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Conserved domains on  [gi|1351476841|ref|XP_023933411|]
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basement membrane-specific heparan sulfate proteoglycan core protein-like [Lingula anatina]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_B pfam00052
Laminin B (Domain IV);
1091-1234 3.22e-46

Laminin B (Domain IV);


:

Pssm-ID: 459652  Cd Length: 136  Bit Score: 162.82  E-value: 3.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841 1091 YFDMPRQFLGNRITSYGGNLQYTVQYQTPTGTQSRLATADVIMKGNGITLYHRR--QTQPRPGLTESISVPLVESAWTTS 1168
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSpdQPPPDPGQEQTYSVRLHEENWRDS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841 1169 EtprrgdqtvPSPASRADIMTVLQNLEYIMIRGSYDTFQTEVRLGNVFLDTAVTTDTGRgRAFLVE 1234
Cdd:pfam00052   81 D---------GAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
Laminin_B pfam00052
Laminin B (Domain IV);
1495-1604 1.21e-42

Laminin B (Domain IV);


:

Pssm-ID: 459652  Cd Length: 136  Bit Score: 152.42  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841 1495 YWSLPQKFLGDRVTAYGGNLRFTISFSDL--GDAPTTEPDVIIVGNDITLTYRHSDVMLS--GTKQSFQVPFYEQFWQRP 1570
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLpgGGSLNSEPDVILEGNGLRLSYSSPDQPPPdpGQEQTYSVRLHEENWRDS 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1351476841 1571 DGSPASREFIMMALSDLSAILIKASYTGRTQETR 1604
Cdd:pfam00052   81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVS 114
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 922-999 8.47e-36

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 cd05743:

Pssm-ID: 472250  Cd Length: 78  Bit Score: 130.69  E-value: 8.47e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSIFAQPDAIVVV 999
Cdd:cd05743      1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILTV 78
I-set pfam07679
Immunoglobulin I-set domain;
689-772 4.44e-19

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.46  E-value: 4.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAG-----SQALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGT 763
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGqplrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81


                   ....*....
gi 1351476841  764 FQATARLIV 772
Cdd:pfam07679   82 AEASAELTV 90
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 826-860 1.85e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 62.99  E-value: 1.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  826 CEPNERQCRNGKCILKIWICDGDNDCGDGSDEQNC 860
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 613-647 3.78e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 59.14  E-value: 3.78e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  613 CGANQFTCTSGQCIRSSQRCDRRRDCQDGSDEVNC 647
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 496-530 1.35e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 57.60  E-value: 1.35e-10
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  496 CSAGEFRCTDGTCIDSRRRCDNFPDCRDRSDEENC 530
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 650-684 3.90e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 56.06  E-value: 3.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  650 CLPGEYRCRNGQCVPRNSRCDRRYDCSDRSDELNC 684
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1270-1312 4.52e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.59  E-value: 4.52e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1351476841 1270 CNCNGH---SNQCDSDRGVCInCQHNTEGNNCERCKPGFYGDARRG 1312
Cdd:cd00055      2 CDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 535-569 2.36e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.13  E-value: 2.36e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  535 CRRDQFRCSNGACIDENKRCDRKLDCQDGTDELGC 569
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 407-442 2.73e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.75  E-value: 2.73e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  407 CHSTEFRCRNnGACITLGQRCDGHRDCADNSDEENC 442
Cdd:cd00112      1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 574-608 3.26e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.75  E-value: 3.26e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  574 CRSGEWRCENGNCIPEAKRCDRTQDCPDNTDELDC 608
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 869-904 3.74e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.36  E-value: 3.74e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  869 CRADEYRCVDGnQCIPQSYQCDGEFDCQDSSDEIGC 904
Cdd:cd00112      1 CPPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 449-491 5.86e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 52.98  E-value: 5.86e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1351476841  449 CYSNEFQCRNGgtanapsgSCISITQVCDGHRDCADNTDEENC 491
Cdd:cd00112      1 CPPNEFRCANG--------RCIPSSWVCDGEDDCGDGSDEENC 35
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1378-1423 2.24e-07

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.89  E-value: 2.24e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1351476841 1378 CNAAGSRLPQPDGR-GQCLCKENTEGPYCDRCKANTFFLSENNPYGC 1423
Cdd:pfam00053    3 CNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 109-174 1.87e-06

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


:

Pssm-ID: 460188  Cd Length: 100  Bit Score: 48.00  E-value: 1.87e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  109 EYFRVTINITSMDYHPALSDRYSPEFQELSTQLAAALTRLFADID-GTQQIN--ILQFRR--GSLMVTFDL 174
Cdd:pfam01390    1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSlRKQYIKshVLRLRPdgGSVVVDVVL 71
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 791-821 6.84e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.12  E-value: 6.84e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1351476841  791 FQCLDReKCLPNDYKCDGDYDCTDRSDELNC 821
Cdd:cd00112      6 FRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Laminin_B pfam00052
Laminin B (Domain IV);
1091-1234 3.22e-46

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 162.82  E-value: 3.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841 1091 YFDMPRQFLGNRITSYGGNLQYTVQYQTPTGTQSRLATADVIMKGNGITLYHRR--QTQPRPGLTESISVPLVESAWTTS 1168
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSpdQPPPDPGQEQTYSVRLHEENWRDS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841 1169 EtprrgdqtvPSPASRADIMTVLQNLEYIMIRGSYDTFQTEVRLGNVFLDTAVTTDTGRgRAFLVE 1234
Cdd:pfam00052   81 D---------GAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
Laminin_B pfam00052
Laminin B (Domain IV);
1495-1604 1.21e-42

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 152.42  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841 1495 YWSLPQKFLGDRVTAYGGNLRFTISFSDL--GDAPTTEPDVIIVGNDITLTYRHSDVMLS--GTKQSFQVPFYEQFWQRP 1570
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLpgGGSLNSEPDVILEGNGLRLSYSSPDQPPPdpGQEQTYSVRLHEENWRDS 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1351476841 1571 DGSPASREFIMMALSDLSAILIKASYTGRTQETR 1604
Cdd:pfam00052   81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVS 114
LamB smart00281
Laminin B domain;
1492-1604 1.25e-39

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 143.56  E-value: 1.25e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  1492 DTYYWSLPQKFLGDRVTAYGGNLRFTISFSDL-GDAPTTEPDVIIVGNDITLTYRHSDVMLSGTKQSFQVPFYEQFWQRP 1570
Cdd:smart00281    3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRrGGTHVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQYY 82

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1351476841  1571 DGSPASREFIMMALSDLSAILIKASYTGRTQETR 1604
Cdd:smart00281   83 GGRPVTREDLMMVLANLTAILIRATYSQQMAGSR 116
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 922-999 8.47e-36

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 130.69  E-value: 8.47e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSIFAQPDAIVVV 999
Cdd:cd05743      1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILTV 78
LamB smart00281
Laminin B domain;
1090-1221 4.01e-33

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 124.68  E-value: 4.01e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  1090 YYFDMPRQFLGNRITSYGGNLQYTVQYQTPTGTqSRLATADVIMKGNGITLYHRRQTQPRPGLTESISVPLVESAWTTSE 1169
Cdd:smart00281    5 VYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG-THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQYYG 83

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1351476841  1170 TprrgdqtvpSPASRADIMTVLQNLEYIMIRGSYDTFQTEVRLGNVFLDTAV 1221
Cdd:smart00281   84 G---------RPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
I-set pfam07679
Immunoglobulin I-set domain;
689-772 4.44e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.46  E-value: 4.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAG-----SQALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGT 763
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGqplrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81


                   ....*....
gi 1351476841  764 FQATARLIV 772
Cdd:pfam07679   82 AEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 907-984 2.04e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 75.29  E-value: 2.04e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  907 PTVTIPPRPMImVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALN 984
Cdd:pfam13927    2 PVITVSPSSVT-VREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 694-772 4.15e-16

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: 74.85  E-value: 4.15e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841   694 PRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKA------SDNRGRLTIQGARVEDSGVYECQALGTGGTFQAT 767
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1351476841   768 ARLIV 772
Cdd:smart00410   81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 917-991 2.44e-14

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: 69.84  E-value: 2.44e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841   917 IMVNIGETITITCTAIGVPVPLITWRLNWG-HVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSIFA 991
Cdd:smart00410    4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 692-773 1.36e-13

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) 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, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-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, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-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 the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 68.06  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  692 VSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKAS----------DNRGRLTIQGARVEDSGVYECQALGTG 761
Cdd:cd05726      4 VKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLLFPYQppqpssrfsvSPTGDLTITNVQRSDVGYYICQALNVA 83

                           90
                   ....*....|..
gi 1351476841  762 GTFQATARLIVS 773
Cdd:cd05726     84 GSILAKAQLEVT 95
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 826-860 1.85e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 62.99  E-value: 1.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  826 CEPNERQCRNGKCILKIWICDGDNDCGDGSDEQNC 860
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 613-647 3.78e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 59.14  E-value: 3.78e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  613 CGANQFTCTSGQCIRSSQRCDRRRDCQDGSDEVNC 647
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
825-860 4.37e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 58.80  E-value: 4.37e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  825 PCEPNERQCRNGKCILKIWICDGDNDCGDGSDEQNC 860
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 826-857 1.20e-10

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 57.64  E-value: 1.20e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   826 CEPNERQCRNGKCILKIWICDGDNDCGDGSDE 857
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 496-530 1.35e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 57.60  E-value: 1.35e-10
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  496 CSAGEFRCTDGTCIDSRRRCDNFPDCRDRSDEENC 530
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 650-684 3.90e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 56.06  E-value: 3.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  650 CLPGEYRCRNGQCVPRNSRCDRRYDCSDRSDELNC 684
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1270-1312 4.52e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.59  E-value: 4.52e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1351476841 1270 CNCNGH---SNQCDSDRGVCInCQHNTEGNNCERCKPGFYGDARRG 1312
Cdd:cd00055      2 CDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1270-1317 6.53e-10

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.82  E-value: 6.53e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1351476841 1270 CNCNGH---SNQCDSDRGVCInCQHNTEGNNCERCKPGFYGDaRRGTPGDC 1317
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGL-PSDPPQGC 49
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 535-569 2.36e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.13  E-value: 2.36e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  535 CRRDQFRCSNGACIDENKRCDRKLDCQDGTDELGC 569
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 407-442 2.73e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.75  E-value: 2.73e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  407 CHSTEFRCRNnGACITLGQRCDGHRDCADNSDEENC 442
Cdd:cd00112      1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
611-647 2.96e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.79  E-value: 2.96e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  611 RPCGANQFTCTSGQCIRSSQRCDRRRDCQDGSDEVNC 647
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 574-608 3.26e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.75  E-value: 3.26e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  574 CRSGEWRCENGNCIPEAKRCDRTQDCPDNTDELDC 608
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 869-904 3.74e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.36  E-value: 3.74e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  869 CRADEYRCVDGnQCIPQSYQCDGEFDCQDSSDEIGC 904
Cdd:cd00112      1 CPPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
496-530 3.81e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.41  E-value: 3.81e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  496 CSAGEFRCTDGTCIDSRRRCDNFPDCRDRSDEENC 530
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 613-644 5.59e-09

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 53.02  E-value: 5.59e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   613 CGANQFTCTSGQCIRSSQRCDRRRDCQDGSDE 644
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 449-491 5.86e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 52.98  E-value: 5.86e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1351476841  449 CYSNEFQCRNGgtanapsgSCISITQVCDGHRDCADNTDEENC 491
Cdd:cd00112      1 CPPNEFRCANG--------RCIPSSWVCDGEDDCGDGSDEENC 35
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1270-1312 1.32e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.32e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1351476841  1270 CNCNG---HSNQCDSDRGVCInCQHNTEGNNCERCKPGFYGDARRG 1312
Cdd:smart00180    1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 496-527 2.02e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 51.48  E-value: 2.02e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   496 CSAGEFRCTDGTCIDSRRRCDNFPDCRDRSDE 527
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 406-439 5.36e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.94  E-value: 5.36e-08
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1351476841   406 TCHSTEFRCRNnGACITLGQRCDGHRDCADNSDE 439
Cdd:smart00192    1 TCPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 650-681 6.40e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.94  E-value: 6.40e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   650 CLPGEYRCRNGQCVPRNSRCDRRYDCSDRSDE 681
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 574-605 7.34e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 7.34e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   574 CRSGEWRCENGNCIPEAKRCDRTQDCPDNTDE 605
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 534-566 1.40e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 48.78  E-value: 1.40e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1351476841   534 QCRRDQFRCSNGACIDENKRCDRKLDCQDGTDE 566
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
868-904 2.05e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 2.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  868 PCRADEYRCVDGnQCIPQSYQCDGEFDCQDSSDEIGC 904
Cdd:pfam00057    2 TCSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEENC 37
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1378-1423 2.24e-07

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.89  E-value: 2.24e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1351476841 1378 CNAAGSRLPQPDGR-GQCLCKENTEGPYCDRCKANTFFLSENNPYGC 1423
Cdd:pfam00053    3 CNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
533-569 2.33e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 2.33e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  533 RQCRRDQFRCSNGACIDENKRCDRKLDCQDGTDELGC 569
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 869-901 2.59e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 48.01  E-value: 2.59e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1351476841   869 CRADEYRCVDGnQCIPQSYQCDGEFDCQDSSDE 901
Cdd:smart00192    2 CPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
650-684 4.19e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.63  E-value: 4.19e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  650 CLPGEYRCRNGQCVPRNSRCDRRYDCSDRSDELNC 684
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 448-488 1.59e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.09  E-value: 1.59e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1351476841   448 RCYSNEFQCRNGgtanapsgSCISITQVCDGHRDCADNTDE 488
Cdd:smart00192    1 TCPPGEFQCDNG--------RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
573-608 1.64e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.09  E-value: 1.64e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  573 PCRSGEWRCENGNCIPEAKRCDRTQDCPDNTDELDC 608
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 109-174 1.87e-06

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 48.00  E-value: 1.87e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  109 EYFRVTINITSMDYHPALSDRYSPEFQELSTQLAAALTRLFADID-GTQQIN--ILQFRR--GSLMVTFDL 174
Cdd:pfam01390    1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSlRKQYIKshVLRLRPdgGSVVVDVVL 71
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
406-442 1.99e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 45.70  E-value: 1.99e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  406 TCHSTEFRCrNNGACITLGQRCDGHRDCADNSDEENC 442
Cdd:pfam00057    2 TCSPNEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1378-1423 3.61e-06

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 45.42  E-value: 3.61e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1351476841 1378 CNAAGSRLPQPD-GRGQCLCKENTEGPYCDRCKANTFFLSEnNPYGC 1423
Cdd:cd00055      4 CNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
448-491 5.11e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.55  E-value: 5.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1351476841  448 RCYSNEFQCRnggtanapSGSCISITQVCDGHRDCADNTDEENC 491
Cdd:pfam00057    2 TCSPNEFQCG--------SGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 791-821 6.84e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.12  E-value: 6.84e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1351476841  791 FQCLDReKCLPNDYKCDGDYDCTDRSDELNC 821
Cdd:cd00112      6 FRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1378-1423 1.53e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 43.45  E-value: 1.53e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1351476841  1378 CNAAGSRLPQPDGR-GQCLCKENTEGPYCDRCKANTFFlseNNPYGC 1423
Cdd:smart00180    3 CDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
791-821 2.10e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.01  E-value: 2.10e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1351476841  791 FQCLDREkCLPNDYKCDGDYDCTDRSDELNC 821
Cdd:pfam00057    8 FQCGSGE-CIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 791-818 5.35e-04

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.77  E-value: 5.35e-04
                            10        20
                    ....*....|....*....|....*...
gi 1351476841   791 FQCLDReKCLPNDYKCDGDYDCTDRSDE 818
Cdd:smart00192    7 FQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
 
Name Accession Description Interval E-value
Laminin_B pfam00052
Laminin B (Domain IV);
1091-1234 3.22e-46

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 162.82  E-value: 3.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841 1091 YFDMPRQFLGNRITSYGGNLQYTVQYQTPTGTQSRLATADVIMKGNGITLYHRR--QTQPRPGLTESISVPLVESAWTTS 1168
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSpdQPPPDPGQEQTYSVRLHEENWRDS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841 1169 EtprrgdqtvPSPASRADIMTVLQNLEYIMIRGSYDTFQTEVRLGNVFLDTAVTTDTGRgRAFLVE 1234
Cdd:pfam00052   81 D---------GAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
Laminin_B pfam00052
Laminin B (Domain IV);
1495-1604 1.21e-42

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 152.42  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841 1495 YWSLPQKFLGDRVTAYGGNLRFTISFSDL--GDAPTTEPDVIIVGNDITLTYRHSDVMLS--GTKQSFQVPFYEQFWQRP 1570
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLpgGGSLNSEPDVILEGNGLRLSYSSPDQPPPdpGQEQTYSVRLHEENWRDS 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1351476841 1571 DGSPASREFIMMALSDLSAILIKASYTGRTQETR 1604
Cdd:pfam00052   81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVS 114
LamB smart00281
Laminin B domain;
1492-1604 1.25e-39

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 143.56  E-value: 1.25e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  1492 DTYYWSLPQKFLGDRVTAYGGNLRFTISFSDL-GDAPTTEPDVIIVGNDITLTYRHSDVMLSGTKQSFQVPFYEQFWQRP 1570
Cdd:smart00281    3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRrGGTHVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQYY 82

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1351476841  1571 DGSPASREFIMMALSDLSAILIKASYTGRTQETR 1604
Cdd:smart00281   83 GGRPVTREDLMMVLANLTAILIRATYSQQMAGSR 116
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 922-999 8.47e-36

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 130.69  E-value: 8.47e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSIFAQPDAIVVV 999
Cdd:cd05743      1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILTV 78
LamB smart00281
Laminin B domain;
1090-1221 4.01e-33

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 124.68  E-value: 4.01e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  1090 YYFDMPRQFLGNRITSYGGNLQYTVQYQTPTGTqSRLATADVIMKGNGITLYHRRQTQPRPGLTESISVPLVESAWTTSE 1169
Cdd:smart00281    5 VYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG-THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREENWQYYG 83

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1351476841  1170 TprrgdqtvpSPASRADIMTVLQNLEYIMIRGSYDTFQTEVRLGNVFLDTAV 1221
Cdd:smart00281   84 G---------RPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
I-set pfam07679
Immunoglobulin I-set domain;
689-772 4.44e-19

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 83.46  E-value: 4.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAG-----SQALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGT 763
Cdd:pfam07679    2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGqplrsSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81


                   ....*....
gi 1351476841  764 FQATARLIV 772
Cdd:pfam07679   82 AEASAELTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 907-984 2.04e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 75.29  E-value: 2.04e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  907 PTVTIPPRPMImVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALN 984
Cdd:pfam13927    2 PVITVSPSSVT-VREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 694-772 4.15e-16

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: 74.85  E-value: 4.15e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841   694 PRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKA------SDNRGRLTIQGARVEDSGVYECQALGTGGTFQAT 767
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 1351476841   768 ARLIV 772
Cdd:smart00410   81 TTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
907-999 8.96e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 71.13  E-value: 8.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMImVNIGETITITCTAIGVPVPLITWRLNwGHVPKP-PRATQTSENGRGVLVIRNAIETDAGAYTCEALNN 985
Cdd:pfam07679    1 PKFTQKPKDVE-VQEGESARFTCTVTGTPDPEVSWFKD-GQPLRSsDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNS 78

                           90
                   ....*....|....
gi 1351476841  986 KGSIFAqpDAIVVV 999
Cdd:pfam07679   79 AGEAEA--SAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 917-991 2.44e-14

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: 69.84  E-value: 2.44e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841   917 IMVNIGETITITCTAIGVPVPLITWRLNWG-HVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSIFA 991
Cdd:smart00410    4 VTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 689-757 1.25e-13

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 67.59  E-value: 1.25e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALP-----FKASDNRGRLTIQGARVEDSGVYECQA 757
Cdd:pfam13927    3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSgstrsRSLSGSNSTLTISNVTRSDAGTYTCVA 76
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 692-773 1.36e-13

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) 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, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-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, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-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 the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 68.06  E-value: 1.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  692 VSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKAS----------DNRGRLTIQGARVEDSGVYECQALGTG 761
Cdd:cd05726      4 VKPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLLFPYQppqpssrfsvSPTGDLTITNVQRSDVGYYICQALNVA 83

                           90
                   ....*....|..
gi 1351476841  762 GTFQATARLIVS 773
Cdd:cd05726     84 GSILAKAQLEVT 95
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 826-860 1.85e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 62.99  E-value: 1.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  826 CEPNERQCRNGKCILKIWICDGDNDCGDGSDEQNC 860
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 689-772 6.86e-12

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: 62.90  E-value: 6.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALP----FKASDNrGRLTIQGARVEDSGVYECQALGTGGTF 764
Cdd:cd20952      1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGkderITTLEN-GSLQIKGAEKSDTGEYTCVALNLSGEA 79


                   ....*...
gi 1351476841  765 QATARLIV 772
Cdd:cd20952     80 TWSAVLDV 87
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 687-772 1.03e-11

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: 62.41  E-value: 1.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGS--QALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTF 764
Cdd:cd20978      1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKplQGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDI 80


                   ....*...
gi 1351476841  765 QATARLIV 772
Cdd:cd20978     81 YTETLLHV 88
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 613-647 3.78e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 59.14  E-value: 3.78e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  613 CGANQFTCTSGQCIRSSQRCDRRRDCQDGSDEVNC 647
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 909-991 3.97e-11

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 60.93  E-value: 3.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  909 VTIPPRPMImVNIGETITITCTAIGVPVPLITWRLNwgHVPKPPRATQTSENGRG-VLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd04978      2 WIIEPPSLV-LSPGETGELICEAEGNPQPTITWRLN--GVPIEPAPEDMRRTVDGrTLIFSNLQPNDTAVYQCNASNVHG 78


                   ....
gi 1351476841  988 SIFA 991
Cdd:cd04978     79 YLLA 82
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
825-860 4.37e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 58.80  E-value: 4.37e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  825 PCEPNERQCRNGKCILKIWICDGDNDCGDGSDEQNC 860
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 687-770 4.88e-11

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 60.62  E-value: 4.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQ--ALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTF 764
Cdd:cd20957      1 PLSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPlgHSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDGDSA 80


                   ....*.
gi 1351476841  765 QATARL 770
Cdd:cd20957     81 QATAEL 86
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 826-857 1.20e-10

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 57.64  E-value: 1.20e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   826 CEPNERQCRNGKCILKIWICDGDNDCGDGSDE 857
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 496-530 1.35e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 57.60  E-value: 1.35e-10
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  496 CSAGEFRCTDGTCIDSRRRCDNFPDCRDRSDEENC 530
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 925-987 1.41e-10

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: 58.49  E-value: 1.41e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351476841  925 ITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 690-771 2.30e-10

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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: 409412  Cd Length: 85  Bit Score: 58.34  E-value: 2.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQ-ILEGRDAVFQCVA-TGNPPPPVRWFKAGSQaLPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTFQAT 767
Cdd:cd05754      3 VTVEEPRSQeVRPGADVSFICRAkSKSPAYTLVWTRVNGT-LPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTDEAT 81


                   ....
gi 1351476841  768 ARLI 771
Cdd:cd05754     82 ATLY 85
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 922-987 2.69e-10

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: 58.33  E-value: 2.69e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGhvPKPPRATQTSENGrgVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd04968     16 GQTVTLECFALGNPVPQIKWRKVDG--SPSSQWEITTSEP--VLEIPNVQFEDEGTYECEAENSRG 77
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 650-684 3.90e-10

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 56.06  E-value: 3.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  650 CLPGEYRCRNGQCVPRNSRCDRRYDCSDRSDELNC 684
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 705-757 4.16e-10

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: 57.34  E-value: 4.16e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  705 AVFQCVATGNPPPPVRWFKAGSQALPFKASDNR-----GRLTIQGARVEDSGVYECQA 757
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgnGTLTISNVTLEDSGTYTCVA 58
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 691-772 4.18e-10

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: 58.01  E-value: 4.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  691 TVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPfKASDNRGRLT-------IQGARVEDSGVYECQALGTGGT 763
Cdd:cd05763      3 TKTPHDITIRAGSTARLECAATGHPTPQIAWQKDGGTDFP-AARERRMHVMpeddvffIVDVKIEDTGVYSCTAQNSAGS 81


                   ....*....
gi 1351476841  764 FQATARLIV 772
Cdd:cd05763     82 ISANATLTV 90
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1270-1312 4.52e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.59  E-value: 4.52e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1351476841 1270 CNCNGH---SNQCDSDRGVCInCQHNTEGNNCERCKPGFYGDARRG 1312
Cdd:cd00055      2 CDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 907-993 5.03e-10

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: 57.79  E-value: 5.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMIMVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGrgvLVIRNAIETDAGAYTCEALNNK 986
Cdd:cd20978      1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGT---LTIINVQPEDTGYYGCVATNEI 77


                   ....*..
gi 1351476841  987 GSIFAQP 993
Cdd:cd20978     78 GDIYTET 84
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 701-772 6.16e-10

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: 56.87  E-value: 6.16e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  701 EGRDAVFQCVATGNPPPPVRWFKAGSQaLPFkasDNR------GRLTIQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd05745      1 EGQTVDFLCEAQGYPQPVIAWTKGGSQ-LSV---DRRhlvlssGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1270-1317 6.53e-10

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.82  E-value: 6.53e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1351476841 1270 CNCNGH---SNQCDSDRGVCInCQHNTEGNNCERCKPGFYGDaRRGTPGDC 1317
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGL-PSDPPQGC 49
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 702-772 1.31e-09

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: 56.45  E-value: 1.31e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  702 GRDAVFQCVATGNPPPPVRWFKAGsQALPfkaSDNR-----GRLTIQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd05728     14 GSSLRWECKASGNPRPAYRWLKNG-QPLA---SENRieveaGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 689-772 1.68e-09

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: 56.27  E-value: 1.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAG----SQALPFKAS----DNRGRLTIQGARVEDSGVYECQALGT 760
Cdd:cd20951      2 EFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGvpidPSSIPGKYKieseYGVHVLHIRRVTVEDSAVYSAVAKNI 81

                           90
                   ....*....|..
gi 1351476841  761 GGTFQATARLIV 772
Cdd:cd20951     82 HGEASSSASVVV 93
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 687-772 1.70e-09

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: 56.02  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKA-GSQALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTFQ 765
Cdd:cd04968      1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVdGSPSSQWEITTSEPVLEIPNVQFEDEGTYECEAENSRGKDT 80


                   ....*..
gi 1351476841  766 ATARLIV 772
Cdd:cd04968     81 VQGRIIV 87
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 694-772 1.92e-09

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: 56.10  E-value: 1.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  694 PRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQ----ALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTFQATAR 769
Cdd:cd20976      8 PKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPlqyaADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAW 87


                   ...
gi 1351476841  770 LIV 772
Cdd:cd20976     88 VTV 90
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 535-569 2.36e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.13  E-value: 2.36e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  535 CRRDQFRCSNGACIDENKRCDRKLDCQDGTDELGC 569
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 407-442 2.73e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.75  E-value: 2.73e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  407 CHSTEFRCRNnGACITLGQRCDGHRDCADNSDEENC 442
Cdd:cd00112      1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
611-647 2.96e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.79  E-value: 2.96e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  611 RPCGANQFTCTSGQCIRSSQRCDRRRDCQDGSDEVNC 647
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 574-608 3.26e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.75  E-value: 3.26e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  574 CRSGEWRCENGNCIPEAKRCDRTQDCPDNTDELDC 608
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 869-904 3.74e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 53.36  E-value: 3.74e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  869 CRADEYRCVDGnQCIPQSYQCDGEFDCQDSSDEIGC 904
Cdd:cd00112      1 CPPNEFRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
496-530 3.81e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.41  E-value: 3.81e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  496 CSAGEFRCTDGTCIDSRRRCDNFPDCRDRSDEENC 530
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 907-984 4.01e-09

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 55.21  E-value: 4.01e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351476841  907 PTVTIPPRPMIMVNI-GETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRgVLVIRNAIETDAGAYTCEALN 984
Cdd:cd20970      1 PVISTPQPSFTVTAReGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGT-TLTIRNIRRSDMGIYLCIASN 78
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 690-772 5.33e-09

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 55.02  E-value: 5.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQILE-GRDAVFQCVATGNPPPPVRWFKagsQALPFKASDNRGR--------LTIQGARVEDSGVYECQALGT 760
Cdd:cd05738      1 IIDMGPQLKVVEkARTATMLCAASGNPDPEISWFK---DFLPVDTATSNGRikqlrsgaLQIENSEESDQGKYECVATNS 77

                           90
                   ....*....|...
gi 1351476841  761 GGT-FQATARLIV 772
Cdd:cd05738     78 AGTrYSAPANLYV 90
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 613-644 5.59e-09

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 53.02  E-value: 5.59e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   613 CGANQFTCTSGQCIRSSQRCDRRRDCQDGSDE 644
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 449-491 5.86e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 52.98  E-value: 5.86e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1351476841  449 CYSNEFQCRNGgtanapsgSCISITQVCDGHRDCADNTDEENC 491
Cdd:cd00112      1 CPPNEFRCANG--------RCIPSSWVCDGEDDCGDGSDEENC 35
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 912-991 6.05e-09

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) 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, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-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, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-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 the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 54.32  E-value: 6.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  912 PPRPMIMVnIGETITITCTAIGVPVPLITWRLNWGHVPKPpRATQTSENGrgvLVIRNAIETDAGAYTCEALNNKGSIFA 991
Cdd:cd05725      3 RPQNQVVL-VDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILDDHS---LKIRKVTAGDMGSYTCVAENMVGKIEA 77
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 692-772 7.92e-09

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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: 409388  Cd Length: 84  Bit Score: 54.12  E-value: 7.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  692 VSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALP---FKASDNRGrLTIQGARVEDSGVYECQALGTGGTFQATA 768
Cdd:cd05723      2 KKPSNIYAHESMDIVFECEVTGKPTPTVKWVKNGDVVIPsdyFKIVKEHN-LQVLGLVKSDEGFYQCIAENDVGNAQASA 80


                   ....
gi 1351476841  769 RLIV 772
Cdd:cd05723     81 QLII 84
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1270-1312 1.32e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.32e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1351476841  1270 CNCNG---HSNQCDSDRGVCInCQHNTEGNNCERCKPGFYGDARRG 1312
Cdd:smart00180    1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 694-772 1.34e-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: 53.74  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  694 PRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQ---ALPFKASDNRG--RLTIQGARVEDSGVYECQALGTGGTFQATA 768
Cdd:cd20972      8 LRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKElqnSPDIQIHQEGDlhSLIIAEAFEEDTGRYSCLATNSVGSDTTSA 87


                   ....
gi 1351476841  769 RLIV 772
Cdd:cd20972     88 EIFV 91
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 496-527 2.02e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 51.48  E-value: 2.02e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   496 CSAGEFRCTDGTCIDSRRRCDNFPDCRDRSDE 527
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 687-772 3.03e-08

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: 52.72  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAgSQALPFKA--SDNRGRLTIQGARVEDSGVYECQALGTGGTF 764
Cdd:cd05851      1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKI-LEPMPATAeiSMSGAVLKIFNIQPEDEGTYECEAENIKGKD 79


                   ....*...
gi 1351476841  765 QATARLIV 772
Cdd:cd05851     80 KHQARVYV 87
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 694-772 4.19e-08

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) 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, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-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, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-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 the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 52.01  E-value: 4.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  694 PRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQaLPfkasdnRGR--------LTIQGARVEDSGVYECQALGTGGTFQ 765
Cdd:cd05725      4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGE-LP------KGRyeilddhsLKIRKVTAGDMGSYTCVAENMVGKIE 76


                   ....*..
gi 1351476841  766 ATARLIV 772
Cdd:cd05725     77 ASATLTV 83
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 406-439 5.36e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.94  E-value: 5.36e-08
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1351476841   406 TCHSTEFRCRNnGACITLGQRCDGHRDCADNSDE 439
Cdd:smart00192    1 TCPPGEFQCDN-GRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 650-681 6.40e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.94  E-value: 6.40e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   650 CLPGEYRCRNGQCVPRNSRCDRRYDCSDRSDE 681
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 907-991 6.73e-08

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as 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. 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: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 51.78  E-value: 6.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMiMVNIGETITITCTAIGVPVPLITWRlnwGHVPKPPRATQTSENGRG--------VLVIRNAIETDAGAY 978
Cdd:cd05765      1 PALVNSPTHQ-TVKVGETASFHCDVTGRPQPEITWE---KQVPGKENLIMRPNHVRGnvvvtnigQLVIYNAQPQDAGLY 76

                           90
                   ....*....|...
gi 1351476841  979 TCEALNNKGSIFA 991
Cdd:cd05765     77 TCTARNSGGLLRA 89
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 574-605 7.34e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 7.34e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1351476841   574 CRSGEWRCENGNCIPEAKRCDRTQDCPDNTDE 605
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 690-772 9.56e-08

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 51.30  E-value: 9.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGS--QALPFKAS--DNRGRLTIQGARVEDSGVYECQALGTGGTFQ 765
Cdd:cd04978      2 WIIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVpiEPAPEDMRrtVDGRTLIFSNLQPNDTAVYQCNASNVHGYLL 81


                   ....*..
gi 1351476841  766 ATARLIV 772
Cdd:cd04978     82 ANAFLHV 88
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 921-987 1.05e-07

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: 51.18  E-value: 1.05e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  921 IGETITITCTAIGVPVPLITWRlnwgHVPKP-PRATQTSENGrGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05851     15 KGQNVTLECFALGNPVPVIRWR----KILEPmPATAEISMSG-AVLKIFNIQPEDEGTYECEAENIKG 77
IgI_1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the ...
 690-770 1.06e-07

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, 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. 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: 409452  Cd Length: 93  Bit Score: 51.20  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQILEGRDAVFQCVATGNPPPpVRWFK------AGSQALPFKASDNRGRLTIQGARVEDSGVYECQAL-GTGG 762
Cdd:cd05866      3 VSISLSKVELSVGESKFFTCTAIGEPES-IDWYNpqgekiVSSQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATdAKGQ 81


                   ....*...
gi 1351476841  763 TFQATARL 770
Cdd:cd05866     82 TQEATVVL 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 919-988 1.11e-07

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: 51.04  E-value: 1.11e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351476841  919 VNIGETITITCTAIGVPVPL-ITWRLNwGHVPKPPRATQTSENGRGV--LVIRNAIETDAGAYTCEALNNKGS 988
Cdd:pfam00047    8 VLEGDSATLTCSASTGSPGPdVTWSKE-GGTLIESLKVKHDNGRTTQssLLISNVTKEDAGTYTCVVNNPGGS 79
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 699-772 1.19e-07

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first 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: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 51.20  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  699 ILEGRDAVFQCVATGNPPPPVRWFKAG-------SQALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTFQATARLI 771
Cdd:cd20974     12 VLEGSTATFEAHVSGKPVPEVSWFRDGqviststLPGVQISFSDGRAKLSIPAVTKANSGRYSLTATNGSGQATSTAELL 91


                   .
gi 1351476841  772 V 772
Cdd:cd20974     92 V 92
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 690-772 1.29e-07

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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: 409561  Cd Length: 92  Bit Score: 50.85  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQIL---EGRDAVFQCVATGNPPPPVRWFKAGSQALPFKASDNR-----GRLTIQGARVEDSGVYECQALGTG 761
Cdd:cd20969      2 AAIRDRKAQQVfvdEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLtvfpdGTLEVRYAQVQDNGTYLCIAANAG 81

                           90
                   ....*....|.
gi 1351476841  762 GTFQATARLIV 772
Cdd:cd20969     82 GNDSMPAHLHV 92
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 534-566 1.40e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 48.78  E-value: 1.40e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1351476841   534 QCRRDQFRCSNGACIDENKRCDRKLDCQDGTDE 566
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 912-999 1.62e-07

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth 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: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 50.54  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  912 PPRPMIMVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSEngrGVLVIRNAIETDAGAYTCEALNNKGSifA 991
Cdd:cd04969      7 PVKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPD---GSLKIKNVTKSDEGKYTCFAVNFFGK--A 81


                   ....*...
gi 1351476841  992 QPDAIVVV 999
Cdd:cd04969     82 NSTGSLSV 89
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 919-988 1.82e-07

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: 50.19  E-value: 1.82e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  919 VNIGETITITCTAIGVPVPLITWRLNWGHVP-KPPRATqTSENGrgVLVIRNAIETDAGAYTCEALNNKGS 988
Cdd:cd20952     11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLgKDERIT-TLENG--SLQIKGAEKSDTGEYTCVALNLSGE 78
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
868-904 2.05e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 2.05e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  868 PCRADEYRCVDGnQCIPQSYQCDGEFDCQDSSDEIGC 904
Cdd:pfam00057    2 TCSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEENC 37
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1378-1423 2.24e-07

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.89  E-value: 2.24e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1351476841 1378 CNAAGSRLPQPDGR-GQCLCKENTEGPYCDRCKANTFFLSENNPYGC 1423
Cdd:pfam00053    3 CNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
533-569 2.33e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 2.33e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  533 RQCRRDQFRCSNGACIDENKRCDRKLDCQDGTDELGC 569
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 708-772 2.44e-07

Fourth 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 fourth 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: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 50.25  E-value: 2.44e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  708 QCVATGNPPPPVRWFKAGsQALP----FKASD---NRGRLT----IQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd20956     22 KCVASGNPLPQITWTLDG-FPIPesprFRVGDyvtSDGDVVsyvnISSVRVEDGGEYTCTATNDVGSVSHSARINV 96
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 694-772 2.59e-07

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: 50.19  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  694 PRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKAS----DNRGR--LTIQGARVEDSGVYECQALGTGGTFQAT 767
Cdd:cd05744      7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHkmlvRENGRhsLIIEPVTKRDAGIYTCIARNRAGENSFN 86


                   ....*
gi 1351476841  768 ARLIV 772
Cdd:cd05744     87 AELVV 91
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 869-901 2.59e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 48.01  E-value: 2.59e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1351476841   869 CRADEYRCVDGnQCIPQSYQCDGEFDCQDSSDE 901
Cdd:smart00192    2 CPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
650-684 4.19e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.63  E-value: 4.19e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1351476841  650 CLPGEYRCRNGQCVPRNSRCDRRYDCSDRSDELNC 684
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 908-998 4.61e-07

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 49.24  E-value: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  908 TVTIPPRPMIMVNiGETITITCTAIGVPVPLITWRLNWghVPKPPratqTSENGR------GVLVIRNAIETDAGAYTCE 981
Cdd:cd05738      1 IIDMGPQLKVVEK-ARTATMLCAASGNPDPEISWFKDF--LPVDT----ATSNGRikqlrsGALQIENSEESDQGKYECV 73

                           90
                   ....*....|....*..
gi 1351476841  982 ALNNKGSIFAQPDAIVV 998
Cdd:cd05738     74 ATNSAGTRYSAPANLYV 90
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 699-772 4.91e-07

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: 48.94  E-value: 4.91e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  699 ILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKAS-DNRGR-LTIQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd05731      7 VLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKfENFNKtLKIENVSEADSGEYQCTASNTMGSARHTISVTV 82
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 914-989 6.04e-07

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: 49.14  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  914 RPMIMVNIGETITITCTAIGVPVPLITWRLNwgHVPKPP----RATQTSENGrGVLVIRNAIETDAGAYTCEALNNKGSI 989
Cdd:cd05729     11 EREHALPAANKVRLECGAGGNPMPNITWLKD--GKEFKKehriGGTKVEEKG-WSLIIERAIPRDKGKYTCIVENEYGSI 87
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 692-772 7.51e-07

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the 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 (Slit-1,Slit-2, Slit-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, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-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 Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 48.55  E-value: 7.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  692 VSPRQLQILEGRDAVFQCVA-TGNPPPPVRWFKAGSqalPFKASDNR------GRLTIQGARVEDSGVYECQALGTGGTF 764
Cdd:cd05724      2 VEPSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQ---PLNLDNERvrivddGNLLIAEARKSDEGTYKCVATNMVGER 78


                   ....*....
gi 1351476841  765 Q-ATARLIV 772
Cdd:cd05724     79 EsRAARLSV 87
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 701-772 7.76e-07

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: 48.66  E-value: 7.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  701 EGRDAVFQCVATG-NPPPPVRWFKAG-------SQALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd05750     13 EGSKLVLKCEATSeNPSPRYRWFKDGkelnrkrPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVTGNVTV 92
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 922-989 1.10e-06

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: 48.40  E-value: 1.10e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGHVPKPPrATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSI 989
Cdd:cd20976     16 GQDFVAQCSARGKPVPRITWIRNAQPLQYAA-DRSTCEAGVGELHIQDVLPEDHGTYTCLAKNAAGQV 82
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 692-770 1.40e-06

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: 47.96  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  692 VSPRQLQILEGRDAVFQC-VATGNPPPPVRWFKAGSQ-ALPFKASDNRGR-----LTIQGARVEDSGVYECQALGTGGTF 764
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCsASTGSPGPDVTWSKEGGTlIESLKVKHDNGRttqssLLISNVTKEDAGTYTCVVNNPGGSA 80


                   ....*.
gi 1351476841  765 QATARL 770
Cdd:pfam00047   81 TLSTSL 86
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 448-488 1.59e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.09  E-value: 1.59e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1351476841   448 RCYSNEFQCRNGgtanapsgSCISITQVCDGHRDCADNTDE 488
Cdd:smart00192    1 TCPPGEFQCDNG--------RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
573-608 1.64e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.09  E-value: 1.64e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1351476841  573 PCRSGEWRCENGNCIPEAKRCDRTQDCPDNTDELDC 608
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 687-772 1.76e-06

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as 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. 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: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 47.93  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVtVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKA--GSQALPFKASD--------NRGRLTIQGARVEDSGVYECQ 756
Cdd:cd05765      1 PALV-NSPTHQTVKVGETASFHCDVTGRPQPEITWEKQvpGKENLIMRPNHvrgnvvvtNIGQLVIYNAQPQDAGLYTCT 79

                           90
                   ....*....|....*.
gi 1351476841  757 ALGTGGTFQATARLIV 772
Cdd:cd05765     80 ARNSGGLLRANFPLSV 95
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 109-174 1.87e-06

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 48.00  E-value: 1.87e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  109 EYFRVTINITSMDYHPALSDRYSPEFQELSTQLAAALTRLFADID-GTQQIN--ILQFRR--GSLMVTFDL 174
Cdd:pfam01390    1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSlRKQYIKshVLRLRPdgGSVVVDVVL 71
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
406-442 1.99e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 45.70  E-value: 1.99e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1351476841  406 TCHSTEFRCrNNGACITLGQRCDGHRDCADNSDEENC 442
Cdd:pfam00057    2 TCSPNEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 690-763 2.41e-06

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 47.24  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKaGSQALpfkASDNR------GRLTIQGARVEDSGVYECQALGTGGT 763
Cdd:cd20968      2 ITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIK-GDDLI---KENNRiavlesGSLRIHNVQKEDAGQYRCVAKNSLGI 77
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 690-770 2.84e-06

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 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-nonNCAM) 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 the Ig1, Ig2, and Ig3 domains. 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). 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: 409366  Cd Length: 95  Bit Score: 47.25  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQILEGRDAVFQCVATGNPPPpVRWFKA-GSQALPFKAS-------DNRGRLTIQGARVEDSGVYECQAL-GT 760
Cdd:cd04977      3 VKIIPSYAEISVGESKFFLCKVSGDAKN-INWVSPnGEKVLTKHGNlkvvnhgSVLSSLTIYNANINDAGIYKCVATnGK 81

                           90
                   ....*....|
gi 1351476841  761 GGTFQATARL 770
Cdd:cd04977     82 GTESEATVKL 91
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 919-998 2.92e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 46.62  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  919 VNIGETITITCTAIGVPVPLITWRlnwghvpKPPRATQTSENgrgvLVIRNAIETDAGAYTCEALNNKGSIFAQPDAIVV 998
Cdd:pfam13895   11 VTEGEPVTLTCSAPGNPPPSYTWY-------KDGSAISSSPN----FFTLSVSAEDSGTYTCVARNGRGGKVSNPVELTV 79
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 922-998 3.51e-06

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 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.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 46.81  E-value: 3.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNW----GHVPKPPRATQtsengRGVLVIRNAIETDAGAYTCEALNNKGSIFAQPDAIV 997
Cdd:cd05867     14 GETARLDCQVEGIPTPNITWSINGapieGTDPDPRRHVS-----SGALILTDVQPSDTAVYQCEARNRHGNLLANAHVHV 88


                   .
gi 1351476841  998 V 998
Cdd:cd05867     89 V 89
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1378-1423 3.61e-06

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 45.42  E-value: 3.61e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1351476841 1378 CNAAGSRLPQPD-GRGQCLCKENTEGPYCDRCKANTFFLSEnNPYGC 1423
Cdd:cd00055      4 CNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGC 49
IgI_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
 907-988 3.74e-06

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409458  Cd Length: 95  Bit Score: 46.90  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMIMVNIGETITITCTAIGVPVPLITWRLNWGH--VPKPPRATQTSENGRGVLVIRNAIETDA--GAYTCEA 982
Cdd:cd05874      1 PTITHQSPKDYIVDPRENIVIQCEAKGKPPPSFSWTRNGTHfdIDKDPKVTMKPNTGTLVINIMNGEKAEAyeGVYQCTA 80


                   ....*.
gi 1351476841  983 LNNKGS 988
Cdd:cd05874     81 RNERGA 86
IgI_1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the ...
 917-987 3.78e-06

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, 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. 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: 409452  Cd Length: 93  Bit Score: 46.97  E-value: 3.78e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  917 IMVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05866     10 VELSVGESKFFTCTAIGEPESIDWYNPQGEKIVSSQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATDAKG 80
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 908-984 4.50e-06

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 46.37  E-value: 4.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351476841  908 TVTIPPrPMIMVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENgrgVLVIRNAIETDAGAYTCEALN 984
Cdd:cd20957      3 SATIDP-PVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRN 75
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 911-992 4.57e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) 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, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-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, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-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 the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 46.87  E-value: 4.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  911 IPPRPMImVNIGETITITCTAIGVPVPLITWR------LNWGHVPKPPrATQTSENGRGVLVIRNAIETDAGAYTCEALN 984
Cdd:cd05726      4 VKPRDQV-VALGRTVTFQCETKGNPQPAIFWQkegsqnLLFPYQPPQP-SSRFSVSPTGDLTITNVQRSDVGYYICQALN 81


                   ....*...
gi 1351476841  985 NKGSIFAQ 992
Cdd:cd05726     82 VAGSILAK 89
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 689-772 4.68e-06

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: 46.49  E-value: 4.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPfKASD------NRGRLTIQGARVEDSGVYECQALGTGG 762
Cdd:cd05736      2 VIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINP-KLSKqltliaNGSELHISNVRYEDTGAYTCIAKNEGG 80

                           90
                   ....*....|
gi 1351476841  763 TFQATARLIV 772
Cdd:cd05736     81 VDEDISSLFV 90
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 707-772 5.06e-06

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: 46.44  E-value: 5.06e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351476841  707 FQCVATGNPPPPVRWFKAGSQALP------FKASDNRGRLTIQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd05729     24 LECGAGGNPMPNITWLKDGKEFKKehriggTKVEEKGWSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
448-491 5.11e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.55  E-value: 5.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1351476841  448 RCYSNEFQCRnggtanapSGSCISITQVCDGHRDCADNTDEENC 491
Cdd:pfam00057    2 TCSPNEFQCG--------SGECIPRSWVCDGDPDCGDGSDEENC 37
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 917-1000 5.14e-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: 46.25  E-value: 5.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  917 IMVNIGETITITCTAIGVPVPLITWRLNWGHVPKpprATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSifAQPDAI 996
Cdd:cd05731      5 TMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPK---GRTKFENFNKTLKIENVSEADSGEYQCTASNTMGS--ARHTIS 79


                   ....
gi 1351476841  997 VVVK 1000
Cdd:cd05731     80 VTVE 83
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 922-989 5.92e-06

Fourth 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 fourth 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: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 5.92e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGHVPKPPRATQ---TSENGRGV--LVIRNAIETDAGAYTCEALNNKGSI 989
Cdd:cd20956     16 GPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVgdyVTSDGDVVsyVNISSVRVEDGGEYTCTATNDVGSV 88
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 708-772 6.65e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); 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 like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. 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: 409442  Cd Length: 92  Bit Score: 46.01  E-value: 6.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  708 QCVATGNPPPPVRWFKAGSQALPFKASDNRGR---LTIQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd05856     25 KCVASGNPRPDITWLKDNKPLTPPEIGENKKKkwtLSLKNLKPEDSGKYTCHVSNRAGEINATYKVDV 92
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 791-821 6.84e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.12  E-value: 6.84e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1351476841  791 FQCLDReKCLPNDYKCDGDYDCTDRSDELNC 821
Cdd:cd00112      6 FRCANG-RCIPSSWVCDGEDDCGDGSDEENC 35
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 690-772 7.39e-06

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: 46.49  E-value: 7.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFK----AGSQAL----PFKASDNRGR-------------LTIQGARVE 748
Cdd:cd04983      1 VTQSPQSLSVQEGENVTLNCNYSTSTFYYLFWYRqypgQGPQFLiyisSDSGNKKKGRfsatldksrksssLHISAAQLS 80

                           90       100
                   ....*....|....*....|....*...
gi 1351476841  749 DSGVYECQALGTGG----TFQATARLIV 772
Cdd:cd04983     81 DSAVYFCALSESGGtgklTFGKGTRLTV 108
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 913-988 1.08e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); 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, 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, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 45.29  E-value: 1.08e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  913 PRPMIMVNIGETITITCTAIGVPVPLITWRLNWGhvPKPPRATQTSENGRgVLVIRNAIETDAGAYTCEALNNKGS 988
Cdd:cd05876      1 SSSSLVALRGQSLVLECIAEGLPTPTVKWLRPSG--PLPPDRVKYQNHNK-TLQLLNVGESDDGEYVCLAENSLGS 73
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 695-772 1.21e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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: 409474  Cd Length: 92  Bit Score: 45.47  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  695 RQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPF-------KASDNRGRLTIQGARVEDSGVYECQALGTGGTFQAT 767
Cdd:cd05893      8 KHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKsdhytiqRDLDGTCSLHTTASTLDDDGNYTIMAANPQGRISCT 87


                   ....*
gi 1351476841  768 ARLIV 772
Cdd:cd05893     88 GRLMV 92
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1378-1423 1.53e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 43.45  E-value: 1.53e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1351476841  1378 CNAAGSRLPQPDGR-GQCLCKENTEGPYCDRCKANTFFlseNNPYGC 1423
Cdd:smart00180    3 CDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 922-987 1.64e-05

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: 44.79  E-value: 1.64e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNwGHVPKPPRATQ--TSENGRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05744     15 GRLCRFDCKVSGLPTPDLFWQLN-GKPVRPDSAHKmlVRENGRHSLIIEPVTKRDAGIYTCIARNRAG 81
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 691-772 1.80e-05

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 44.51  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  691 TVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPfkasDNR---GRLTIQGARVEDSGVYECQALGTGGTFQAT 767
Cdd:cd05739      1 SIPPSNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTK----EDEmpvGRNVLELTNIYESANYTCVAISSLGMIEAT 76


                   ....*
gi 1351476841  768 ARLIV 772
Cdd:cd05739     77 AQVTV 81
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 698-772 2.03e-05

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  698 QILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKAS---DNRGR-LTIQGARVEDSGVYECQAL-GTGGTFQATARLIV 772
Cdd:cd20970     13 TAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRyivRENGTtLTIRNIRRSDMGIYLCIASnGVPGSVEKRITLQV 92
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
791-821 2.10e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.01  E-value: 2.10e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1351476841  791 FQCLDREkCLPNDYKCDGDYDCTDRSDELNC 821
Cdd:pfam00057    8 FQCGSGE-CIPRSWVCDGDPDCGDGSDEENC 37
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 690-772 2.52e-05

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: 45.02  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  690 VTVSPRQLQILEGRDAVFQCVATG-NPPPPVRWFK-AGSQALPF----------------------KASDNRGRLTIQGA 745
Cdd:cd00099      1 VTQSPRSLSVQEGESVTLSCEVSSsFSSTYIYWYRqKPGQGPEFliylssskgktkggvpgrfsgsRDGTSSFSLTISNL 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1351476841  746 RVEDSGVYECQALGTGGTFQAT----ARLIV 772
Cdd:cd00099     81 QPEDSGTYYCAVSESGGTDKLTfgsgTRLTV 111
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 687-760 2.52e-05

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first 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, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. 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 lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 44.32  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSqalPFKASD--------NRGRLTIQ--GARVED-SGVYEC 755
Cdd:cd05733      1 PTITEQSPKDYIVDPRDNITIKCEAKGNPQPTFRWTKDGK---FFDPAKdprvsmrrRSGTLVIDnhNGGPEDyQGEYQC 77


                   ....*...
gi 1351476841  756 QA---LGT 760
Cdd:cd05733     78 YAsneLGT 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 917-988 2.93e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 43.73  E-value: 2.93e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351476841  917 IMVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGS 988
Cdd:cd05748      2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGE 73
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 907-987 2.93e-05

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: 44.17  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMIMvNIGETITITCTAIGVPVPLITWRLNWGHV-PKPPRATQTSENGRGvLVIRNAIETDAGAYTCEALNN 985
Cdd:cd05736      1 PVIRVYPEFQAK-EPGVEASLRCHAEGIPLPRVQWLKNGMDInPKLSKQLTLIANGSE-LHISNVRYEDTGAYTCIAKNE 78


                   ..
gi 1351476841  986 KG 987
Cdd:cd05736     79 GG 80
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 691-763 3.07e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. 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. The Ig-like domain of the Twitchin is a member of the I-set 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. 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.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 44.24  E-value: 3.07e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  691 TVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKASDNRGR-----LTIQGARVEDSGVYECQALGTGGT 763
Cdd:cd20949      3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMSKYRiladgLLINKVTQDDTGEYTCRAYQVNSI 80
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 922-987 3.14e-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: 44.44  E-value: 3.14e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  922 GETITITCTAIGVPVPLITWRL---NWGHVPKPP--RATQTSENGRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05732     16 LEQITLTCEAEGDPIPEITWRRatrGISFEEGDLdgRIVVRGHARVSSLTLKDVQLTDAGRYDCEASNRIG 86
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 686-753 5.45e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 43.36  E-value: 5.45e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351476841  686 VPTVVTvsprqlqILEGRDAVFQCVATGNPPPPVRWFKAGSQALP---FKASDNRGR---LTIQGARVEDSGVY 753
Cdd:cd05891      7 LPDVVT-------IMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELsehYSVKLEQGKyasLTIKGVTSEDSGKY 73
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 912-988 6.27e-05

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 43.25  E-value: 6.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  912 PPRPMIMVN-----IGETITITCTAIGVPVPLITWRLNWG-----HVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCE 981
Cdd:cd05734      1 PPRFVVQPNdqdgiYGKAVVLNCSADGYPPPTIVWKHSKGsgvpqFQHIVPLNGRIQLLSNGSLLIKHVLEEDSGYYLCK 80


                   ....*..
gi 1351476841  982 ALNNKGS 988
Cdd:cd05734     81 VSNDVGA 87
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 920-1000 6.37e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third 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.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.38  E-value: 6.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  920 NIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGrGVLVIRNAIETDAGAYTCEALNNKGsifaQPDAIVVV 999
Cdd:cd05730     16 NLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDG-SEMTILDVDKLDEAEYTCIAENKAG----EQEAEIHL 90


                   .
gi 1351476841 1000 K 1000
Cdd:cd05730     91 K 91
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 686-753 7.89e-05

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.96  E-value: 7.89e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351476841  686 VPTVVTvsprqlqILEGRDAVFQCVATGNPPPPVRWFKaGSQALPFKASDN----RGR---LTIQGARVEDSGVY 753
Cdd:cd05737      7 LPDVVT-------IMEGKTLNLTCNVWGDPPPEVSWLK-NDQALAFLDHCNlkveAGRtvyFTINGVSSEDSGKY 73
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 923-989 7.91e-05

First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; The members here are composed of the first 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: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 43.00  E-value: 7.91e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  923 ETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRgvLVIRNAIET-DAGAYTCEALNNKGSI 989
Cdd:cd04967     20 KKVALNCRARANPVPSYRWLMNGTEIDLESDYRYSLVDGT--LVISNPSKAkDAGHYQCLATNTVGSV 85
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 909-998 8.47e-05

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 42.61  E-value: 8.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  909 VTIPPRPMIMVnIGETITITCTAIGVPVPLITWrlnwghvpkPPRATQTSENGR------GVLVIRNAIETDAGAYTCEA 982
Cdd:cd20968      2 ITRPPTNVTII-EGLKAVLPCTTMGNPKPSVSW---------IKGDDLIKENNRiavlesGSLRIHNVQKEDAGQYRCVA 71

                           90
                   ....*....|....*.
gi 1351476841  983 LNNKGSIFAQPDAIVV 998
Cdd:cd20968     72 KNSLGIAYSKPVTIEV 87
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 917-987 1.12e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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: 409582  Cd Length: 91  Bit Score: 42.39  E-value: 1.12e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351476841  917 IMVNIGETITITCTAIGVPVPLITWRLNWGHV-PKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd20990     10 LTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIrPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAG 81
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 915-991 1.37e-04

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: 42.22  E-value: 1.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351476841  915 PM-IMVNIGETITITCTAIGVPVPLITWRLNWG-HVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSIFA 991
Cdd:cd05763      6 PHdITIRAGSTARLECAATGHPTPQIAWQKDGGtDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISA 84
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 908-985 1.73e-04

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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: 409412  Cd Length: 85  Bit Score: 41.77  E-value: 1.73e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351476841  908 TVTIPPRPMIMVNIGETITITCTAIG-VPVPLITWRLNWGhvPKPPRATQTSengrGVLVIRNAIETDAGAYTCEALNN 985
Cdd:cd05754      2 QVTVEEPRSQEVRPGADVSFICRAKSkSPAYTLVWTRVNG--TLPSRAMDFN----GILTIRNVQLSDAGTYVCTGSNM 74
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 701-772 1.88e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 41.61  E-value: 1.88e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351476841  701 EGRDAVFQCVATGNPPPPVRWFKAGsqalpfKASDNRGRLTIQGARVEDSGVYECQA-LGTGGTFQATARLIV 772
Cdd:pfam13895   13 EGEPVTLTCSAPGNPPPSYTWYKDG------SAISSSPNFFTLSVSAEDSGTYTCVArNGRGGKVSNPVELTV 79
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 907-988 1.90e-04

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first 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, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. 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 lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 42.01  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMIMVNIGETITITCTAIGVPVPLITWRLNWGH--VPKPPRATQTSENGRGVLVIRNAIETD-AGAYTCEAL 983
Cdd:cd05733      1 PTITEQSPKDYIVDPRDNITIKCEAKGNPQPTFRWTKDGKFfdPAKDPRVSMRRRSGTLVIDNHNGGPEDyQGEYQCYAS 80


                   ....*
gi 1351476841  984 NNKGS 988
Cdd:cd05733     81 NELGT 85
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 919-987 1.95e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(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. 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: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.89  E-value: 1.95e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  919 VNIGETITITCTAIGVPVPLITWRLNWGHVpkppRATQTSENGRGV---------LVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05869     14 MELEEQITLTCEASGDPIPSITWRTSTRNI----SSEEKTLDGHIVvrsharvssLTLKYIQYTDAGEYLCTASNTIG 87
IgI_hNeurofascin_like cd05875
Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig ...
 907-988 2.03e-04

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. 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 lacks a C" strand.


Pssm-ID: 409459  Cd Length: 95  Bit Score: 41.88  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMIMVNIGETITITCTAIGVPVPLITWRLN--WGHVPKPPRATQTSENgrGVLVIRNA----IETDAGAYTC 980
Cdd:cd05875      1 PTITKQSAKDYIVDPRDNILIECEAKGNPVPTFHWTRNgkFFNVAKDPRVSMRRRS--GTLVIDFRgggrPEDYEGEYQC 78


                   ....*...
gi 1351476841  981 EALNNKGS 988
Cdd:cd05875     79 FARNKFGT 86
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 694-772 2.08e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. 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: 409473  Cd Length: 92  Bit Score: 41.68  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  694 PRQLQILEGRDAVFQCVATGNPPPPVRWfKAGSQALPFKAS------DNRGRLT--IQGARVEDSGVYECQALGTGGTFQ 765
Cdd:cd05892      7 PQNKKVLEGDPVRLECQISAIPPPQIFW-KKNNEMLQYNTDrislyqDNCGRICllIQNANKKDAGWYTVSAVNEAGVVS 85


                   ....*..
gi 1351476841  766 ATARLIV 772
Cdd:cd05892     86 CNARLDV 92
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
 912-983 2.31e-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: 42.14  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  912 PPRPMIMVNIGETITITCTAIgVPVPLITwRLNW---------GHVPKPPRATQTSENG--RGVLVIRNAIETDAGAYTC 980
Cdd:cd05742      7 PNAEPTVLPQGETLVLNCTAN-VNLNEVV-DFQWtypsekegkLALLKPDIKVDWSEPGefVSTLTIPEATLKDSGTYTC 84


                   ...
gi 1351476841  981 EAL 983
Cdd:cd05742     85 AAR 87
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 912-988 2.59e-04

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: 41.53  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  912 PPR----PM-IMVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSEN----GRGVLVIRNAIETDAGAYTCEA 982
Cdd:cd20954      1 PPRwivePVdANVAAGQDVMLHCQADGFPTPTVTWKKATGSTPGEYKDLLYDPNvrilPNGTLVFGHVQKENEGHYLCEA 80


                   ....*.
gi 1351476841  983 LNNKGS 988
Cdd:cd20954     81 KNGIGS 86
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 709-762 2.80e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth 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: 143223  Cd Length: 69  Bit Score: 40.63  E-value: 2.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1351476841  709 CVATGNPPPPVRWFKAGSQAL---PFKASDNrGRLTIQGARVEDSGVYECQALGTGG 762
Cdd:cd05746      5 CSAQGDPEPTITWNKDGVQVTesgKFHISPE-GYLAIRDVGVADQGRYECVARNTIG 60
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 919-988 2.86e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). 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 human APEG-1 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: 409567  Cd Length: 91  Bit Score: 41.30  E-value: 2.86e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  919 VNIGETITITCTAIGVPVPLITWRLNWGHV-PKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGS 988
Cdd:cd20975     12 VREGQDVIMSIRVQGEPKPVVSWLRNRQPVrPDQRRFAEEAEGGLCRLRILAAERGDAGFYTCKAVNEYGA 82
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 686-772 3.04e-04

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: 41.67  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  686 VPTVVTVSprqlqilEGRDAVFQCVATG---NPPPPVRWFKAGSQALPFKA-----------------------SDNRGR 739
Cdd:pfam07686    2 TPREVTVA-------LGGSVTLPCTYSSsmsEASTSVYWYRQPPGKGPTFLiayysngseegvkkgrfsgrgdpSNGDGS 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1351476841  740 LTIQGARVEDSGVYECQALGTG-GTFQATARLIV 772
Cdd:pfam07686   75 LTIQNLTLSDSGTYTCAVIPSGeGVFGKGTRLTV 108
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 699-764 3.24e-04

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 41.01  E-value: 3.24e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351476841  699 ILEGRDAVFQCVATGNPPPPVRWFKAGSQaLPF----KASDNrGRLTIQGA-RVEDSGVYECQALGTGGTF 764
Cdd:cd20958     12 AVAGQTLRLHCPVAGYPISSITWEKDGRR-LPLnhrqRVFPN-GTLVIENVqRSSDEGEYTCTARNQQGQS 80
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 925-988 3.27e-04

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth 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: 143223  Cd Length: 69  Bit Score: 40.63  E-value: 3.27e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  925 ITITCTAIGVPVPLITWRLNwghvpkpprATQTSENGR------GVLVIRNAIETDAGAYTCEALNNKGS 988
Cdd:cd05746      1 VQIPCSAQGDPEPTITWNKD---------GVQVTESGKfhispeGYLAIRDVGVADQGRYECVARNTIGY 61
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 686-753 4.00e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. 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: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 41.19  E-value: 4.00e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351476841  686 VPTVVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAG-----SQALPFKASDNRGRLTIQGARVEDSGVY 753
Cdd:cd05747      2 LPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGqiivsSQRHQITSTEYKSTFEISKVQMSDEGNY 74
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 692-772 4.22e-04

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). 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 human APEG-1 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: 409567  Cd Length: 91  Bit Score: 40.92  E-value: 4.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  692 VSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFK------ASDNRGRLTIQGARVEDSGVYECQALGTGGTFQ 765
Cdd:cd20975      5 VSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQrrfaeeAEGGLCRLRILAAERGDAGFYTCKAVNEYGARQ 84


                   ....*..
gi 1351476841  766 ATARLIV 772
Cdd:cd20975     85 CEARLEV 91
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 693-768 4.52e-04

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409454  Cd Length: 89  Bit Score: 40.73  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  693 SPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGS--QALPFKASDNRGRLTIQGARVED--SGVYECQALGTGGTFQATA 768
Cdd:cd05868      5 APTNLVLSPGEDGTLICRANGNPKPSISWLTNGVpiEIAPTDPSRKVDGDTIIFSKVQErsSAVYQCNASNEYGYLLANA 84
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 922-987 4.77e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. 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: 409473  Cd Length: 92  Bit Score: 40.91  E-value: 4.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGHVP-KPPRATQTSEN-GRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05892     15 GDPVRLECQISAIPPPQIFWKKNNEMLQyNTDRISLYQDNcGRICLLIQNANKKDAGWYTVSAVNEAG 82
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 791-818 5.35e-04

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 38.77  E-value: 5.35e-04
                            10        20
                    ....*....|....*....|....*...
gi 1351476841   791 FQCLDReKCLPNDYKCDGDYDCTDRSDE 818
Cdd:smart00192    7 FQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
 695-757 5.58e-04

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: 40.30  E-value: 5.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  695 RQLQILEGRDAVFQCVATGnPPPPVRWFKAG-----SQALPFKASDNRGRLTIQGARVEDSGVYECQA 757
Cdd:cd20967      5 PAVQVSKGHKIRLTVELAD-PDAEVKWYKDGqelqsSSKVIFESIGAKRTLTVQQASLADAGEYQCVA 71
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 914-991 8.20e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); 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 like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. 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: 409442  Cd Length: 92  Bit Score: 40.23  E-value: 8.20e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1351476841  914 RPMIMVNIGETITITCTAIGVPVPLITWRLNwgHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKGSIFA 991
Cdd:cd05856     11 RRVIARPVGSSVRLKCVASGNPRPDITWLKD--NKPLTPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINA 86
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 687-767 9.02e-04

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: 40.23  E-value: 9.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTvSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGsQALPFKASDNRGR-----------LTIQGARV--EDSGVY 753
Cdd:cd07693      1 PRIVE-HPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNG-QPLETDKDDPRSHrivlpsgslffLRVVHGRKgrSDEGVY 78

                           90
                   ....*....|....*..
gi 1351476841  754 ECQA---LGTGGTFQAT 767
Cdd:cd07693     79 VCVAhnsLGEAVSRNAS 95
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 689-770 9.27e-04

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: 39.77  E-value: 9.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKA-------GSQALPFkasdNRGRLTIQGARVEDSGVYECQALGTG 761
Cdd:cd05764      2 LITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPegklisnSSRTLVY----DNGTLDILITTVKDTGAFTCIASNPA 77


                   ....*....
gi 1351476841  762 GtfQATARL 770
Cdd:cd05764     78 G--EATARV 84
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 691-761 1.20e-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: 39.60  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  691 TVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKA-GSQALPFK--ASDNR------GRLTIQGARVEDSGVYECQA---L 758
Cdd:cd20954      5 IVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKAtGSTPGEYKdlLYDPNvrilpnGTLVFGHVQKENEGHYLCEAkngI 84


                   ...
gi 1351476841  759 GTG 761
Cdd:cd20954     85 GSG 87
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 687-777 1.23e-03

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: 39.84  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTVSPRQLQILEGRDAVFQCVATGNPP-----------PPVRWFKAGSQALPFKASDNRGRLTIQGARVEDSGVYEC 755
Cdd:cd04970      2 ATRITLAPSNADITVGENATLQCHASHDPTldltftwsfngVPIDLEKIEGHYRRRYGKDSNGDLEIVNAQLKHAGRYTC 81

                           90       100
                   ....*....|....*....|..
gi 1351476841  756 QALGTGGTFQATARLIVsRGQP 777
Cdd:cd04970     82 TAQTVVDSDSASATLVV-RGPP 102
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 700-763 1.27e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); 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, 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, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 39.12  E-value: 1.27e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  700 LEGRDAVFQCVATGNPPPPVRWFKAGSQALPFKAS--DNRGRLTIQGARVEDSGVYECQALGTGGT 763
Cdd:cd05876      8 LRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKyqNHNKTLQLLNVGESDDGEYVCLAENSLGS 73
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 707-773 1.33e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 39.01  E-value: 1.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351476841  707 FQCVATGNPPPPVRW-FKAG----SQALPFKASDNRGRLTIQGARVEDSGVYECQALGTGGTFQATARLIVS 773
Cdd:cd05743      6 FTCVATGVPTPIINWrLNWGhvpdSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILT 77
IgI_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
 687-774 1.42e-03

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409458  Cd Length: 95  Bit Score: 39.58  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  687 PTVVTVSPRQLQILEGRDAVFQCVATGNPPPPVRWFKAGSQALPFK-----ASDNRGRLTIQ---GARVED-SGVYECQA 757
Cdd:cd05874      1 PTITHQSPKDYIVDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIDKdpkvtMKPNTGTLVINimnGEKAEAyEGVYQCTA 80

                           90
                   ....*....|....*..
gi 1351476841  758 LGTGGTfqATARLIVSR 774
Cdd:cd05874     81 RNERGA--AVSNNIVIR 95
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 907-1000 1.86e-03

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: 39.33  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMiMVNIGETITITCTAIGVPVPLITWRLNwgHVP-----KPPRATQTSENGRGVLVIRNAIETDAGAYTCE 981
Cdd:cd20951      1 PEFIIRLQSH-TVWEKSDAKLRVEVQGKPDPEVKWYKN--GVPidpssIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAV 77

                           90
                   ....*....|....*....
gi 1351476841  982 ALNNKGSifAQPDAIVVVK 1000
Cdd:cd20951     78 AKNIHGE--ASSSASVVVE 94
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 907-988 1.94e-03

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: 39.10  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRPMiMVNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNK 986
Cdd:cd20972      2 PQFIQKLRSQ-EVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80


                   ..
gi 1351476841  987 GS 988
Cdd:cd20972     81 GS 82
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 695-772 2.28e-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: 38.71  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  695 RQLQILEGRDAVFQCVATGNPPPPVRWFKAGSqalPFKAS---------DNRGRLTIQGARVEDSGVYECQALGTGGTFQ 765
Cdd:cd20973      5 RDKEVVEGSAARFDCKVEGYPDPEVKWMKDDN---PIVESrrfqidqdeDGLCSLIISDVCGDDSGKYTCKAVNSLGEAT 81


                   ....*..
gi 1351476841  766 ATARLIV 772
Cdd:cd20973     82 CSAELTV 88
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 919-991 2.51e-03

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: 38.35  E-value: 2.51e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351476841  919 VNIGETITITCTAIGVPVPLITWRLNWGHVPKPPRAtqtsENGRGVLVIRNAIETDAGAYTCEALNNKGSIFA 991
Cdd:cd05728     11 ADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRI----EVEAGDLRITKLSLSDSGMYQCVAENKHGTIYA 79
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 912-987 2.57e-03

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 38.70  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  912 PP--RPMIMVNI--GETITITCTAIGVPVPLITWRlnwghvpkppRATQT-SENGR------GVLVIRNA-IETDAGAYT 979
Cdd:cd20958      1 PPfiRPMGNLTAvaGQTLRLHCPVAGYPISSITWE----------KDGRRlPLNHRqrvfpnGTLVIENVqRSSDEGEYT 70


                   ....*...
gi 1351476841  980 CEALNNKG 987
Cdd:cd20958     71 CTARNQQG 78
Ig1_FcgammaR_like cd05752
First immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; ...
 689-761 2.68e-03

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: 38.11  E-value: 2.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  689 VVTVSPRQLQILEGRDAVFQCvaTGNPPP---PVRWFKAGSqALPFKASDnrgrLTIQGARVEDSGVYECQALGTG 761
Cdd:cd05752      2 VVSLDPPWTTVFQGEKVTLTC--QGFYSPeqnSTQWYHNGT-LISSTSSS----YRIVAATVNDSGEYRCQTQGSS 70
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 707-772 3.02e-03

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 38.68  E-value: 3.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351476841  707 FQCVATGNPPPPVRWFKAGSqalPFKASDNRG---------RLTIQGARVEDSGVYECQALGTGGTFQATARLIV 772
Cdd:cd05857     24 FRCPAAGNPTPTMRWLKNGK---EFKQEHRIGgykvrnqhwSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 95
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
 922-987 3.34e-03

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: 38.42  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351476841  922 GETITITCTAIGVPVPLITWR-----LNWGHVPKPP--RATQTSENGRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05870     16 NGAATLSCKAEGEPIPEITWKrasdgHTFSEGDKSPdgRIEVKGQHGESSLHIKDVKLSDSGRYDCEAASRIG 88
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 913-984 3.41e-03

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


Pssm-ID: 409368  Cd Length: 88  Bit Score: 38.21  E-value: 3.41e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351476841  913 PRPMIMVNIGETITITCT--AIGVPVpliTWRLNWGHVPKPPRATQTSEnGRGVLVIRNAIETDAGAYTCEALN 984
Cdd:cd04979      2 SFKQISVKEGDTVILSCSvkSNNAPV---TWIHNGKKVPRYRSPRLVLK-TERGLLIRSAQEADAGVYECHSGE 71
IgI_NCAM-2 cd05870
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 2 (NCAM-2); The members ...
 692-770 5.08e-03

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: 38.03  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  692 VSPRQLQI-----LEGRDAVFQCVATGNPPPPVRWFKAgSQALPFKASDN--------RGR-----LTIQGARVEDSGVY 753
Cdd:cd05870      1 VQPHIIQLknettVENGAATLSCKAEGEPIPEITWKRA-SDGHTFSEGDKspdgrievKGQhgessLHIKDVKLSDSGRY 79

                           90
                   ....*....|....*..
gi 1351476841  754 ECQALGTGGTFQATARL 770
Cdd:cd05870     80 DCEAASRIGGHQKSMYL 96
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
 907-988 6.69e-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: 37.68  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  907 PTVTIPPRpmimVNIGETITITCTAI-GVPVPLITWRLNWGHVPKPPRATQTSENGR-------GVLVIRNAIETDAGAY 978
Cdd:cd20950      1 PTVNIPSS----ATIGNRAVLTCSEPdGSPPSEYTWFKDGVVMPTNPKSTRAFSNSSysldpttGELVFDPLSASDTGEY 76

                           90
                   ....*....|
gi 1351476841  979 TCEALNNKGS 988
Cdd:cd20950     77 SCEARNGYGT 86
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 911-990 7.03e-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: 37.82  E-value: 7.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351476841  911 IPPRPmIMVNIGETITITCTA---IGVPVPLITW-RLNWGHVP---------------KPPR--ATQTSENGRGVLVIRN 969
Cdd:pfam07686    1 QTPRE-VTVALGGSVTLPCTYsssMSEASTSVYWyRQPPGKGPtfliayysngseegvKKGRfsGRGDPSNGDGSLTIQN 79

                           90       100
                   ....*....|....*....|.
gi 1351476841  970 AIETDAGAYTCEALNNKGSIF 990
Cdd:pfam07686   80 LTLSDSGTYTCAVIPSGEGVF 100
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 913-987 7.15e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the 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 (Slit-1,Slit-2, Slit-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, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-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 Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 37.38  E-value: 7.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351476841  913 PRPMiMVNIGETITITCTA-IGVPVPLITWRLNwgHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEALNNKG 987
Cdd:cd05724      4 PSDT-QVAVGEMAVLECSPpRGHPEPTVSWRKD--GQPLNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVG 76
IgI_VCAM-1 cd20943
First immunoglobulin-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1), ...
 908-982 8.12e-03

First immunoglobulin-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1), and similar domains; member of the I-set of IgSF domains; The members here include the first immunoglobulin-like domain of vascular endothelial cell adhesion molecule-1 (VCAM-1; also known as Cluster of Differentiation 106 (CD106)) and similar proteins. During the inflammation process, these molecules recruit leukocytes onto the vascular endothelium before extravasation to the injured tissues. The interaction of VCAM-1 binding to the beta1 integrin very late antigen (VLA-4) expressed by lymphocytes and monocytes mediates the adhesion of leucocytes to blood vessel walls, and regulates migration across the endothelium. During metastasis, some circulating cancer cells extravasate to a secondary site by a similar process. VCAM-1 may be involved in organ targeted tumor metastasis and may also act as host receptors for viruses and parasites. VCAM-1 contains seven Ig domains. 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 first Ig-like domain of VCAM-1 is a member of the I-set 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, the A strand of the I-set is discontinuous, but lacks a C" strand.


Pssm-ID: 409536  Cd Length: 89  Bit Score: 37.26  E-value: 8.12e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1351476841  908 TVTIPPRPMIMVNIGETITITCTAIGVPVPLITWRLnwgHVPKPPRATQTSENGRGVLVIRNAIETDAGAYTCEA 982
Cdd:cd20943      2 KVEISPGSRYAAQIGDSVSLTCSTTGCESPSFSWRT---QIDSPLNGKVRNEGTTSTLTLSPVSFENEHSYLCTV 73
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 922-988 9.85e-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: 36.45  E-value: 9.85e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351476841  922 GETITITCTAIGVPVPLITWRLNWGHVPKPPRATQTSEngrGVLVIRNAIETDAGAYTCEALNNKGS 988
Cdd:cd05745      2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSS---GTLRISRVALHDQGQYECQAVNIVGS 65
 
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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