|1767893484|ref|NP_001362226|]
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low affinity immunoglobulin gamma Fc region receptor II-a isoform 4 precursor [Homo sapiens]

Protein Classification

Ig1_FcgammaR_like and Ig2_FcgammaR_like domain-containing protein( domain architecture ID 10146245)

Ig1_FcgammaR_like and Ig2_FcgammaR_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig2_FcgammaR_like cd05753
Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
122-204 1.24e-47

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


:

Pssm-ID: 409411  Cd Length: 83  Bit Score: 153.23  E-value: 1.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484 122 WLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVT 201
Cdd:cd05753     1 WLLLQAPSAVVFEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSESVN 80

                  ...
gi 1767893484 202 ITV 204
Cdd:cd05753    81 ITV 83
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
40-118 4.62e-37

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


:

Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 125.94  E-value: 4.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  40 AVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTqPSYRFK-ANNNDSGEYTCQTGQTSLSDPVHLTV 118
Cdd:cd05752     1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTS-SSYRIVaATVNDSGEYRCQTQGSSLSDPVHLEV 79
 
Name Accession Description Interval E-value
Ig2_FcgammaR_like cd05753
Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
122-204 1.24e-47

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409411  Cd Length: 83  Bit Score: 153.23  E-value: 1.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484 122 WLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVT 201
Cdd:cd05753     1 WLLLQAPSAVVFEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSESVN 80

                  ...
gi 1767893484 202 ITV 204
Cdd:cd05753    81 ITV 83
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
40-118 4.62e-37

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 125.94  E-value: 4.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  40 AVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTqPSYRFK-ANNNDSGEYTCQTGQTSLSDPVHLTV 118
Cdd:cd05752     1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTS-SSYRIVaATVNDSGEYRCQTQGSSLSDPVHLEV 79
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
122-201 3.27e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 433563 [Multi-domain]  Cd Length: 76  Bit Score: 49.71  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484 122 WLVLQTPHLEFQEGETIMLRCHSWkDKPLVKVTFFQNGKSQKFShldPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVT 201
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSAP-GNPPASYTWYKGGEALNSS---PNFFILAVSAEDSGTYTCVARNGRGGKVSNPVE 76
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
42-115 4.92e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 433563 [Multi-domain]  Cd Length: 76  Bit Score: 49.32  E-value: 4.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767893484  42 LKLEPPWINVLQEDSVTLTCQgARSPESDSIQWFHNGNLIPTHtQPSYRFKANNNDSGEYTCQTGQTS---LSDPVH 115
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCS-APGNPPASYTWYKGGEALNSS-PNFFILAVSAEDSGTYTCVARNGRggkVSNPVE 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
128-204 8.02e-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: 45.96  E-value: 8.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  128 PHLEFQEGETIMLRCH---------SWKDKPLVKVtFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSk 198
Cdd:smart00410   2 PSVTVKEGESVTLSCEasgspppevTWYKQGGKLL-AESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS- 79

                   ....*.
gi 1767893484  199 PVTITV 204
Cdd:smart00410  80 GTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
46-118 5.32e-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: 43.65  E-value: 5.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484   46 PPWINVLQEDSVTLTCQgARSPESDSIQWFHNG----------NLIPTHTQPSYRFK-ANNNDSGEYTCQ--TGQTSLSD 112
Cdd:smart00410   1 PPSVTVKEGESVTLSCE-ASGSPPPEVTWYKQGgkllaesgrfSVSRSGSTSTLTISnVTPEDSGTYTCAatNSSGSASS 79

                   ....*.
gi 1767893484  113 PVHLTV 118
Cdd:smart00410  80 GTTLTV 85
 
Name Accession Description Interval E-value
Ig2_FcgammaR_like cd05753
Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
122-204 1.24e-47

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409411  Cd Length: 83  Bit Score: 153.23  E-value: 1.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484 122 WLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVT 201
Cdd:cd05753     1 WLLLQAPSAVVFEGEPLTLRCHGWKDKKVHKVTYYKDGKALKFSYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSESVN 80

                  ...
gi 1767893484 202 ITV 204
Cdd:cd05753    81 ITV 83
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
40-118 4.62e-37

First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 125.94  E-value: 4.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  40 AVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTqPSYRFK-ANNNDSGEYTCQTGQTSLSDPVHLTV 118
Cdd:cd05752     1 AVVSLDPPWTTVFQGEKVTLTCQGFYSPEQNSTQWYHNGTLISSTS-SSYRIVaATVNDSGEYRCQTQGSSLSDPVHLEV 79
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
122-201 3.27e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 433563 [Multi-domain]  Cd Length: 76  Bit Score: 49.71  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484 122 WLVLQTPHLEFQEGETIMLRCHSWkDKPLVKVTFFQNGKSQKFShldPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVT 201
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSAP-GNPPASYTWYKGGEALNSS---PNFFILAVSAEDSGTYTCVARNGRGGKVSNPVE 76
IgC2_D1_D2_LILR_KIR_like cd16843
Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer ...
51-118 4.32e-08

Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains; The members here are composed of the first and second immunoglobulin (Ig)-like domains found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules.


Pssm-ID: 409518 [Multi-domain]  Cd Length: 90  Bit Score: 49.69  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  51 VLQEDSVTLTCQGArsPESDSIQWFHNGNLIPTHTQ--PSYRFKAN-------NNDSGEYTCQ----TGQTSLSDPVHLT 117
Cdd:cd16843    12 VPLGENVTIRCQGP--PEAVLFQLYKEGNSLSQGTVreKEPQNKAEfyiphmdRNHAGRYRCRyrsgTLWSEPSDPLELV 89

                  .
gi 1767893484 118 V 118
Cdd:cd16843    90 V 90
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
42-115 4.92e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 433563 [Multi-domain]  Cd Length: 76  Bit Score: 49.32  E-value: 4.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767893484  42 LKLEPPWINVLQEDSVTLTCQgARSPESDSIQWFHNGNLIPTHtQPSYRFKANNNDSGEYTCQTGQTS---LSDPVH 115
Cdd:pfam13895   2 PVLTPSPTVVTEGEPVTLTCS-APGNPPASYTWYKGGEALNSS-PNFFILAVSAEDSGTYTCVARNGRggkVSNPVE 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
37-104 2.44e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 47.19  E-value: 2.44e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767893484  37 PPkaVLKLEPPWINVLQEDSVTLTCQGARSPESdSIQWFHNGNLIPTHTQPSYRF-------KANNNDSGEYTCQ 104
Cdd:pfam13927   1 KP--VITVSPSSVVVVEGETVTLTCEASGSPPP-TITWYKNGGKLSSGRTSLVGGngtltisNVTREDSGTYTCT 72
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
128-204 8.02e-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: 45.96  E-value: 8.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  128 PHLEFQEGETIMLRCH---------SWKDKPLVKVtFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSk 198
Cdd:smart00410   2 PSVTVKEGESVTLSCEasgspppevTWYKQGGKLL-AESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS- 79

                   ....*.
gi 1767893484  199 PVTITV 204
Cdd:smart00410  80 GTTLTV 85
Ig_4 pfam16680
T-cell surface glycoprotein CD3 delta chain; This is an immunoglobulin-like domain. It is ...
54-109 4.41e-06

T-cell surface glycoprotein CD3 delta chain; This is an immunoglobulin-like domain. It is found on the T-cell surface glycoprotein CD3 delta chain. CD3delta and CD3epsilon complex together as part of the T-cell receptor complex.


Pssm-ID: 435510  Cd Length: 63  Bit Score: 43.39  E-value: 4.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1767893484  54 EDSVTLTCQGarspESDSIQWFHNGNLIPTHTQPSYRF-KANNNDSGEYTCQTGQTS 109
Cdd:pfam16680   1 EDKVFLTCNS----SSKSITWLKGGKGILSTNNKTLDLgKRILDPRGTYQCQGEKKK 53
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
46-118 5.32e-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: 43.65  E-value: 5.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484   46 PPWINVLQEDSVTLTCQgARSPESDSIQWFHNG----------NLIPTHTQPSYRFK-ANNNDSGEYTCQ--TGQTSLSD 112
Cdd:smart00410   1 PPSVTVKEGESVTLSCE-ASGSPPPEVTWYKQGgkllaesgrfSVSRSGSTSTLTISnVTPEDSGTYTCAatNSSGSASS 79

                   ....*.
gi 1767893484  113 PVHLTV 118
Cdd:smart00410  80 GTTLTV 85
IgC2_D1_LILR_KIR_like cd05751
First immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs), Natural ...
51-118 7.90e-06

First immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains; The members here are composed of the first immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors (LILRs) and Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules.


Pssm-ID: 409409  Cd Length: 88  Bit Score: 43.20  E-value: 7.90e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1767893484  51 VLQEDSVTLTCQGarSPESDSIQWFHNGNLIPTHTQPSYRFKA-------NNNDSGEYTCQ----TGQTSLSDPVHLTV 118
Cdd:cd05751    12 IPLEKSVTIRCQG--TPEAFLYQLEKEGNSTETVIPKKPQKKAefiiphmNSRTAGRYRCRyrkgAGWSEPSDLLELVV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
57-104 1.53e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.93  E-value: 1.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1767893484  57 VTLTCQGARSPESdSIQWFHNGNLIPTHTQPSYRFKANN----------NDSGEYTCQ 104
Cdd:cd00096     1 VTLTCSASGNPPP-TITWYKNGKPLPPSSRDSRRSELGNgtltisnvtlEDSGTYTCV 57
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
51-103 7.90e-05

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: 40.45  E-value: 7.90e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767893484  51 VLQEDSVTLTCQGARSPESdSIQWFHNGNLIpthTQPSYRFKANNN----------DSGEYTC 103
Cdd:cd20978    13 VKGGQDVTLPCQVTGVPQP-KITWLHNGKPL---QGPMERATVEDGtltiinvqpeDTGYYGC 71
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
51-119 9.16e-05

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 40.46  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  51 VLQEDSVTLTCqgarSPES--DSIQWFHNGNLIPTHtqPSYRFKANN----------NDSGEYTCQTGQ---TSLSDPVH 115
Cdd:cd05740    12 VEDKDAVTLTC----EPETqnTSYLWWFNGQSLPVT--PRLTLSNGNrtltllnvtrEDAGAYQCEISNpvsANRSDPVT 85

                  ....
gi 1767893484 116 LTVL 119
Cdd:cd05740    86 LDVI 89
I-set pfam07679
Immunoglobulin I-set domain;
38-104 1.28e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1767893484  38 PKAVLKLEPpwINVLQEDSVTLTCQGARSPESdSIQWFHNGnlIPTHTQPSYRFKANNN------------DSGEYTCQ 104
Cdd:pfam07679   1 PKFTQKPKD--VEVQEGESARFTCTVTGTPDP-EVSWFKDG--QPLRSSDRFKVTYEGGtytltisnvqpdDSGKYTCV 74
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
51-118 1.79e-04

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 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 Ig 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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 39.40  E-value: 1.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767893484  51 VLQEDSVTLTCQGARSPeSDSIQWFHNGNLIPTH-----TQP--SYRFK-ANNNDSGEYTCQTGQTSLSDPVHLTV 118
Cdd:cd20952    11 VAVGGTVVLNCQATGEP-VPTISWLKDGVPLLGKderitTLEngSLQIKgAEKSDTGEYTCVALNLSGEATWSAVL 85
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
51-103 2.07e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 39.41  E-value: 2.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767893484  51 VLQEDSVTLTCQGARSPESDsIQWFHNGNLIPTHTQpSYRFKANNN----------DSGEYTC 103
Cdd:cd20970    14 AREGENATFMCRAEGSPEPE-ISWTRNGNLIIEFNT-RYIVRENGTtltirnirrsDMGIYLC 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
44-105 8.01e-04

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 37.56  E-value: 8.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767893484  44 LEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNlipTHTQPSYRFKANN--------------NDSGEYTCQT 105
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGG---TLIESLKVKHDNGrttqssllisnvtkEDAGTYTCVV 73
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
123-187 8.96e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 37.18  E-value: 8.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484 123 LVLQTPHLEFQEGETIMLRCHSwKDKPLVKVTFFQNGKSQKFSHLDP-----TFSIPQANHSHSGDYHCT 187
Cdd:pfam13927   4 ITVSPSSVVVVEGETVTLTCEA-SGSPPPTITWYKNGGKLSSGRTSLvggngTLTISNVTREDSGTYTCT 72
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
46-119 1.77e-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: 36.67  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767893484  46 PPWINVLQEDSVTLTC--QGARSPESdsiqWFHNGNLIPTHTQPSYR---------FKANNNDSGEYTCQTGQT---SLS 111
Cdd:cd04979     3 FKQISVKEGDTVILSCsvKSNNAPVT----WIHNGKKVPRYRSPRLVlkterglliRSAQEADAGVYECHSGERvlgSTL 78

                  ....*...
gi 1767893484 112 DPVHLTVL 119
Cdd:cd04979    79 RSVTLHVL 86
IgC2_D1_D2_LILR_KIR_like cd16843
Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer ...
135-204 3.30e-03

Immunoglobulin (Ig)-like domain found in Leukocyte Ig-like receptors, Natural killer inhibitory receptors (KIRs) and similar domains; member of Immunoglobulin Constant-2 set of IgSF domains; The members here are composed of the first and second immunoglobulin (Ig)-like domains found in Leukocyte Ig-like receptors (LILRs), Natural killer inhibitory receptors (KIRs, also known as also known as cluster of differentiation (CD) 158), and similar proteins. This group includes LILRB1 (also known as LIR-1), LILRA5 (also known as LIR9), an activating natural cytotoxicity receptor NKp46, the immune-type receptor glycoprotein VI (GPVI), and the IgA-specific receptor Fc-alphaRI (also known as cluster of differentiation (CD) 89). LILRs are a family of immunoreceptors expressed on expressed on T and B cells, on monocytes, dendritic cells, and subgroups of natural killer (NK) cells. The human LILR family contains nine proteins (LILRA1-3, and 5, and LILRB1-5). From functional assays, and as the cytoplasmic domains of various LILRs, for example LILRB1, LILRB2 (also known as LIR-2), and LILRB3 (also known as LIR-3) contain immunoreceptor tyrosine-based inhibitory motifs (ITIMs), it is thought that LIR proteins are inhibitory receptors. Of the eight LIR family proteins, only LILRB1, and LILRB2, show detectable binding to class I MHC molecules; ligands for the other members have yet to be determined. The extracellular portions of the different LIR proteins contain different numbers of Ig-like domains for example, four in the case of LILRB1, and LILRB2, and two in the case of LILRB4 (also known as LIR-5). The activating natural cytotoxicity receptor NKp46 is expressed in natural killer cells, and is organized as an extracellular portion having two Ig-like extracellular domains, a transmembrane domain, and a small cytoplasmic portion. GPVI, which also contains two Ig-like domains, participates in the processes of collagen-mediated platelet activation and arterial thrombus formation. Fc-alphaRI is expressed on monocytes, eosinophils, neutrophils, and macrophages; it mediates IgA-induced immune effector responses such as phagocytosis, antibody-dependent cell-mediated cytotoxicity and respiratory burst. Killer cell immunoglobulin-like receptors (KIRs; also known as CD158 for human KIR) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. KIRs are a family of highly polymorphic activating and inhibitory receptors that serve as key regulators of human NK cell function. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The major ligands for KIR are MHC class I (HLA-A, -B or -C) molecules.


Pssm-ID: 409518 [Multi-domain]  Cd Length: 90  Bit Score: 35.82  E-value: 3.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767893484 135 GETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPT-----FSIPQANHSHSGDYHCTGNIGyTLFS--SKPVTITV 204
Cdd:cd16843    15 GENVTIRCQGPPEAVLFQLYKEGNSLSQGTVREKEPqnkaeFYIPHMDRNHAGRYRCRYRSG-TLWSepSDPLELVV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
130-189 3.55e-03

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 35.63  E-value: 3.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1767893484 130 LEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDP---------TFSIPQANHSHSGDYHCTGN 189
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKhdngrttqsSLLISNVTKEDAGTYTCVVN 74
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
70-118 6.36e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group 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 Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 35.24  E-value: 6.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767893484  70 DSIQWFHNGNLIPTHtqpsYRFKANNN------------DSGEYTC----QTGQTSLSDpVHLTV 118
Cdd:cd20958    30 SSITWEKDGRRLPLN----HRQRVFPNgtlvienvqrssDEGEYTCtarnQQGQSASRS-VFVKV 89
I-set pfam07679
Immunoglobulin I-set domain;
124-187 9.66e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 34.54  E-value: 9.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767893484 124 VLQTPH-LEFQEGETIMLRCHSWKDkPLVKVTFFQNGK--------SQKFSHLDPTFSIPQANHSHSGDYHCT 187
Cdd:pfam07679   3 FTQKPKdVEVQEGESARFTCTVTGT-PDPEVSWFKDGQplrssdrfKVTYEGGTYTLTISNVQPDDSGKYTCV 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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