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Conserved domains on  [gi|283436188|ref|NP_084457|]
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V-set and immunoglobulin domain-containing protein 1 isoform 1 precursor [Mus musculus]

Protein Classification

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 ...
 23-129 4.04e-19

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


The actual alignment was detected with superfamily member cd05715:

Pssm-ID: 472250  Cd Length: 117  Bit Score: 82.48  E-value: 4.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  23 VQVTIPDTfVNVTVGSNVTLLCLYTTTEKSLEKLSIQWSFfHNKEMEEPISIYYSEGGQA--SAIGQFKDRIIGATNPG- 99
Cdd:cd05715    1 MEVYTPRE-LNVLNGSDVRLTCTFTSCYTVGDAFSVTWTY-QPEGGNTTESMFHYSKGKPyiLKVGRFKDRVSWAGNPSk 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 283436188 100 -NASITILHMQPADSGIYICDVNNPPDFVGK 129
Cdd:cd05715   79 kDASIVISNLQFSDNGTYTCDVKNPPDIVGG 109
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 154-229 1.07e-08

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


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 1.07e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283436188   154 EAGHPISLSClSAFGTPSPLYYWYKIEGNTIVP---VKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:smart00410   7 KEGESVTLSC-EASGSPPPEVTWYKQGGKLLAEsgrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
Trypan_PARP super family cl42451
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 314-359 2.22e-05

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


The actual alignment was detected with superfamily member pfam05887:

Pssm-ID: 368653  Cd Length: 134  Bit Score: 44.01  E-value: 2.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 283436188  314 EPTTTAVLEPEYEPNPPLETTTQPDPEPEgsvPVLAPEAEIQPHPE 359
Cdd:pfam05887  68 EPEPEPEPEPEPEPEPEPEPEPEPEPEPE---PEPEPEPEPEPEPE 110
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 261-359 1.71e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.52  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188 261 NKVKSKQQKNLN------SSTELEPMTKVHHPQQSEAISadgvQLEGTLPSSIHAGHNTEPTTTAVLEPEYEPNPPLETT 334
Cdd:NF033839 103 NKLQNIKNEYLNkivestSKSQLQKLMMESQSKVDEAVS----KFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPD 178

                         90       100
                 ....*....|....*....|....*
gi 283436188 335 TQPDPEPEGSVPvlaPEAEIQPHPE 359
Cdd:NF033839 179 TKPSPQPEGKKP---SVPDINQEKE 200
 
Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 23-129 4.04e-19

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 82.48  E-value: 4.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  23 VQVTIPDTfVNVTVGSNVTLLCLYTTTEKSLEKLSIQWSFfHNKEMEEPISIYYSEGGQA--SAIGQFKDRIIGATNPG- 99
Cdd:cd05715    1 MEVYTPRE-LNVLNGSDVRLTCTFTSCYTVGDAFSVTWTY-QPEGGNTTESMFHYSKGKPyiLKVGRFKDRVSWAGNPSk 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 283436188 100 -NASITILHMQPADSGIYICDVNNPPDFVGK 129
Cdd:cd05715   79 kDASIVISNLQFSDNGTYTCDVKNPPDIVGG 109
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 32-137 1.54e-13

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: 66.33  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188   32 VNVTVGSNVTLLCLYTTTEkSLEKLSIQWSFFHNKEMEEPISIYYSEGGQasaIGQFKDRIIGATNP--GNASITILHMQ 109
Cdd:pfam07686   6 VTVALGGSVTLPCTYSSSM-SEASTSVYWYRQPPGKGPTFLIAYYSNGSE---EGVKKGRFSGRGDPsnGDGSLTIQNLT 81

                          90       100
                  ....*....|....*....|....*...
gi 283436188  110 PADSGIYICDVNNPPDFVGKNQGLLDVT 137
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 154-229 1.07e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 1.07e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283436188   154 EAGHPISLSClSAFGTPSPLYYWYKIEGNTIVP---VKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:smart00410   7 KEGESVTLSC-EASGSPPPEVTWYKQGGKLLAEsgrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 144-217 5.26e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.87  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  144 KPFCTIQGRPEA---GHPISLSClSAFGTPSPLYYWYKiEGNTIVPV---KESFNTATGVLVIGNLTNFEQGYYQCTAIN 217
Cdd:pfam13927   1 KPVITVSPSSVTvreGETVTLTC-EATGSPPPTITWYK-NGEPISSGstrSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 32-138 3.04e-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: 45.19  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188    32 VNVTVGSNVTLLCLYTTTEKSleklSIQWSFFHNKEMeepisiyyseggqasaigQFKDRIIGATNPGNASITILHMQPA 111
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPP----EVTWYKQGGKLL------------------AESGRFSVSRSGSTSTLTISNVTPE 61

                           90       100
                   ....*....|....*....|....*..
gi 283436188   112 DSGIYICDVNNPpdfVGKNQGLLDVTV 138
Cdd:smart00410  62 DSGTYTCAATNS---SGSASSGTTLTV 85
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 156-229 3.35e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 44.71  E-value: 3.35e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 283436188 156 GHPISLSCLsAFGTPSPLYYWYKIEGNTI--VPVKESFNTAtgvLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:cd05731   10 GGVLLLECI-AEGLPTPDIRWIKLGGELPkgRTKFENFNKT---LKIENVSEADSGEYQCTASNTMGSARHTISVT 81
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 314-359 2.22e-05

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 44.01  E-value: 2.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 283436188  314 EPTTTAVLEPEYEPNPPLETTTQPDPEPEgsvPVLAPEAEIQPHPE 359
Cdd:pfam05887  68 EPEPEPEPEPEPEPEPEPEPEPEPEPEPE---PEPEPEPEPEPEPE 110
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 261-359 1.71e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.52  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188 261 NKVKSKQQKNLN------SSTELEPMTKVHHPQQSEAISadgvQLEGTLPSSIHAGHNTEPTTTAVLEPEYEPNPPLETT 334
Cdd:NF033839 103 NKLQNIKNEYLNkivestSKSQLQKLMMESQSKVDEAVS----KFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPD 178

                         90       100
                 ....*....|....*....|....*
gi 283436188 335 TQPDPEPEGSVPvlaPEAEIQPHPE 359
Cdd:NF033839 179 TKPSPQPEGKKP---SVPDINQEKE 200
 
Name Accession Description Interval E-value
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 23-129 4.04e-19

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 82.48  E-value: 4.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  23 VQVTIPDTfVNVTVGSNVTLLCLYTTTEKSLEKLSIQWSFfHNKEMEEPISIYYSEGGQA--SAIGQFKDRIIGATNPG- 99
Cdd:cd05715    1 MEVYTPRE-LNVLNGSDVRLTCTFTSCYTVGDAFSVTWTY-QPEGGNTTESMFHYSKGKPyiLKVGRFKDRVSWAGNPSk 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 283436188 100 -NASITILHMQPADSGIYICDVNNPPDFVGK 129
Cdd:cd05715   79 kDASIVISNLQFSDNGTYTCDVKNPPDIVGG 109
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 29-129 1.28e-15

Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 72.60  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  29 DTFVNVTVGSNVTLLCLYTTTEKSLEKLSIQWSFF--HNKEMeepISIYYSEGGQAS--AIGQFKDRIIGATNPG--NAS 102
Cdd:cd05879    6 DREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQpdGSRDA---ISIFHYGKGQPYidNVGPFKERIEWVGNPSrkDGS 82

                         90       100
                 ....*....|....*....|....*..
gi 283436188 103 ITILHMQPADSGIYICDVNNPPDFVGK 129
Cdd:cd05879   83 IVIHNLDYTDNGTFTCDVKNPPDIVGK 109
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 32-137 1.54e-13

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: 66.33  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188   32 VNVTVGSNVTLLCLYTTTEkSLEKLSIQWSFFHNKEMEEPISIYYSEGGQasaIGQFKDRIIGATNP--GNASITILHMQ 109
Cdd:pfam07686   6 VTVALGGSVTLPCTYSSSM-SEASTSVYWYRQPPGKGPTFLIAYYSNGSE---EGVKKGRFSGRGDPsnGDGSLTIQNLT 81

                          90       100
                  ....*....|....*....|....*...
gi 283436188  110 PADSGIYICDVNNPPDFVGKNQGLLDVT 137
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 25-118 4.12e-11

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: 59.66  E-value: 4.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  25 VTIPDTFVNVTVGSNVTLLCLYTTTEKSLeklSIQWsfFHNKEMEEPISIYYSEGGQASAIGQFKDRIIGATNPGN-ASI 103
Cdd:cd00099    1 VTQSPRSLSVQEGESVTLSCEVSSSFSST---YIYW--YRQKPGQGPEFLIYLSSSKGKTKGGVPGRFSGSRDGTSsFSL 75

                         90
                 ....*....|....*
gi 283436188 104 TILHMQPADSGIYIC 118
Cdd:cd00099   76 TISNLQPEDSGTYYC 90
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 37-128 7.34e-11

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 59.07  E-value: 7.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  37 GSNVTLLCLYTTTEKSLEKLSIQWSFFHNKEMEEPISIYYSEGGQASAIGQFKDRIIGATNP--GNASITILHMQPADSG 114
Cdd:cd05880   14 GTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHKRPYPPPDGRFKGRVVWDGNImrRDASILIWQLQPTDNG 93

                         90
                 ....*....|....
gi 283436188 115 IYICDVNNPPDFVG 128
Cdd:cd05880   94 TYTCQVKNPPDVHG 107
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 23-124 1.01e-08

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 52.84  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  23 VQVTIPDTFVNVTVGSNVTLLCLYTTTEKSLEKLSIQWSFfHNKEMEEPISIYYSeGGQA--SAIGQFKDRIIGATN--P 98
Cdd:cd20960    1 LLITSAQTEIKKVAGENVTLPCHHQLGLEDQGTLDIEWLL-LPSDKVEKVVITYS-GDRVynHYYPALKGRVAFTSNdlS 78

                         90       100
                 ....*....|....*....|....*.
gi 283436188  99 GNASITILHMQPADSGIYICDVNNPP 124
Cdd:cd20960   79 GDASLNISNLKLSDTGTYQCKVKKAP 104
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 154-229 1.07e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 1.07e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283436188   154 EAGHPISLSClSAFGTPSPLYYWYKIEGNTIVP---VKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:smart00410   7 KEGESVTLSC-EASGSPPPEVTWYKQGGKLLAEsgrFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 144-217 5.26e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 49.87  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  144 KPFCTIQGRPEA---GHPISLSClSAFGTPSPLYYWYKiEGNTIVPV---KESFNTATGVLVIGNLTNFEQGYYQCTAIN 217
Cdd:pfam13927   1 KPVITVSPSSVTvreGETVTLTC-EATGSPPPTITWYK-NGEPISSGstrSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 32-138 3.04e-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: 45.19  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188    32 VNVTVGSNVTLLCLYTTTEKSleklSIQWSFFHNKEMeepisiyyseggqasaigQFKDRIIGATNPGNASITILHMQPA 111
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPPP----EVTWYKQGGKLL------------------AESGRFSVSRSGSTSTLTISNVTPE 61

                           90       100
                   ....*....|....*....|....*..
gi 283436188   112 DSGIYICDVNNPpdfVGKNQGLLDVTV 138
Cdd:smart00410  62 DSGTYTCAATNS---SGSASSGTTLTV 85
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 156-229 3.35e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 44.71  E-value: 3.35e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 283436188 156 GHPISLSCLsAFGTPSPLYYWYKIEGNTI--VPVKESFNTAtgvLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:cd05731   10 GGVLLLECI-AEGLPTPDIRWIKLGGELPkgRTKFENFNKT---LKIENVSEADSGEYQCTASNTMGSARHTISVT 81
IgI_2_Dscam cd20953
Second immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 154-229 1.72e-05

Second 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 second immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. 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: 409545  Cd Length: 95  Bit Score: 43.30  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188 154 EAGHPISLSCLsAFGTPSPLYYWYK-IEGNT---IVPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:cd20953   16 SSASSIALLCP-AQGYPAPSFRWYKfIEGTTrkqAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLT 94
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 314-359 2.22e-05

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 44.01  E-value: 2.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 283436188  314 EPTTTAVLEPEYEPNPPLETTTQPDPEPEgsvPVLAPEAEIQPHPE 359
Cdd:pfam05887  68 EPEPEPEPEPEPEPEPEPEPEPEPEPEPE---PEPEPEPEPEPEPE 110
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 159-220 2.36e-05

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.93  E-value: 2.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436188 159 ISLSClSAFGTPSPLYYWYK--IEGNTIVPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLG 220
Cdd:cd00096    1 VTLTC-SASGNPPPTITWYKngKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
 145-220 5.66e-05

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 second Ig-like domain of JAM1 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, the A strand of the I-set is discontinuous but lacks 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: 409542  Cd Length: 97  Bit Score: 41.92  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188 145 PFCTIQGRPEAGHPISLSCLSAFGTPSPLYYWYKieGNTIVPVKE-----------SFNTATGVLVIGNLTNFEQGYYQC 213
Cdd:cd20950    1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFK--DGVVMPTNPkstrafsnssySLDPTTGELVFDPLSASDTGEYSC 78


                 ....*..
gi 283436188 214 TAINSLG 220
Cdd:cd20950   79 EARNGYG 85
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 322-359 1.58e-04

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 41.32  E-value: 1.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 283436188  322 EPEYEPNPPLETTTQPDPEPEgsvPVLAPEAEIQPHPE 359
Cdd:pfam05887  62 EPEPEPEPEPEPEPEPEPEPE---PEPEPEPEPEPEPE 96
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 34-125 1.71e-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: 40.26  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188   34 VTVGSNVTLLCLYTTTEKSLEklsIQWsFFHNKEMEEPISIYYSEGGQasaigqfkdriigatnpGNASITILHMQPADS 113
Cdd:pfam00047   8 VLEGDSATLTCSASTGSPGPD---VTW-SKEGGTLIESLKVKHDNGRT-----------------TQSSLLISNVTKEDA 66

                          90
                  ....*....|..
gi 283436188  114 GIYICDVNNPPD 125
Cdd:pfam00047  67 GTYTCVVNNPGG 78
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 156-220 2.58e-04

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 39.45  E-value: 2.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436188 156 GHPISLSCLsAFGTPSPLYYWYKIEGNtiVPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLG 220
Cdd:cd04968   16 GQTVTLECF-ALGNPVPQIKWRKVDGS--PSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSRG 77
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
 27-121 3.30e-04

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 39.89  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  27 IPDTFVNVTVGSNVTLLCLYTTTEK-SLEKLSIQWSFFHNKEMEEpiSIYYSEGGQASAIGQFKDRII---GATNPGNAS 102
Cdd:cd20934    2 VPEDPVVALVGTDATLRCSFSPEPGfSLAQLSVFWQLTDTKQLVH--SFTESQDQGRDQGSAYANRTAlfpDLLAQGNAS 79

                         90
                 ....*....|....*....
gi 283436188 103 ITILHMQPADSGIYICDVN 121
Cdd:cd20934   80 LRLQRVRVADEGSYTCFVS 98
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 32-140 5.94e-04

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 39.50  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  32 VNVTVGSNVTLLCLYTTTEK----SLEKLSIQWSFFH-NKEMEEPISIYYSEGGQASAIGQFKDRIIGATNP---GNASI 103
Cdd:cd05714    7 VFSHLGGNVTLPCKFYRDPTafgsGIHKIRIKWTKLTsDSGYLKEVDVLVAMGNVVYHKKTYGGRVSVPLKPgsdSDASL 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 283436188 104 TILHMQPADSGIYICDVnnppdfvgkNQGLLDVTVLV 140
Cdd:cd05714   87 VITDLTASDYGLYRCEV---------IEGIEDDQDVV 114
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 156-220 6.49e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 38.46  E-value: 6.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436188 156 GHPISLSCLsAFGTPSPLYYWYKIegNTIVPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLG 220
Cdd:cd05851   16 GQNVTLECF-ALGNPVPVIRWRKI--LEPMPATAEISMSGAVLKIFNIQPEDEGTYECEAENIKG 77
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 168-228 8.98e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). 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: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 38.25  E-value: 8.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436188 168 GTPSPLYYWyKIEGNTIVPVKESF----NTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDL 228
Cdd:cd05744   26 GLPTPDLFW-QLNGKPVRPDSAHKmlvrENGRHSLIIEPVTKRDAGIYTCIARNRAGENSFNAEL 89
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 25-118 9.19e-04

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: 38.41  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  25 VTIPDTFVNVTVGSNVTLLCLYTTTEKSleklSIQWsF--FHNKEMEEPISIYYSEGGQASaiGQFkdRIIGATNPGNAS 102
Cdd:cd04983    1 VTQSPQSLSVQEGENVTLNCNYSTSTFY----YLFW-YrqYPGQGPQFLIYISSDSGNKKK--GRF--SATLDKSRKSSS 71

                         90
                 ....*....|....*.
gi 283436188 103 ITILHMQPADSGIYIC 118
Cdd:cd04983   72 LHISAAQLSDSAVYFC 87
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 37-140 1.15e-03

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 38.46  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  37 GSNVTLLCLYTT--TEKSLEKLSIQWSFFHNKEMEEPIsIYYSEGGQASAIGQFKDRI-IGATNPGNASITILHMQPADS 113
Cdd:cd05877   12 GGNVTLPCRYHYepELSAPRKIRVKWTKLEVDYAKEED-VLVAIGTRHKSYGSYQGRVfLRRADDLDASLVITDLRLEDY 90

                         90       100
                 ....*....|....*....|....*..
gi 283436188 114 GIYICDVNNppdfvgknqGLLDVTVLV 140
Cdd:cd05877   91 GRYRCEVID---------GLEDESVVV 108
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 155-229 1.67e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup 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. 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. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin 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. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 37.60  E-value: 1.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 283436188 155 AGHPISLSClSAFGTPSPLYYWYKIEGNTIVPVKE---SFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:cd05763   13 AGSTARLEC-AATGHPTPQIAWQKDGGTDFPAARErrmHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATLT 89
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 34-138 1.71e-03

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 37.71  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  34 VTVGSNVTLLCLYTTTEkslEKLSIQWsffhNKEM---EEPISIYYSEGGQaSAIGQFKDRIIGAT-NPGNASITILHMQ 109
Cdd:cd05846   10 AVLGGNATLSCNLTLPE---EVLQVTW----QKIKassPENIVTYSKKYGV-KIQPSYVRRISFTSsGLNSTSITIWNVT 81

                         90       100
                 ....*....|....*....|....*....
gi 283436188 110 PADSGIYICDVNNPPDfvGKNQGLLDVTV 138
Cdd:cd05846   82 LEDEGCYKCLFNTFPD--GIKSGTACLTV 108
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 261-359 1.71e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.52  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188 261 NKVKSKQQKNLN------SSTELEPMTKVHHPQQSEAISadgvQLEGTLPSSIHAGHNTEPTTTAVLEPEYEPNPPLETT 334
Cdd:NF033839 103 NKLQNIKNEYLNkivestSKSQLQKLMMESQSKVDEAVS----KFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPD 178

                         90       100
                 ....*....|....*....|....*
gi 283436188 335 TQPDPEPEGSVPvlaPEAEIQPHPE 359
Cdd:NF033839 179 TKPSPQPEGKKP---SVPDINQEKE 200
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 32-120 1.82e-03

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: 37.83  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  32 VNVTVGSNVTLLClyTTTEKSLEKLSIQWsfFHNKEMEEPISIYYSEGGQASAIgqfKDRIIGATNPGNASITILHMQPA 111
Cdd:cd04984    8 LSVSPGETVTITC--TGSSGNISGNYVNW--YQQKPGSAPRYLIYEDKHRPSGI---PDRFSGSKSGNTASLTISGAQTE 80


                 ....*....
gi 283436188 112 DSGIYICDV 120
Cdd:cd04984   81 DEADYYCQV 89
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 32-139 1.90e-03

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain


Pssm-ID: 409471  Cd Length: 108  Bit Score: 37.57  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  32 VNVTVGSNVTLLCLYTTtEKSLEKLSIQWSFFHNKEMEEPISIYYSEGGQaSAIGQFKDRIIGATN--PGNASITILHMQ 109
Cdd:cd05888    3 VTVVLGQDAKLPCFYRG-DSGEQVGQVAWARVDAGEGAQEIALLHSKYGL-HVFPAYEGRVEQPPPprPADGSVLLRNAV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 283436188 110 PADSGIYICDVNNPPdfVGKNQGLLDVTVL 139
Cdd:cd05888   81 QADEGEYECRVSTFP--AGNFQAELRLRVL 108
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 155-223 2.58e-03

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: 36.71  E-value: 2.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188 155 AGHPISLSClSAFGTPSPLYYWYKiEGNTIVPVKESFNT-ATGVLVIGNLTNFEQGYYQCTAINSLGNSS 223
Cdd:cd20952   13 VGGTVVLNC-QATGEPVPTISWLK-DGVPLLGKDERITTlENGSLQIKGAEKSDTGEYTCVALNLSGEAT 80
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
 32-141 2.65e-03

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 80). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as cluster of differentiation 152/CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. CD80 contains two Ig-like domains, an amino-terminal immunoglobulin variable (IgV)-like domain characteristic of adhesion molecules and a membrane proximal immunoglobulin constant (IgC)-like domain similar to the constant domains of antigen receptors. Members of the Ig family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and Major Histocompatibility Complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 319335  Cd Length: 105  Bit Score: 37.04  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  32 VNVTVGSNVTLLCLYTTTEKSLEKLSIQWsffhNKEMEEPISIYyseGGQASAIGQFKDRIIgATNPGNASITILHMQPA 111
Cdd:cd16086    4 VTKSVKEKALLSCDYNVSVDELAQVRIYW----QKDDKMVLTII---SGDVKVWPEYKNRTL-FDITNNLSIVILALRLS 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 283436188 112 DSGIYICDVNNPPDFVGKNQGLLDVTVLVK 141
Cdd:cd16086   76 DRGTYTCVVQKKERGAYKREHLASVTLSVR 105
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 159-220 2.76e-03

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 36.84  E-value: 2.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436188 159 ISLSClSAFGTPSPLYYWYKIEGNTIVPVKESFNTATGVLVIGNLTNF-EQGYYQCTAINSLG 220
Cdd:cd05848   22 VILNC-EARGNPVPTYRWLRNGTEIDTESDYRYSLIDGNLIISNPSEVkDSGRYQCLATNSIG 83
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 154-223 2.76e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 36.72  E-value: 2.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436188 154 EAGHPISLSCLSAFGTPSPLYYWYKiEGNTI-----VPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSS 223
Cdd:cd05750   12 QEGSKLVLKCEATSENPSPRYRWFK-DGKELnrkrpKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDT 85
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 27-139 2.87e-03

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 37.22  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  27 IPDTFVNVTVGSNVTLLCLYTTTEkSLEKLSiqWSFFHNKEmEEPISIYYSEGGqASAIGQFKDRIIgATNPG--NASIT 104
Cdd:cd05887    4 IVEPHVTAVWGKNVSLKCLIEVNE-TITQIS--WEKIHGKS-SQTVAVHHPQYG-ISIQGEYQGRVS-FKNYSlnDATIT 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 283436188 105 ILHMQPADSGIYICDVNNPPdfVGKNQGLLDVTVL 139
Cdd:cd05887   78 LHNVGFSDSGKYICKAVTFP--LGNAQSSTTVTVL 110
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 156-230 3.04e-03

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: 36.60  E-value: 3.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436188 156 GHPISLSClSAFGTPSPLYYWYKiEGNTIVPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLTS 230
Cdd:cd20978   16 GQDVTLPC-QVTGVPQPKITWLH-NGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLLHV 88
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 32-120 3.81e-03

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409462  Cd Length: 125  Bit Score: 37.21  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  32 VNVTVGSNVTLLCLYT------TTEKSLEKLSIQWS---FFHNKEMEEPISIyySEGGQASAIGQFKDRIIGATNP---G 99
Cdd:cd05878    7 VRVLLGTSVTLPCYFIdpphpvTPSTAPLAPRIKWSkvsVDGKKEKEVVLLV--ATEGRVRVNSAYQGRVSLPNYPaipS 84

                         90       100
                 ....*....|....*....|.
gi 283436188 100 NASITILHMQPADSGIYICDV 120
Cdd:cd05878   85 DATLEVQSLRASDSGLYRCEV 105
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 156-222 3.89e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. 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, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 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.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 36.76  E-value: 3.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 283436188 156 GHPISLSClSAFGTPSPLYYWYKiEGNTIVPVKESFNTATGVLVIGNLTNF----------EQGYYQCTAINSLGNS 222
Cdd:cd07693   15 GDPATLNC-KAEGRPTPTIQWLK-NGQPLETDKDDPRSHRIVLPSGSLFFLrvvhgrkgrsDEGVYVCVAHNSLGEA 89
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 156-228 4.59e-03

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (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: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 35.91  E-value: 4.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436188 156 GHPISLSClSAFGTPSPLYYWYKIEGNTIVPVKESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDL 228
Cdd:cd05764   15 GQRATLRC-KARGDPEPAIHWISPEGKLISNSSRTLVYDNGTLDILITTVKDTGAFTCIASNPAGEATARVEL 86
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 156-229 4.72e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. 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 telokin Ig domain 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: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 36.01  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188 156 GHPISLSCLSAfGTPSPLYYWYKiEGNtivPVKESFNTATG-------VLVIGNLTNFEQGYYQCTAINSLGNSSCEIDL 228
Cdd:cd20973   12 GSAARFDCKVE-GYPDPEVKWMK-DDN---PIVESRRFQIDqdedglcSLIISDVCGDDSGKYTCKAVNSLGEATCSAEL 86


                 .
gi 283436188 229 T 229
Cdd:cd20973   87 T 87
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 23-138 5.12e-03

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 36.66  E-value: 5.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  23 VQVTIPDTfVNVTVGSNVTLLCLYTTTEKslEKLS-IQWSFFHNKEmEEPISIYYSEGGqASAIGQFKDRIIG---ATNP 98
Cdd:cd05718    1 QRVQVPTE-VTGFLGGSVTLPCSLTSPGT--TKITqVTWMKIGAGS-SQNVAVFHPQYG-PSVPNPYAERVEFlaaRLGL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 283436188  99 GNASITILHMQPADSGIYICDVNNPPDfvGKNQGLLDVTV 138
Cdd:cd05718   76 RNATLRIRNLRVEDEGNYICEFATFPQ--GNRQGTTWLRV 113
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
 24-125 5.32e-03

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: 36.34  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  24 QVTIPDTFVNVTVGSNVTLLCLYTTTeksleklsiqWSFFH--------NKEMEepISIYYSEGGQASAIGQFKDRIIGA 95
Cdd:cd07706    1 KVTQAQPDVSVQVGEEVTLNCRYETS----------WTNYYlfwykqlpSGEMT--FLIRQDSSEQNAKSGRYSVNFQKA 68

                         90       100       110
                 ....*....|....*....|....*....|
gi 283436188  96 TNpgNASITILHMQPADSGIYICDVNNPPD 125
Cdd:cd07706   69 QK--SISLTISALQLEDSAKYFCALSLPYD 96
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 156-223 5.47e-03

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. 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 structures of the titin-A168169 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: 409563  Cd Length: 93  Bit Score: 35.91  E-value: 5.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436188 156 GHPISLSClSAFGTPSPLYYWYKIEgnTIVPVKESFNTATG------VLVIGNLTNFEQGYYQCTAINSLGNSS 223
Cdd:cd20971   16 QSNATLVC-KVTGHPKPIVKWYRQG--KEIIADGLKYRIQEfkggyhQLIIASVTDDDATVYQVRATNQGGSVS 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 24-122 5.75e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188   24 QVTIPDTFVNVTVGSNVTLLCLYTTTEKSleklSIQWsfFHNKEMEEPISIYYSEggqasaigqfkdriigaTNPGNASI 103
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPP----TITW--YKNGEPISSGSTRSRS-----------------LSGSNSTL 59

                          90
                  ....*....|....*....
gi 283436188  104 TILHMQPADSGIYICDVNN 122
Cdd:pfam13927  60 TISNVTRSDAGTYTCVASN 78
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 25-118 6.25e-03

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 36.45  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188  25 VTIPDTFVNVTVGSNVTLLCLYTTTEK-SLEKLSIQWsffhnkEMEEPISIYYSEGG-----QASAIGQ----FKDRIIg 94
Cdd:cd20947    1 VTVPKDLYVVEYGSNMTIECKFPVEKQlDLAALIVYW------EMEDKNIIQFVHGEedlkvQHSSYRQrarlLKDQLS- 73

                         90       100
                 ....*....|....*....|....
gi 283436188  95 atnPGNASITILHMQPADSGIYIC 118
Cdd:cd20947   74 ---LGNAALQITDVKLQDAGVYRC 94
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 154-220 6.38e-03

Seventh 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 seventh 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: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 35.75  E-value: 6.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 283436188 154 EAGHPISLSClSAFGTPSPLYYWYKIEGNTIVPVKESFNTAT------GVLVIGNLTNFEQGYYQCTAINSLG 220
Cdd:cd20954   14 AAGQDVMLHC-QADGFPTPTVTWKKATGSTPGEYKDLLYDPNvrilpnGTLVFGHVQKENEGHYLCEAKNGIG 85
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 156-229 6.66e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 35.30  E-value: 6.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436188 156 GHPISLSClSAFGTPSPLYYWYKieGNTIVPV-KESFNTATGVLVIGNLTNFEQGYYQCTAINSLGNSSCEIDLT 229
Cdd:cd05745    2 GQTVDFLC-EAQGYPQPVIAWTK--GGSQLSVdRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLT 73
IGv smart00406
Immunoglobulin V-Type;
39-120 8.66e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 35.05  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436188    39 NVTLLClyTTTEKSLEKLSIQWSF-FHNKEMEEPISIYYSEGGQASAigQFKDRIIGATNPGN--ASITILHMQPADSGI 115
Cdd:smart00406   1 SVTLSC--KFSGSTFSSYYVSWVRqPPGKGLEWLGYIGSNGSSYYQE--SYKGRFTISKDTSKndVSLTISNLRVEDTGT 76


                   ....*
gi 283436188   116 YICDV 120
Cdd:smart00406  77 YYCAV 81
 
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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