NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1258501204|pdb|5XCQ|B]
View 

Chain B, VL-SARAH(M24C) chimera

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 6-111 2.38e-57

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


:

Pssm-ID: 409373  Cd Length: 105  Bit Score: 174.57  E-value: 2.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        6 VVTQESALTTSPGETVTLTCRSSTGAvTTSNYANWVQEKPDHLFTGLIVGTNNRVPGVPPRFSGSLIEDKAALTITGAQT 85
Cdd:cd04984   1 VLTQPSSLSVSPGETVTITCTGSSGN-ISGNYVNWYQQKPGSAPRYLIYEDKHRPSGIPDRFSGSKSGNTASLTISGAQT 79

                        90       100
                ....*....|....*....|....*.
5XCQ_B       86 EDEAIYFCALWYSNHWVFGGGTKLTV 111
Cdd:cd04984  80 EDEADYYCQVWDSNSYVFGGGTKLTV 105
SARAH_MST1 cd21887
C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called ...
 116-164 3.88e-32

C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called serine/threonine-protein kinase 4, MST-1, STE20-like kinase MST1, or serine/threonine-protein kinase (STK) Krs-2, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST1. The MST1 SARAH domain also interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.


:

Pssm-ID: 439181  Cd Length: 49  Bit Score: 108.84  E-value: 3.88e-32
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XCQ_B      116 DYEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:cd21887   1 DYEFLKSWSVEELQRRLASLDPMMEQEIEEIRQKYQSKRQPILDAIEAK 49
 
Name Accession Description Interval E-value
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 6-111 2.38e-57

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409373  Cd Length: 105  Bit Score: 174.57  E-value: 2.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        6 VVTQESALTTSPGETVTLTCRSSTGAvTTSNYANWVQEKPDHLFTGLIVGTNNRVPGVPPRFSGSLIEDKAALTITGAQT 85
Cdd:cd04984   1 VLTQPSSLSVSPGETVTITCTGSSGN-ISGNYVNWYQQKPGSAPRYLIYEDKHRPSGIPDRFSGSKSGNTASLTISGAQT 79

                        90       100
                ....*....|....*....|....*.
5XCQ_B       86 EDEAIYFCALWYSNHWVFGGGTKLTV 111
Cdd:cd04984  80 EDEADYYCQVWDSNSYVFGGGTKLTV 105
SARAH_MST1 cd21887
C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called ...
 116-164 3.88e-32

C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called serine/threonine-protein kinase 4, MST-1, STE20-like kinase MST1, or serine/threonine-protein kinase (STK) Krs-2, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST1. The MST1 SARAH domain also interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.


Pssm-ID: 439181  Cd Length: 49  Bit Score: 108.84  E-value: 3.88e-32
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XCQ_B      116 DYEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:cd21887   1 DYEFLKSWSVEELQRRLASLDPMMEQEIEEIRQKYQSKRQPILDAIEAK 49
Mst1_SARAH pfam11629
C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH ...
 117-164 1.51e-29

C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH domain of Mst1. SARAH controls apoptosis and cell cycle arrest via the Ras, RASSF, MST pathway. The Mst1 SARAH domain interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.


Pssm-ID: 463314  Cd Length: 48  Bit Score: 102.34  E-value: 1.51e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
5XCQ_B        117 YEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:pfam11629   1 FEFLKFLSVDELQQRLANLDPEMEREIEELRKRYQAKRQPILDAIDAK 48
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 8-112 2.22e-19

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 78.27  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B          8 TQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIV--GTNNRVPGVPPRFS--GSLIEDKAALTITGA 83
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAyySNGSEEGVKKGRFSgrGDPSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
5XCQ_B         84 QTEDEAIYFCALWYSNHWVFGGGTKLTVL 112
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 13-111 2.70e-12

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: 59.06  E-value: 2.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B          13 LTTSPGETVTLTCRSSTgavTTSNYANWVQEKPDHLFTglivgtnnrvpgvPPRFSGSLIEDKAALTITGAQTEDEAIYF 92
Cdd:smart00410   4 VTVKEGESVTLSCEASG---SPPPEVTWYKQGGKLLAE-------------SGRFSVSRSGSTSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*....
5XCQ_B          93 CALWYSNHWVFgGGTKLTV 111
Cdd:smart00410  68 CAATNSSGSAS-SGTTLTV 85
 
Name Accession Description Interval E-value
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 6-111 2.38e-57

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409373  Cd Length: 105  Bit Score: 174.57  E-value: 2.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        6 VVTQESALTTSPGETVTLTCRSSTGAvTTSNYANWVQEKPDHLFTGLIVGTNNRVPGVPPRFSGSLIEDKAALTITGAQT 85
Cdd:cd04984   1 VLTQPSSLSVSPGETVTITCTGSSGN-ISGNYVNWYQQKPGSAPRYLIYEDKHRPSGIPDRFSGSKSGNTASLTISGAQT 79

                        90       100
                ....*....|....*....|....*.
5XCQ_B       86 EDEAIYFCALWYSNHWVFGGGTKLTV 111
Cdd:cd04984  80 EDEADYYCQVWDSNSYVFGGGTKLTV 105
SARAH_MST1 cd21887
C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called ...
 116-164 3.88e-32

C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called serine/threonine-protein kinase 4, MST-1, STE20-like kinase MST1, or serine/threonine-protein kinase (STK) Krs-2, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST1. The MST1 SARAH domain also interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.


Pssm-ID: 439181  Cd Length: 49  Bit Score: 108.84  E-value: 3.88e-32
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XCQ_B      116 DYEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:cd21887   1 DYEFLKSWSVEELQRRLASLDPMMEQEIEEIRQKYQSKRQPILDAIEAK 49
Mst1_SARAH pfam11629
C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH ...
 117-164 1.51e-29

C terminal SARAH domain of Mst1; This family of proteins represents the C terminal SARAH domain of Mst1. SARAH controls apoptosis and cell cycle arrest via the Ras, RASSF, MST pathway. The Mst1 SARAH domain interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.


Pssm-ID: 463314  Cd Length: 48  Bit Score: 102.34  E-value: 1.51e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
5XCQ_B        117 YEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:pfam11629   1 FEFLKFLSVDELQQRLANLDPEMEREIEELRKRYQAKRQPILDAIDAK 48
IgV_L_kappa cd04980
Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are ...
 5-111 1.04e-27

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.


Pssm-ID: 409369  Cd Length: 106  Bit Score: 99.39  E-value: 1.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        5 TVVTQESA-LTTSPGETVTLTCRSSTGavTTSNYANWVQEKPDHLFTGLIVGTNNRVPGVPPRFSGSLIEDKAALTITGA 83
Cdd:cd04980   1 IVMTQSPAsLSVSPGERVTISCKASQS--ISSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGSGSGTDFTLTISSV 78

                        90       100
                ....*....|....*....|....*...
5XCQ_B       84 QTEDEAIYFCALWYSNHWVFGGGTKLTV 111
Cdd:cd04980  79 EPEDAAVYYCQQGYTFPYTFGGGTKLEI 106
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 7-111 9.84e-26

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 94.32  E-value: 9.84e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        7 VTQ-ESALTTSPGETVTLTCRSSTGavTTSNYANWVQEKPDHLFTGLI---VGTNNRVPGVPPRFSGSLIEDK-AALTIT 81
Cdd:cd00099   1 VTQsPRSLSVQEGESVTLSCEVSSS--FSSTYIYWYRQKPGQGPEFLIylsSSKGKTKGGVPGRFSGSRDGTSsFSLTIS 78

                        90       100       110
                ....*....|....*....|....*....|...
5XCQ_B       82 GAQTEDEAIYFCALWYS---NHWVFGGGTKLTV 111
Cdd:cd00099  79 NLQPEDSGTYYCAVSESggtDKLTFGSGTRLTV 111
SARAH_MST_Hpo cd21884
C-terminal SARAH domain found in the mammalian STE20-like protein kinase (MST) subfamily; The ...
 117-164 1.52e-25

C-terminal SARAH domain found in the mammalian STE20-like protein kinase (MST) subfamily; The MST subfamily includes MST1 and MST2, as well as Drosophila melanogaster homolog protein, Hippo (Hpo). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 and MST2 are STE20 family stress-activated, pro-apoptotic serine/threonine-protein kinases which, following caspase-cleavage, enter the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. They are key components of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. Hpo, also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation, and promotes apoptosis in conjunction with salvador and warts. Hpo plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain of mammalian STE20-like protein kinases and the Drosophila melanogaster homolog Hippo.


Pssm-ID: 439178  Cd Length: 48  Bit Score: 92.29  E-value: 1.52e-25
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
5XCQ_B      117 YEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:cd21884   1 FEFLKSLSYEELQERLALLDPEMEREIEELRKRYQAKRQPILDAIEAK 48
SARAH_MST2 cd21888
C-terminal SARAH domain of mammalian STE20-like protein kinase 2 (MST2); MST2, also called ...
 116-164 2.52e-21

C-terminal SARAH domain of mammalian STE20-like protein kinase 2 (MST2); MST2, also called serine/threonine-protein kinase 3, MST-2, STE20-like kinase MST2, or serine/threonine-protein kinase (STK) Krs-1, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST2. Similar to MST1, MST2 may also form heterodimers with other SARAH domain-containing proteins.


Pssm-ID: 439182  Cd Length: 49  Bit Score: 81.57  E-value: 2.52e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XCQ_B      116 DYEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:cd21888   1 DFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAK 49
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 8-112 2.22e-19

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 78.27  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B          8 TQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIV--GTNNRVPGVPPRFS--GSLIEDKAALTITGA 83
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAyySNGSEEGVKKGRFSgrGDPSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
5XCQ_B         84 QTEDEAIYFCALWYSNHWVFGGGTKLTVL 112
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
SARAH_Hpo cd21889
C-terminal SARAH domain of Drosophila melanogaster protein Hippo (Hpo) and similar proteins; ...
 115-164 2.51e-18

C-terminal SARAH domain of Drosophila melanogaster protein Hippo (Hpo) and similar proteins; Hpo, also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation, and promotes apoptosis in conjunction with salvador and warts. Hpo plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain of Hpo, which mediates complex formation between Hpo and Sav, as well as homodimerization.


Pssm-ID: 439183  Cd Length: 56  Bit Score: 74.13  E-value: 2.51e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
5XCQ_B      115 SDYEFLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEAK 164
Cdd:cd21889   1 GEFDFLKFLTYDDLNQRLANIDSEMEREIEELNKRYHAKRQPILDAMDAK 50
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 7-111 8.11e-16

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 68.84  E-value: 8.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        7 VTQ-ESALTTSPGETVTLTCRSSTgavTTSNYANWVQEKPDHLFTGLIVGTNNRVPGVPPRFSGSLIEDK--AALTITGA 83
Cdd:cd04983   1 VTQsPQSLSVQEGENVTLNCNYST---STFYYLFWYRQYPGQGPQFLIYISSDSGNKKKGRFSATLDKSRksSSLHISAA 77

                        90       100       110
                ....*....|....*....|....*....|.
5XCQ_B       84 QTEDEAIYFCAL--WYSNH-WVFGGGTKLTV 111
Cdd:cd04983  78 QLSDSAVYFCALseSGGTGkLTFGKGTRLTV 108
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 7-111 6.59e-13

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409503  Cd Length: 112  Bit Score: 61.38  E-value: 6.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        7 VTQESALTTSP-GETVTLTCRSSTgaVTTSNYANWVQEKPDHLFTGLIVGTNNRVPGVPPRFSGSLIE-DKA-ALTITGA 83
Cdd:cd07706   2 VTQAQPDVSVQvGEEVTLNCRYET--SWTNYYLFWYKQLPSGEMTFLIRQDSSEQNAKSGRYSVNFQKaQKSiSLTISAL 79

                        90       100       110
                ....*....|....*....|....*....|.
5XCQ_B       84 QTEDEAIYFCAL---WYSNHWVFGGGTKLTV 111
Cdd:cd07706  80 QLEDSAKYFCALslpYDTDKLIFGKGTRLTV 110
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 13-111 2.70e-12

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: 59.06  E-value: 2.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B          13 LTTSPGETVTLTCRSSTgavTTSNYANWVQEKPDHLFTglivgtnnrvpgvPPRFSGSLIEDKAALTITGAQTEDEAIYF 92
Cdd:smart00410   4 VTVKEGESVTLSCEASG---SPPPEVTWYKQGGKLLAE-------------SGRFSVSRSGSTSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*....
5XCQ_B          93 CALWYSNHWVFgGGTKLTV 111
Cdd:smart00410  68 CAATNSSGSAS-SGTTLTV 85
IGv smart00406
Immunoglobulin V-Type;
20-94 3.37e-12

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 58.93  E-value: 3.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B          20 TVTLTCRSSTGAvTTSNYANWVQEKPDHLFTGLIVGTNNRV----PGVPPRFSGSLIEDK--AALTITGAQTEDEAIYFC 93
Cdd:smart00406   1 SVTLSCKFSGST-FSSYYVSWVRQPPGKGLEWLGYIGSNGSsyyqESYKGRFTISKDTSKndVSLTISNLRVEDTGTYYC 79


                   .
5XCQ_B          94 A 94
Cdd:smart00406  80 A 80
SARAH_SF cd21883
C-terminal SARAH domain found in scaffold protein salvador (Sav), Ras-association domain ...
 119-163 9.15e-12

C-terminal SARAH domain found in scaffold protein salvador (Sav), Ras-association domain proteins, and mammalian STE20-like protein kinases (MST); The SARAH (Salvador-RassF-Hippo) domain family includes scaffold protein salvador (Sav), Ras-association domain proteins (RASSF1-6), and mammalian STE20-like protein kinase (MST) subfamily members (MST1-2 and Hippo). Sav is a scaffold protein mainly found in metazoans. Drosophila melanogaster Sav, also called Shar-pei (SHRP), promotes both cell cycle exit and apoptosis in Drosophila. It plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Human protein salvador homolog 1, also called 45 kDa WW domain protein (WW45), acts as a mammalian sterile 20-like kinase 1 (MST1)-binding protein required to enhance MST1-mediated apoptosis. It is a regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway. Classical RASSF proteins interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. They seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. RASSF1-6 contains a conserved SARAH motif adjacent to the RA domain that functions in scaffolding and regulatory interactions. MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 and MST2 are STE20 family stress-activated, pro-apoptotic serine/threonine-protein kinases which, following caspase-cleavage, enter the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. They are key components of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. Hippo (Hpo), also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation and promotes apoptosis in conjunction with salvador and warts. Hpo also plays a key role in the Hippo/SWH signaling pathway. This model corresponds to the C-terminal SARAH domain, a characteristic coiled-coil structure. It is a small helical module that is important in signal-transduction networks. The central function of the SARAH domain seems to be the mediation of homo- and heterodimerization between SARAH domain-containing proteins.


Pssm-ID: 439177  Cd Length: 45  Bit Score: 56.64  E-value: 9.15e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
5XCQ_B      119 FLKSWTVEDLQKRLLALDPMCEQEIEEIRQKYQSKRQPILDAIEA 163
Cdd:cd21883   1 QLKNFSLPELQMFLKMLDPEEEREIEQLVKKYTAYRQAILDALEE 45
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 9-111 1.31e-10

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigens as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain the standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409371  Cd Length: 117  Bit Score: 55.45  E-value: 1.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        9 QESALTTSPGETVTLTCRSStGAVTTSNYANWVQEKPD----HLFTGLIVGTNNRVPGVPP-RFSGSLIEDK--AALTIT 81
Cdd:cd04982   4 PQLSITREESKSVTISCKVS-GIDFSTTYIHWYRQKPGqaleRLLYVSSTSAVRKDSGKTKnKFEARKDVGKstSTLTIT 82

                        90       100       110
                ....*....|....*....|....*....|....
5XCQ_B       82 GAQTEDEAIYFCALW--YSNHW--VFGGGTKLTV 111
Cdd:cd04982  83 NLEKEDSATYYCAYWesGSGYYikVFGSGTKLIV 116
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
 7-111 3.73e-10

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here are composed of the immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409480  Cd Length: 110  Bit Score: 54.21  E-value: 3.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        7 VTQE-SALTTSPGETVTLTCRSSTGAvttsNYANWVQEKPDH----LFTgLIVGTNNRVPGVPP-RFSGSLIED-KAALT 79
Cdd:cd05899   1 VTQSpRYLIKRRGQSVTLRCSQKSGH----DNMYWYRQDPGKglqlLFY-SYGGGLNEEGDLPGdRFSASRPSLtRSSLT 75

                        90       100       110
                ....*....|....*....|....*....|....*
5XCQ_B       80 ITGAQTEDEAIYFCAL---WYSNHWVFGGGTKLTV 111
Cdd:cd05899  76 IKSAEPEDSAVYLCASslgGGADEAYFGPGTRLTV 110
IgV_H cd04981
Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the ...
 9-111 4.58e-09

Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains.


Pssm-ID: 409370 [Multi-domain]  Cd Length: 118  Bit Score: 51.54  E-value: 4.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        9 QES-ALTTSPGETVTLTCRSStGAVTTSNYANWVQEKPDH--LFTGLIV---GTNNRVPGVPPRFSGSLIEDK--AALTI 80
Cdd:cd04981   3 QESgPGLVKPGQSLKLSCKAS-GFTFTSYGMGWVRQAPGKglEWIGLIYpggGDTYYADSFKGRFTITRDTSKstAYLQL 81

                        90       100       110
                ....*....|....*....|....*....|....*...
5XCQ_B       81 TGAQTEDEAIYFCA-------LWYSNHWvfGGGTKLTV 111
Cdd:cd04981  82 NSLTSEDTAVYYCArglggygYSYFDYW--GQGTTVTV 117
IgV_TCR_gammadelta cd20988
Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the ...
 6-111 4.86e-09

Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409580  Cd Length: 114  Bit Score: 51.40  E-value: 4.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B        6 VVTQESALTTSPGETVTLTCrSSTGAVTTSNYANWVQEKPDHLFTGLIVGTNNRVPGVPPRFSGSL--IEDKAALTITGA 83
Cdd:cd20988   1 LVPEHQTVTVSVGKPVTLKC-SMKGEAISNYYINWYRKTQGNTMTFIYREGGIYGPGFKDNFRGDIdsSNNLAVLKILEA 79

                        90       100       110
                ....*....|....*....|....*....|....
5XCQ_B       84 QTEDEAIYFCA------LWYSNHWVFGGGTKLTV 111
Cdd:cd20988  80 SERDEGSYYCAsdtpggGREYDPLIFGKGTYLTV 113
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 13-100 1.94e-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: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B         13 LTTSPGETVTLTCRSSTGavTTSNYANWVQEKPDHLFTGLIVGTNNRvpgvppRFSGSliedkaaLTITGAQTEDEAIYF 92
Cdd:pfam00047   6 VTVLEGDSATLTCSASTG--SPGPDVTWSKEGGTLIESLKVKHDNGR------TTQSS-------LLISNVTKEDAGTYT 70


                  ....*...
5XCQ_B         93 CALWYSNH 100
Cdd:pfam00047  71 CVVNNPGG 78
IgV_CD8_beta cd07700
Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The ...
 11-111 2.42e-03

Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409497  Cd Length: 116  Bit Score: 35.89  E-value: 2.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCQ_B       11 SALTTSPGETVTLTCRSSTGAVTTSNYanWVQEKPDHL------FTGLIVGTNNRVPG---VPPRFSGSLIEDKAA--LT 79
Cdd:cd07700   6 GSLLVQTNQTVKMSCEAKTSPKNTRIY--WLRQRQAPSkdshfeFLASWDPSKGIVYGegvDQEKLIILSDSDSSRyiLS 83

                        90       100       110
                ....*....|....*....|....*....|..
5XCQ_B       80 ITGAQTEDEAIYFCALWYSNHWVFGGGTKLTV 111
Cdd:cd07700  84 LMSVKPEDSGTYFCMTVGSPELIFGTGTKLSV 115
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH