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Conserved domains on  [gi|116006959|ref|NP_039252|]
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pro-neuregulin-1, membrane-bound isoform isoform HRG-beta3 [Homo sapiens]

Protein Classification

Ig_Pro_neuregulin-1 and EGF domain-containing protein( domain architecture ID 10862069)

Ig_Pro_neuregulin-1 and EGF domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
37-129 6.99e-55

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


:

Pssm-ID: 409476  Cd Length: 93  Bit Score: 170.94  E-value: 6.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  37 PRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVIS 116
Cdd:cd05895    1 PKLKEMKSQEVAAGSKLVLRCETSSEYPSLRFKWFKNGKEINRKNKPENIKIQKKKKKSELRINKASLADSGEYMCKVSS 80
                         90
                 ....*....|...
gi 116006959 117 KLGNDSASANITI 129
Cdd:cd05895   81 KLGNDSASANVTI 93
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
190-220 8.51e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 33.13  E-value: 8.51e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 116006959  190 CVNGGECFMVkdlsnPSRYLCKCPNEFTGDR 220
Cdd:pfam00008   6 CSNGGTCVDT-----PGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
37-129 6.99e-55

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 170.94  E-value: 6.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  37 PRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVIS 116
Cdd:cd05895    1 PKLKEMKSQEVAAGSKLVLRCETSSEYPSLRFKWFKNGKEINRKNKPENIKIQKKKKKSELRINKASLADSGEYMCKVSS 80
                         90
                 ....*....|...
gi 116006959 117 KLGNDSASANITI 129
Cdd:cd05895   81 KLGNDSASANVTI 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
43-129 4.31e-13

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: 62.91  E-value: 4.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959    43 KSQESAAGSKLVLRCETSSeYSSLRFKWFKNGNELnrKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDS 122
Cdd:smart00410   2 PSVTVKEGESVTLSCEASG-SPPPEVTWYKQGGKL--LAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                   ....*..
gi 116006959   123 ASANITI 129
Cdd:smart00410  79 SGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
39-129 4.70e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.96  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959   39 LKEMKSQESAAGSKLVLRCETSsEYSSLRFKWFKNGNELNRKNKpqnIKIQKKPGKSELRINKASLADSGEYMCKVISKL 118
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVT-GTPDPEVSWFKDGQPLRSSDR---FKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                          90
                  ....*....|.
gi 116006959  119 GNDSASANITI 129
Cdd:pfam07679  80 GEAEASAELTV 90
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
60-128 9.80e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 39.13  E-value: 9.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116006959  60 SSEYSSLRFKWFKNGNELnrknkPQNIKIQKKPGKSELRINKASLADSGEYMCKVisKLGNDSASANIT 128
Cdd:PHA02826 158 SSTFKDYTLTWYKNGNIV-----LYTDRIQLRNNNSTLVIKSATHDDSGIYTCNL--RFNKNSNNYNIT 219
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
190-220 8.51e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 33.13  E-value: 8.51e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 116006959  190 CVNGGECFMVkdlsnPSRYLCKCPNEFTGDR 220
Cdd:pfam00008   6 CSNGGTCVDT-----PGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
37-129 6.99e-55

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 170.94  E-value: 6.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  37 PRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVIS 116
Cdd:cd05895    1 PKLKEMKSQEVAAGSKLVLRCETSSEYPSLRFKWFKNGKEINRKNKPENIKIQKKKKKSELRINKASLADSGEYMCKVSS 80
                         90
                 ....*....|...
gi 116006959 117 KLGNDSASANITI 129
Cdd:cd05895   81 KLGNDSASANVTI 93
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
37-129 1.31e-46

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: 149.97  E-value: 1.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  37 PRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKnKPQNIKIQKKPGKSELRINKASLADSGEYMCKVIS 116
Cdd:cd05750    1 PKLKEMKSQTVQEGSKLVLKCEATSENPSPRYRWFKDGKELNRK-RPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVEN 79
                         90
                 ....*....|...
gi 116006959 117 KLGNDSASANITI 129
Cdd:cd05750   80 ILGKDTVTGNVTV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
43-129 4.31e-13

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: 62.91  E-value: 4.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959    43 KSQESAAGSKLVLRCETSSeYSSLRFKWFKNGNELnrKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDS 122
Cdd:smart00410   2 PSVTVKEGESVTLSCEASG-SPPPEVTWYKQGGKL--LAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78

                   ....*..
gi 116006959   123 ASANITI 129
Cdd:smart00410  79 SGTTLTV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
36-131 4.09e-10

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. 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. 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 Ig I1 domain of the titin I-band 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, 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: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 55.12  E-value: 4.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  36 PPRLKEMKSQESAAGSKLVLRCETSSEySSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVI 115
Cdd:cd20951    1 PEFIIRLQSHTVWEKSDAKLRVEVQGK-PDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAK 79
                         90
                 ....*....|....*.
gi 116006959 116 SKLGNDSASANItIVE 131
Cdd:cd20951   80 NIHGEASSSASV-VVE 94
I-set pfam07679
Immunoglobulin I-set domain;
39-129 4.70e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.96  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959   39 LKEMKSQESAAGSKLVLRCETSsEYSSLRFKWFKNGNELNRKNKpqnIKIQKKPGKSELRINKASLADSGEYMCKVISKL 118
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVT-GTPDPEVSWFKDGQPLRSSDR---FKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79
                          90
                  ....*....|.
gi 116006959  119 GNDSASANITI 129
Cdd:pfam07679  80 GEAEASAELTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
43-127 1.54e-08

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: 50.66  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959   43 KSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQniKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDS 122
Cdd:pfam00047   4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVK--HDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSAT 81

                  ....*
gi 116006959  123 ASANI 127
Cdd:pfam00047  82 LSTSL 86
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
36-129 2.09e-08

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. 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 structure of the titin Z1z2 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: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 50.27  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  36 PPR-LKEMKSQESAAGSKLVLRCETSSEySSLRFKWFKNGNELnrKNKPqNIKIQKKPGKSELRINKASLADSGEYMCKV 114
Cdd:cd20972    1 PPQfIQKLRSQEVAEGSKVRLECRVTGN-PTPVVRWFCEGKEL--QNSP-DIQIHQEGDLHSLIIAEAFEEDTGRYSCLA 76
                         90
                 ....*....|....*
gi 116006959 115 ISKLGNDSASANITI 129
Cdd:cd20972   77 TNSVGSDTTSAEIFV 91
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
53-125 2.19e-07

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: 46.94  E-value: 2.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116006959  53 LVLRCETSSeYSSLRFKWFKNGNELNRKNKPqniKIQKKPGKSELRINKASLADSGEYMCKVISKL-GNDSASA 125
Cdd:cd00096    1 VTLTCSASG-NPPPTITWYKNGKPLPPSSRD---SRRSELGNGTLTISNVTLEDSGTYTCVASNSAgGSASASV 70
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
46-114 5.29e-07

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. 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 Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. 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: 409559  Cd Length: 82  Bit Score: 46.08  E-value: 5.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116006959  46 ESAAGSKLVLRCETSSEYSSLRfkWFKNGNELNRKNKpqnIKIQKKPGKSELRINKASLADSGEYMCKV 114
Cdd:cd20967    8 QVSKGHKIRLTVELADPDAEVK--WYKDGQELQSSSK---VIFESIGAKRTLTVQQASLADAGEYQCVA 71
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
39-129 6.44e-07

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 46.05  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  39 LKEMKSQESAAGSKLVLRCETSSEySSLRFKWFKNGNELNRKNKpqnikIQKKPGKseLRINKASLADSGEYMCKVISKL 118
Cdd:cd05728    3 LKVISDTEADIGSSLRWECKASGN-PRPAYRWLKNGQPLASENR-----IEVEAGD--LRITKLSLSDSGMYQCVAENKH 74
                         90
                 ....*....|.
gi 116006959 119 GNDSASANITI 129
Cdd:cd05728   75 GTIYASAELAV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
36-114 1.74e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 44.86  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959   36 PPRLK-EMKSQESAAGSKLVLRCETSSeYSSLRFKWFKNGNELNrknKPQNIKIQKKPGKSELRINKASLADSGEYMCKV 114
Cdd:pfam13927   1 KPVITvSPSSVTVREGETVTLTCEATG-SPPPTITWYKNGEPIS---SGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
48-129 5.35e-06

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: 43.64  E-value: 5.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  48 AAGSKLVLRCETSSEYSSLrFKWFKNGNELNRKNkpQNIKIQKKpgkSELRINKASLADSGEYMCKVISKLGNDSASANI 127
Cdd:cd20952   12 AVGGTVVLNCQATGEPVPT-ISWLKDGVPLLGKD--ERITTLEN---GSLQIKGAEKSDTGEYTCVALNLSGEATWSAVL 85

                 ..
gi 116006959 128 TI 129
Cdd:cd20952   86 DV 87
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
50-129 7.60e-06

Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth 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.


Pssm-ID: 409359  Cd Length: 102  Bit Score: 43.69  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  50 GSKLVLRCETS-SEYSSLRFKWFKNGNELNRkNKPqNIKIQKKPGK---SELRINKASLADSGEYMCKVISKLGNDSASA 125
Cdd:cd04970   17 GENATLQCHAShDPTLDLTFTWSFNGVPIDL-EKI-EGHYRRRYGKdsnGDLEIVNAQLKHAGRYTCTAQTVVDSDSASA 94

                 ....
gi 116006959 126 NITI 129
Cdd:cd04970   95 TLVV 98
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
50-113 5.98e-05

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


Pssm-ID: 409410 [Multi-domain]  Cd Length: 79  Bit Score: 40.42  E-value: 5.98e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116006959  50 GSKLVLRCETSSEYSSLRFKWFKNGNELNRKNkpqnikiqkkpgkSELRINKASLADSGEYMCK 113
Cdd:cd05752   15 GEKVTLTCQGFYSPEQNSTQWYHNGTLISSTS-------------SSYRIVAATVNDSGEYRCQ 65
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
37-124 7.75e-05

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 40.59  E-value: 7.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  37 PRLKEMKSQESAAGSKLVLRCETSSE-YSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVI 115
Cdd:cd05732    3 PKITYLENQTAVELEQITLTCEAEGDpIPEITWRRATRGISFEEGDLDGRIVVRGHARVSSLTLKDVQLTDAGRYDCEAS 82

                 ....*....
gi 116006959 116 SKLGNDSAS 124
Cdd:cd05732   83 NRIGGDQQS 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
69-129 1.30e-04

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: 39.87  E-value: 1.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116006959  69 KWFKNGNELNRKNKPQNIkiQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITI 129
Cdd:cd20973   30 KWMKDDNPIVESRRFQID--QDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCSAELTV 88
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
37-129 1.89e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143278 [Multi-domain]  Cd Length: 98  Bit Score: 39.57  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  37 PRLKEMKSQESAAGSKLVLRCETSSE-YSSLRFKWFKNGNELNRKNKPQN--IKIQKKPGKSELRINKASLADSGEYMCK 113
Cdd:cd05870    3 PHIIQLKNETTVENGAATLSCKAEGEpIPEITWKRASDGHTFSEGDKSPDgrIEVKGQHGESSLHIKDVKLSDSGRYDCE 82
                         90
                 ....*....|....*.
gi 116006959 114 VISKLGNDSASANITI 129
Cdd:cd05870   83 AASRIGGHQKSMYLDI 98
IgI_VEGFR cd05862
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); ...
43-131 1.93e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R); member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor(R). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (also known as Flt-1), VEGFR-2 (also known as KDR or Flk-1) and VEGFR-3 (also known as Flt-4). VEGF_A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF, VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth.


Pssm-ID: 409448  Cd Length: 102  Bit Score: 39.73  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  43 KSQESAAGSKLVLRCETSSEYSS-LRFKW-FKNGNELNRKNKPQNIKIQKKPGK---SELRINKASLADSGEYMCKVISK 117
Cdd:cd05862    9 KPVELLVGEKLVLNCTARTELNVgVDFQWdYPGKKEQRRASVRRRRKQQSSEATefsSTLTIDNVTLSDKGLYTCAASSG 88
                         90
                 ....*....|....
gi 116006959 118 LGNDSASANITIVE 131
Cdd:cd05862   89 PMFKKNSTSVIVHE 102
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
43-132 2.93e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 38.78  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  43 KSQESAAGSKLVLRCETSSEySSLRFKWFKNGNELNRKnkpQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDS 122
Cdd:cd05736    8 EFQAKEPGVEASLRCHAEGI-PLPRVQWLKNGMDINPK---LSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEGGVDE 83
                         90
                 ....*....|
gi 116006959 123 ASANITIVES 132
Cdd:cd05736   84 DISSLFVEDS 93
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
34-129 3.55e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 38.39  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  34 ALPPRLkemksqESAAGSKLVLRCeTSSEYSSLRFKWFKNGNELNRKNKpqniKIQKKPGKSELRINKASLADSGEYMCK 113
Cdd:cd20976    6 SVPKDL------EAVEGQDFVAQC-SARGKPVPRITWIRNAQPLQYAAD----RSTCEAGVGELHIQDVLPEDHGTYTCL 74
                         90
                 ....*....|....*.
gi 116006959 114 VISKLGNDSASANITI 129
Cdd:cd20976   75 AKNAAGQVSCSAWVTV 90
IgI_1_FGFR cd04973
First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
33-122 3.83e-04

First immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for all FGFs.


Pssm-ID: 409362  Cd Length: 94  Bit Score: 38.72  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  33 PALPPR------LKEMKSQESAAGSKLVLRCETSSEYSSLrfKWFKNGNELNRKNKPQNIKiqkkpgkSELRINKASLAD 106
Cdd:cd04973    1 PTLPPEapptyqISEVESYSAHPGDLLQLRCRLRDDVQSI--NWTKDGVQLGENNRTRITG-------EEVQIKDAVPRD 71
                         90
                 ....*....|....*.
gi 116006959 107 SGEYMCKVISKLGNDS 122
Cdd:cd04973   72 SGLYACVTSSPSGSDT 87
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
35-130 7.11e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF; VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity.


Pssm-ID: 409404  Cd Length: 102  Bit Score: 37.90  E-value: 7.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  35 LPPRLKEMKSQesaaGSKLVLRCETSSEYSS-LRFKWFKNGNELNRKNKPQ-NIKIQKKPGK---SELRINKASLADSGE 109
Cdd:cd05742    6 SPNAEPTVLPQ----GETLVLNCTANVNLNEvVDFQWTYPSEKEGKLALLKpDIKVDWSEPGefvSTLTIPEATLKDSGT 81
                         90       100
                 ....*....|....*....|.
gi 116006959 110 YMCKVISKLGNDSASANITIV 130
Cdd:cd05742   82 YTCAARSGVMKKEKQTSVSVH 102
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
60-128 9.80e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 39.13  E-value: 9.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116006959  60 SSEYSSLRFKWFKNGNELnrknkPQNIKIQKKPGKSELRINKASLADSGEYMCKVisKLGNDSASANIT 128
Cdd:PHA02826 158 SSTFKDYTLTWYKNGNIV-----LYTDRIQLRNNNSTLVIKSATHDDSGIYTCNL--RFNKNSNNYNIT 219
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
50-119 1.18e-03

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: 37.30  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116006959  50 GSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKP----QNIKIQKKPGKSELRINKASLADSGEYMCKVISKLG 119
Cdd:cd20950   12 GNRAVLTCSEPDGSPPSEYTWFKDGVVMPTNPKStrafSNSSYSLDPTTGELVFDPLSASDTGEYSCEARNGYG 85
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
43-121 1.52e-03

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: 37.31  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  43 KSQESAAGSKLVLRCETSSEYSSLRFKWF--------------KNGNELNRKNKPQNIKIQKKPGKS-ELRINKASLADS 107
Cdd:cd00099    6 RSLSVQEGESVTLSCEVSSSFSSTYIYWYrqkpgqgpefliylSSSKGKTKGGVPGRFSGSRDGTSSfSLTISNLQPEDS 85
                         90
                 ....*....|....
gi 116006959 108 GEYMCKVISKLGND 121
Cdd:cd00099   86 GTYYCAVSESGGTD 99
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
43-117 1.64e-03

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 37.05  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959   43 KSQESAAGSKLVLRCETSSEYS--SLRFKW---------------FKNGNELNRKnkPQNIKIQKKPGKS--ELRINKAS 103
Cdd:pfam07686   4 REVTVALGGSVTLPCTYSSSMSeaSTSVYWyrqppgkgptfliayYSNGSEEGVK--KGRFSGRGDPSNGdgSLTIQNLT 81
                          90
                  ....*....|....
gi 116006959  104 LADSGEYMCKVISK 117
Cdd:pfam07686  82 LSDSGTYTCAVIPS 95
Ig6_Contactin-4 cd05853
Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth ...
44-129 4.02e-03

Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-4. 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 different contactins show different expression patterns in the central nervous system. Highest expression of contactin-4 is in testes, thyroid, small intestine, uterus, and brain. Contactin-4 plays a role in the response of neuroblastoma cells to differentiating agents, such as retinoids. The contactin 4 gene is associated with cerebellar degeneration in spinocerebellar ataxia type 16.


Pssm-ID: 409439  Cd Length: 102  Bit Score: 35.76  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  44 SQESAAGSKLVLRCETSSEYS-SLRFKWFKNGNELN-RKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGND 121
Cdd:cd05853   11 SMDVTVGESIVLPCQVSHDHSlDIVFTWSFNGHLIDfQKDGDHFERVGGQDSAGDLMIRSIQLKHAGKYVCMVQTSVDKL 90

                 ....*...
gi 116006959 122 SASANITI 129
Cdd:cd05853   91 SAAADLIV 98
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
50-129 4.37e-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: 34.91  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  50 GSKLVLRCETSSeYSSLRFKWFKNGNELNRKNKPQNIKiqkkpgKSELRINKASLADSGEYMCKVISKLGNDSASANITI 129
Cdd:cd05745    2 GQTVDFLCEAQG-YPQPVIAWTKGGSQLSVDRRHLVLS------SGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
44-129 5.67e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 34.68  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959   44 SQESAAGSKLVLRCETSSEYSSLrFKWFKNGNELNrknkpqnikiqkkpGKSELRINKASLADSGEYMCKV-ISKLGNDS 122
Cdd:pfam13895   8 PTVVTEGEPVTLTCSAPGNPPPS-YTWYKDGSAIS--------------SSPNFFTLSVSAEDSGTYTCVArNGRGGKVS 72

                  ....*..
gi 116006959  123 ASANITI 129
Cdd:pfam13895  73 NPVELTV 79
IgI_1_hemolin-like cd20979
First immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
37-125 6.65e-03

First 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 first 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 first 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 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, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM).


Pssm-ID: 409571  Cd Length: 91  Bit Score: 34.85  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  37 PRLKEMKSQ----ESAAGsklVLRCETSSEYSSLRFKWFKNGNELNRKNkpQNIKIQKKPGKSELRINKASlaDSGEYMC 112
Cdd:cd20979    1 PVLKEQPAEvlfrEGQPT---VLECVTEGGDQGVKYSWLKDGKSFNWQE--HNVAQRKDEGSLVFLKPQAS--DEGQYQC 73
                         90
                 ....*....|...
gi 116006959 113 KVISKLGNDSASA 125
Cdd:cd20979   74 FAETPAGVASSRV 86
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
190-220 8.51e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 33.13  E-value: 8.51e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 116006959  190 CVNGGECFMVkdlsnPSRYLCKCPNEFTGDR 220
Cdd:pfam00008   6 CSNGGTCVDT-----PGGYTCICPEGYTGKR 31
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
49-129 8.60e-03

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 34.89  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116006959  49 AGSKLVLRCETSSEySSLRFKWFKNGNELNRKNKPQNIKIQKKpgKSELRINKASLADSGEYMCKVISKLGNDSASANIT 128
Cdd:cd05729   18 AANKVRLECGAGGN-PMPNITWLKDGKEFKKEHRIGGTKVEEK--GWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVD 94

                 .
gi 116006959 129 I 129
Cdd:cd05729   95 V 95
IgI_VEGFR-3 cd05863
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); ...
46-111 9.74e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 3 (VEGFR-3). The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-3 (Flt-4) binds two members of the VEGF family (VEGF-C and VEGF-D) and is involved in tumor angiogenesis and growth. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409449  Cd Length: 88  Bit Score: 34.53  E-value: 9.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116006959  46 ESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPqnikiqkkpgkSELRINKASLADSGEYM 111
Cdd:cd05863   14 EATAGDELVKLPVKVAAYPPPEFQWYKDGKLISGKHSP-----------HSLQIKDVTEASAGTYT 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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