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Conserved domains on  [gi|27370250|ref|NP_766421|]
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mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MALT1_Ig pfam18703
MALT1 Ig-like domain; This is an Immunoglobulin like domain which can be found in the ...
 580-716 3.70e-79

MALT1 Ig-like domain; This is an Immunoglobulin like domain which can be found in the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase. Malt1 is a key component of the Carma1/Bcl10/MALT1 signalosome and is critical for NF-kB signaling in multiple contexts. The MALT1 C-terminal Ig domain is suggested to recruit key factors to promote NF-kB activation. The It is also proposed to undergo Lys63-linked ubiquitylation via TRAF6 in potentially nine different lysines to recruit the IKK complex.


:

Pssm-ID: 465840  Cd Length: 138  Bit Score: 251.08  E-value: 3.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   580 AHELPESMCLKFQCGVHIQLGFAAEFSNVMIIYTSIVHKPPEIIMCDAYVTDFPLDLDIDPKHANKGTPEETGSYLVSK- 658
Cdd:pfam18703   1 AHVLPESRCLDFDCGVQVQLGFAAEFSNVMVIYTTIKEKPPEIQDCTAQLTDFPEDLDMDDKFSNQGTSEEMGSLLLSKe 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27370250   659 DLPKHCLYTRLSSLQKLKEHLIFTVCLSYQYSGLEDTVEEKQEVNVGKPLIAKLDMHR 716
Cdd:pfam18703  81 DLPDCCLYTRLCSLQKLKESLVFTVCLHYTYSDMDERVTERQEVDIGKPLVAKLKLHR 138
Death_MALT1 cd08783
Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation ...
 36-132 2.16e-43

Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation gene 1; Death domain (DD) similar to that found in Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1). Malt1, together with Bcl10 (B-cell lymphoma 10), are the integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260053  Cd Length: 96  Bit Score: 151.80  E-value: 2.16e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250  36 LNRLPEPLLRRLSESLDRAPEgRGWRQLAELAGSRGRLRLSGLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDF 115
Cdd:cd08783   1 INSLQEPVLRRLCELLDQASD-KGWRKLAEAVGSDPRFKISSQELEQCSLKVLEPEGSPSRCLLKLMGERGCTLKDLTDF 79

                        90
                ....*....|....*..
gi 27370250 116 LQALEHTEVLPLLNPPG 132
Cdd:cd08783  80 LQTMGHTEALQLLKPPG 96
COG4249 COG4249
Uncharacterized conserved protein, contains caspase domain [General function prediction only];
331-554 2.35e-29

Uncharacterized conserved protein, contains caspase domain [General function prediction only];


:

Pssm-ID: 443391  Cd Length: 238  Bit Score: 116.96  E-value: 2.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 331 QTGQPLAKDKVALLIGNMSYWEHPKLKAPLVDVYELTNLLRQLDFKVVSLL-DLTEYEMCNAVDEFLLLLDKGVYGLLYY 409
Cdd:COG4249   1 AAAAAAAEKRVALVIGNSAYQDLPPLPNAVNDAEALAEALREAGFDEVILLtDATRAEIRRALRDFFAKAQPGDVALFYF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 410 AGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCR--------KRNDYDDTIPILDALKVTA 481
Cdd:COG4249  81 AGHGIQDDGENYLLPVDASPDDLESTAISLSELLDALAESPAKKVLVILDACRsgpfarggRRSAGPSSSRGLAELAAGR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370250 482 NIVFGYATCQGAEAFEiqHSGLANGIF----MKFLKDRLLEDKKITV--LLDEVAEDMGKchLTKGRQALEIRSSLSEK 554
Cdd:COG4249 161 GTLVLTASAPGQVALE--GPEGGHGVFtyalLEGLRGPADGDGGITLeeLFKYVRRRVRE--LTGGKQTPWFISSLGGD 235
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 130-200 1.70e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 69.13  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   130 PPglKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIP---------YGNSSELVFNTVHVKDAGFYVCRVNN 200
Cdd:pfam13927   1 KP--VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISsgstrsrslSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 237-303 3.90e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.50  E-value: 3.90e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370250   237 QICVEPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHY---------TVPYVDIEHEGTYWCHVYN 303
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRslsgsnstlTISNVTRSDAGTYTCVASN 78
 
Name Accession Description Interval E-value
MALT1_Ig pfam18703
MALT1 Ig-like domain; This is an Immunoglobulin like domain which can be found in the ...
 580-716 3.70e-79

MALT1 Ig-like domain; This is an Immunoglobulin like domain which can be found in the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase. Malt1 is a key component of the Carma1/Bcl10/MALT1 signalosome and is critical for NF-kB signaling in multiple contexts. The MALT1 C-terminal Ig domain is suggested to recruit key factors to promote NF-kB activation. The It is also proposed to undergo Lys63-linked ubiquitylation via TRAF6 in potentially nine different lysines to recruit the IKK complex.


Pssm-ID: 465840  Cd Length: 138  Bit Score: 251.08  E-value: 3.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   580 AHELPESMCLKFQCGVHIQLGFAAEFSNVMIIYTSIVHKPPEIIMCDAYVTDFPLDLDIDPKHANKGTPEETGSYLVSK- 658
Cdd:pfam18703   1 AHVLPESRCLDFDCGVQVQLGFAAEFSNVMVIYTTIKEKPPEIQDCTAQLTDFPEDLDMDDKFSNQGTSEEMGSLLLSKe 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27370250   659 DLPKHCLYTRLSSLQKLKEHLIFTVCLSYQYSGLEDTVEEKQEVNVGKPLIAKLDMHR 716
Cdd:pfam18703  81 DLPDCCLYTRLCSLQKLKESLVFTVCLHYTYSDMDERVTERQEVDIGKPLVAKLKLHR 138
Death_MALT1 cd08783
Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation ...
 36-132 2.16e-43

Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation gene 1; Death domain (DD) similar to that found in Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1). Malt1, together with Bcl10 (B-cell lymphoma 10), are the integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260053  Cd Length: 96  Bit Score: 151.80  E-value: 2.16e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250  36 LNRLPEPLLRRLSESLDRAPEgRGWRQLAELAGSRGRLRLSGLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDF 115
Cdd:cd08783   1 INSLQEPVLRRLCELLDQASD-KGWRKLAEAVGSDPRFKISSQELEQCSLKVLEPEGSPSRCLLKLMGERGCTLKDLTDF 79

                        90
                ....*....|....*..
gi 27370250 116 LQALEHTEVLPLLNPPG 132
Cdd:cd08783  80 LQTMGHTEALQLLKPPG 96
COG4249 COG4249
Uncharacterized conserved protein, contains caspase domain [General function prediction only];
331-554 2.35e-29

Uncharacterized conserved protein, contains caspase domain [General function prediction only];


Pssm-ID: 443391  Cd Length: 238  Bit Score: 116.96  E-value: 2.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 331 QTGQPLAKDKVALLIGNMSYWEHPKLKAPLVDVYELTNLLRQLDFKVVSLL-DLTEYEMCNAVDEFLLLLDKGVYGLLYY 409
Cdd:COG4249   1 AAAAAAAEKRVALVIGNSAYQDLPPLPNAVNDAEALAEALREAGFDEVILLtDATRAEIRRALRDFFAKAQPGDVALFYF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 410 AGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCR--------KRNDYDDTIPILDALKVTA 481
Cdd:COG4249  81 AGHGIQDDGENYLLPVDASPDDLESTAISLSELLDALAESPAKKVLVILDACRsgpfarggRRSAGPSSSRGLAELAAGR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370250 482 NIVFGYATCQGAEAFEiqHSGLANGIF----MKFLKDRLLEDKKITV--LLDEVAEDMGKchLTKGRQALEIRSSLSEK 554
Cdd:COG4249 161 GTLVLTASAPGQVALE--GPEGGHGVFtyalLEGLRGPADGDGGITLeeLFKYVRRRVRE--LTGGKQTPWFISSLGGD 235
Peptidase_C14 pfam00656
Caspase domain;
340-550 1.60e-23

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 99.32  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   340 KVALLIGNMSYWEH-PKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMCNAVDEFLLLL-----DKGVYGLLYYAGHG 413
Cdd:pfam00656   2 GLALIIGNNNYPGTkAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARAdhsdgDSFVVVLLYYSGHG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   414 YENFGN------SFMVPVDAPNpyrseNCLCVQNILKLMQEKetgLNVFLLDMCRkRNDYDDTIpildalkVTANIVFGY 487
Cdd:pfam00656  82 EQVPGGdiygtdEYLVPVDALT-----NLFTGDDCLPSLVGK---PKLFIIDACR-GNLEDGGV-------VEADFLVAY 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370250   488 ATCQGAEAFEiqhSGLANGIFMKFLKDRLLEDKK---ITVLLDEVAEDMgkCHLTKGRQALEIRSS 550
Cdd:pfam00656 146 STAPGQVSWR---NTGSGSWFIQALCQVLREYGHgldLLSLLTKVRRRV--AEATGKKQMPCLSSS 206
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 130-200 1.70e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 69.13  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   130 PPglKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIP---------YGNSSELVFNTVHVKDAGFYVCRVNN 200
Cdd:pfam13927   1 KP--VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISsgstrsrslSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 237-303 3.90e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.50  E-value: 3.90e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370250   237 QICVEPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHY---------TVPYVDIEHEGTYWCHVYN 303
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRslsgsnstlTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 150-207 1.71e-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: 1.71e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370250 150 VKLCCRATGHPFVQYQWFKMNKEIP---------YGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFS 207
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPpssrdsrrsELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 253-313 4.36e-09

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: 53.49  E-value: 4.36e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 253 LLLQCVAIGSPMPHYQWFKDESPLTHETKKHY---------TVPYVDIEHEGTYWCHVYNDRDSQDSKKA 313
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRrselgngtlTISNVTLEDSGTYTCVASNSAGGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 139-207 5.07e-09

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: 53.66  E-value: 5.07e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370250    139 PESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIP----------YGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFS 207
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 242-317 7.37e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.58  E-value: 7.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250    242 PRSQRLVPGSMLLLQCVAIGSPMPHYQWFKD------ESP---LTHETKKHY-TVPYVDIEHEGTYWCHVYNDRDsQDSK 311
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQggkllaESGrfsVSRSGSTSTlTISNVTPEDSGTYTCAATNSSG-SASS 79


                   ....*.
gi 27370250    312 KAEVTI 317
Cdd:smart00410  80 GTTLTV 85
 
Name Accession Description Interval E-value
MALT1_Ig pfam18703
MALT1 Ig-like domain; This is an Immunoglobulin like domain which can be found in the ...
 580-716 3.70e-79

MALT1 Ig-like domain; This is an Immunoglobulin like domain which can be found in the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase. Malt1 is a key component of the Carma1/Bcl10/MALT1 signalosome and is critical for NF-kB signaling in multiple contexts. The MALT1 C-terminal Ig domain is suggested to recruit key factors to promote NF-kB activation. The It is also proposed to undergo Lys63-linked ubiquitylation via TRAF6 in potentially nine different lysines to recruit the IKK complex.


Pssm-ID: 465840  Cd Length: 138  Bit Score: 251.08  E-value: 3.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   580 AHELPESMCLKFQCGVHIQLGFAAEFSNVMIIYTSIVHKPPEIIMCDAYVTDFPLDLDIDPKHANKGTPEETGSYLVSK- 658
Cdd:pfam18703   1 AHVLPESRCLDFDCGVQVQLGFAAEFSNVMVIYTTIKEKPPEIQDCTAQLTDFPEDLDMDDKFSNQGTSEEMGSLLLSKe 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27370250   659 DLPKHCLYTRLSSLQKLKEHLIFTVCLSYQYSGLEDTVEEKQEVNVGKPLIAKLDMHR 716
Cdd:pfam18703  81 DLPDCCLYTRLCSLQKLKESLVFTVCLHYTYSDMDERVTERQEVDIGKPLVAKLKLHR 138
Death_MALT1 cd08783
Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation ...
 36-132 2.16e-43

Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation gene 1; Death domain (DD) similar to that found in Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1). Malt1, together with Bcl10 (B-cell lymphoma 10), are the integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260053  Cd Length: 96  Bit Score: 151.80  E-value: 2.16e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250  36 LNRLPEPLLRRLSESLDRAPEgRGWRQLAELAGSRGRLRLSGLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDF 115
Cdd:cd08783   1 INSLQEPVLRRLCELLDQASD-KGWRKLAEAVGSDPRFKISSQELEQCSLKVLEPEGSPSRCLLKLMGERGCTLKDLTDF 79

                        90
                ....*....|....*..
gi 27370250 116 LQALEHTEVLPLLNPPG 132
Cdd:cd08783  80 LQTMGHTEALQLLKPPG 96
COG4249 COG4249
Uncharacterized conserved protein, contains caspase domain [General function prediction only];
331-554 2.35e-29

Uncharacterized conserved protein, contains caspase domain [General function prediction only];


Pssm-ID: 443391  Cd Length: 238  Bit Score: 116.96  E-value: 2.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 331 QTGQPLAKDKVALLIGNMSYWEHPKLKAPLVDVYELTNLLRQLDFKVVSLL-DLTEYEMCNAVDEFLLLLDKGVYGLLYY 409
Cdd:COG4249   1 AAAAAAAEKRVALVIGNSAYQDLPPLPNAVNDAEALAEALREAGFDEVILLtDATRAEIRRALRDFFAKAQPGDVALFYF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 410 AGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCR--------KRNDYDDTIPILDALKVTA 481
Cdd:COG4249  81 AGHGIQDDGENYLLPVDASPDDLESTAISLSELLDALAESPAKKVLVILDACRsgpfarggRRSAGPSSSRGLAELAAGR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370250 482 NIVFGYATCQGAEAFEiqHSGLANGIF----MKFLKDRLLEDKKITV--LLDEVAEDMGKchLTKGRQALEIRSSLSEK 554
Cdd:COG4249 161 GTLVLTASAPGQVALE--GPEGGHGVFtyalLEGLRGPADGDGGITLeeLFKYVRRRVRE--LTGGKQTPWFISSLGGD 235
Peptidase_C14 pfam00656
Caspase domain;
340-550 1.60e-23

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 99.32  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   340 KVALLIGNMSYWEH-PKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMCNAVDEFLLLL-----DKGVYGLLYYAGHG 413
Cdd:pfam00656   2 GLALIIGNNNYPGTkAPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARAdhsdgDSFVVVLLYYSGHG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   414 YENFGN------SFMVPVDAPNpyrseNCLCVQNILKLMQEKetgLNVFLLDMCRkRNDYDDTIpildalkVTANIVFGY 487
Cdd:pfam00656  82 EQVPGGdiygtdEYLVPVDALT-----NLFTGDDCLPSLVGK---PKLFIIDACR-GNLEDGGV-------VEADFLVAY 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370250   488 ATCQGAEAFEiqhSGLANGIFMKFLKDRLLEDKK---ITVLLDEVAEDMgkCHLTKGRQALEIRSS 550
Cdd:pfam00656 146 STAPGQVSWR---NTGSGSWFIQALCQVLREYGHgldLLSLLTKVRRRV--AEATGKKQMPCLSSS 206
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 130-200 1.70e-14

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 69.13  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   130 PPglKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIP---------YGNSSELVFNTVHVKDAGFYVCRVNN 200
Cdd:pfam13927   1 KP--VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISsgstrsrslSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 237-303 3.90e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.50  E-value: 3.90e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370250   237 QICVEPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHY---------TVPYVDIEHEGTYWCHVYN 303
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRslsgsnstlTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 150-207 1.71e-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: 1.71e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370250 150 VKLCCRATGHPFVQYQWFKMNKEIP---------YGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFS 207
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPpssrdsrrsELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 253-313 4.36e-09

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: 53.49  E-value: 4.36e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 253 LLLQCVAIGSPMPHYQWFKDESPLTHETKKHY---------TVPYVDIEHEGTYWCHVYNDRDSQDSKKA 313
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRrselgngtlTISNVTLEDSGTYTCVASNSAGGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 139-207 5.07e-09

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: 53.66  E-value: 5.07e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370250    139 PESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIP----------YGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFS 207
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 236-307 8.20e-09

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: 53.30  E-value: 8.20e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370250 236 LQICVEPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHYT------VPYVDIEHEGTYWCHVYNDRDS 307
Cdd:cd20957   2 LSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILsedvlvIPSVKREDKGMYQCFVRNDGDS 79
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 241-317 2.30e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 51.63  E-value: 2.30e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370250   241 EPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLthETKKHYTVPYVDIEHEGTYWCHVYNDRDSQDSKKAEVTI 317
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAI--SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPVELTV 79
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 250-303 2.86e-08

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: 51.78  E-value: 2.86e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370250 250 GSMLLLQCVAIGSPMPHYQWFKDESPLTHET-----KKHYTVPYVDI--EHEGTYWCHVYN 303
Cdd:cd05856  19 GSSVRLKCVASGNPRPDITWLKDNKPLTPPEigenkKKKWTLSLKNLkpEDSGKYTCHVSN 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 242-317 7.37e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.58  E-value: 7.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250    242 PRSQRLVPGSMLLLQCVAIGSPMPHYQWFKD------ESP---LTHETKKHY-TVPYVDIEHEGTYWCHVYNDRDsQDSK 311
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQggkllaESGrfsVSRSGSTSTlTISNVTPEDSGTYTCAATNSSG-SASS 79


                   ....*.
gi 27370250    312 KAEVTI 317
Cdd:smart00410  80 GTTLTV 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 134-207 8.04e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 50.09  E-value: 8.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370250   134 KITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPygNSSELVFNTVHVKDAGFYVCRVNNSSTFEFS 207
Cdd:pfam13895   1 KPVLTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAIS--SSPNFFTLSVSAEDSGTYTCVARNGRGGKVS 72
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 131-200 1.24e-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: 50.20  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 131 PGLKITVNPESKAvlaGQFVKLCCRATG-HPFVQYQWFKMNKE--------IPYGN---SSELVFNTVHVKDAGFYVCRV 198
Cdd:cd05750   1 PKLKEMKSQTVQE---GSKLVLKCEATSeNPSPRYRWFKDGKElnrkrpknIKIRNkkkNSELQINKAKLEDSGEYTCVV 77


                ..
gi 27370250 199 NN 200
Cdd:cd05750  78 EN 79
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 144-202 1.75e-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: 49.50  E-value: 1.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   144 VLAGQFVKLCCRA-TGHPFVQYQWFKMNKEIP----------YGNSSELVFNTVHVKDAGFYVCRVNNSS 202
Cdd:pfam00047   8 VLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIeslkvkhdngRTTQSSLLISNVTKEDAGTYTCVVNNPG 77
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 242-279 1.96e-07

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: 49.13  E-value: 1.96e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 27370250 242 PRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHE 279
Cdd:cd05739   4 PSNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKE 41
I-set pfam07679
Immunoglobulin I-set domain;
242-317 2.97e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   242 PRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLT-------HETKKHYT--VPYVDIEHEGTYWCHVYNdRDSQDSKK 312
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssdrfkvTYEGGTYTltISNVQPDDSGKYTCVATN-SAGEAEAS 85


                  ....*
gi 27370250   313 AEVTI 317
Cdd:pfam07679  86 AELTV 90
Death_IRAK cd08309
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ...
 36-121 1.89e-06

Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260023  Cd Length: 88  Bit Score: 46.57  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250  36 LNRLPEPLLRRLSESLDrAPEGRGWRQLAELagsrgrLRLSGLDLEQCSlKVLEPEGSPSLCLLKLMGEKGCTVTELSDF 115
Cdd:cd08309   3 IRNLPPWVLKRLCKVLD-ALELAGWRQLASL------IPYDQTDVRQIE-SMKQRGQSPTRELLWDWGTQNATVQDLVQL 74


                ....*.
gi 27370250 116 LQALEH 121
Cdd:cd08309  75 LTQLGL 80
I-set pfam07679
Immunoglobulin I-set domain;
134-202 2.84e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 46.10  E-value: 2.84e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370250   134 KITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPY---------GNSSELVFNTVHVKDAGFYVCRVNNSS 202
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSsdrfkvtyeGGTYTLTISNVQPDDSGKYTCVATNSA 79
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 240-317 3.07e-06

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: 45.85  E-value: 3.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 240 VEPRSQRLVPGSMLLLQCVA-IGSPMPHYQWFKDESPLTHETKKHYTV-------PYVDIEHEGTYWCHVYNDRDSQDSK 311
Cdd:cd05724   2 VEPSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVddgnlliAEARKSDEGTYKCVATNMVGERESR 81


                ....*.
gi 27370250 312 KAEVTI 317
Cdd:cd05724  82 AARLSV 87
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 135-200 4.19e-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: 45.72  E-value: 4.19e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370250 135 ITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPY---------GNSSELVFNTVHVKDAGFYVCRVNN 200
Cdd:cd05736   3 IRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPklskqltliANGSELHISNVRYEDTGAYTCIAKN 77
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 244-304 5.30e-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: 45.63  E-value: 5.30e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370250 244 SQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPL---------THETKKHYTVPYVDI-----EHEGTYWCHVYND 304
Cdd:cd20956  10 EQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIpesprfrvgDYVTSDGDVVSYVNIssvrvEDGGEYTCTATND 84
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 238-306 6.70e-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: 45.33  E-value: 6.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 238 ICVEPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHYT---------VPYVDIEHEGTYWCHVYN----D 304
Cdd:cd05736   3 IRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTliangselhISNVRYEDTGAYTCIAKNeggvD 82


                ..
gi 27370250 305 RD 306
Cdd:cd05736  83 ED 84
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 250-317 9.94e-06

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: 44.46  E-value: 9.94e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27370250 250 GSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHYT-----VPYVDIEHEGTYWCHVYNDRdSQDSKKAEVTI 317
Cdd:cd04968  16 GQTVTLECFALGNPVPQIKWRKVDGSPSSQWEITTSepvleIPNVQFEDEGTYECEAENSR-GKDTVQGRIIV 87
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 144-201 2.43e-05

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: 43.32  E-value: 2.43e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370250 144 VLAGQFVKLCCRATGHPFVQYQWFKMNKEIPYG-------NSSELVFNTVHVKDAGFYVCRVNNS 201
Cdd:cd20958  12 AVAGQTLRLHCPVAGYPISSITWEKDGRRLPLNhrqrvfpNGTLVIENVQRSSDEGEYTCTARNQ 76
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 130-201 2.58e-05

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: 43.46  E-value: 2.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 130 PPglKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIP--------------YGNSSeLVFNTVHVKDAGFYV 195
Cdd:cd20954   1 PP--RWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKATGSTPgeykdllydpnvriLPNGT-LVFGHVQKENEGHYL 77


                ....*.
gi 27370250 196 CRVNNS 201
Cdd:cd20954  78 CEAKNG 83
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 45-125 5.59e-05

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260026  Cd Length: 79  Bit Score: 42.20  E-value: 5.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250  45 RRLSESLD-RAPEGRGWRQLAELAGsrgrlrlsgldLEQCSLKVLEPEGSPSLCLLKL--MGEKGCTVTELSDFLQALEH 121
Cdd:cd08312   3 KKLSLYLNpEKVVANDWRGLAELMG-----------FDYLEIRNFERQSSPTERLLEDweTRPPGATVGNLLEILEELER 71


                ....
gi 27370250 122 TEVL 125
Cdd:cd08312  72 KDVL 75
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 238-299 7.38e-05

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: 42.10  E-value: 7.38e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370250 238 ICVEPRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKHYTVP-------YVDIEHEGTYWC 299
Cdd:cd20952   2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLEngslqikGAEKSDTGEYTC 70
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 240-313 7.57e-05

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: 42.18  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250   240 VEPRSQRLVPGSMLLLQC-VAIGSPMPHYQWFKD--ESPLTHETKKHY--------TVPYVDIEHEGTYWChVYNDRDSQ 308
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCsASTGSPGPDVTWSKEggTLIESLKVKHDNgrttqsslLISNVTKEDAGTYTC-VVNNPGGS 79


                  ....*
gi 27370250   309 DSKKA 313
Cdd:pfam00047  80 ATLST 84
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
 140-200 9.93e-05

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


Pssm-ID: 409476  Cd Length: 93  Bit Score: 41.90  E-value: 9.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370250 140 ESKAVLAGQFVKLCCRATG-HPFVQYQWFKMNKEIPYGN------------SSELVFNTVHVKDAGFYVCRVNN 200
Cdd:cd05895   7 KSQEVAAGSKLVLRCETSSeYPSLRFKWFKNGKEINRKNkpenikiqkkkkKSELRINKASLADSGEYMCKVSS 80
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 136-200 1.01e-04

First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-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: 409436 [Multi-domain]  Cd Length: 95  Bit Score: 41.86  E-value: 1.01e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27370250 136 TVNPESKavLAGQfVKLCCRATGHPFVQYQWFKMNKEIPYGNS------SELVFNTV-HVKDAGFYVCRVNN 200
Cdd:cd05849  11 TIYPEES--TEGK-VSVNCRARANPFPIYKWRKNNLDIDLTNDrysmvgGNLVINNPdKYKDAGRYVCIVSN 79
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 241-303 1.17e-04

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: 41.82  E-value: 1.17e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370250 241 EPRSQRLVP---GSMLLLQCVAIGSPMPHYQWFKDESPLTHET--------KKHYT--VPYVDIEHEGTYWCHVYN 303
Cdd:cd05729   7 EKMEEREHAlpaANKVRLECGAGGNPMPNITWLKDGKEFKKEHriggtkveEKGWSliIERAIPRDKGKYTCIVEN 82
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 150-201 1.49e-04

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: 41.46  E-value: 1.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 150 VKLCCRATGHPFVQYQWFKMNKEIPYGNSSE--------LVFNTVHVKDAGFYVCRVNNS 201
Cdd:cd04967  22 VALNCRARANPVPSYRWLMNGTEIDLESDYRyslvdgtlVISNPSKAKDAGHYQCLATNT 81
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 241-317 1.52e-04

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: 41.34  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 241 EPRSQRLVPGSMLLLQCVAIG-SPMPHYQWFKDESPLTHETKKHYTVP-----------YVDIEHEGTYWCHVYNdRDSQ 308
Cdd:cd05750   5 EMKSQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPKNIKIRnkkknselqinKAKLEDSGEYTCVVEN-ILGK 83


                ....*....
gi 27370250 309 DSKKAEVTI 317
Cdd:cd05750  84 DTVTGNVTV 92
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
 136-200 1.99e-04

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The second Ig-like domain of JAM1 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, the A strand of the I-set is discontinuous but lacks a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409542  Cd Length: 97  Bit Score: 41.15  E-value: 1.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 136 TVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIP--------YGNSS--------ELVFNTVHVKDAGFYVCRVN 199
Cdd:cd20950   2 TVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVMPtnpkstraFSNSSysldpttgELVFDPLSASDTGEYSCEAR 81


                .
gi 27370250 200 N 200
Cdd:cd20950  82 N 82
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 250-316 2.05e-04

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. 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' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 40.56  E-value: 2.05e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370250 250 GSMLLLQCVAIGSPMPHYQWFKDESPLTHETKkhYTVPYVDIEHEGTYWCHVYNDRDSQDSKKAEVT 316
Cdd:cd20948  10 GENLNLSCHAASNPPAQYSWTINGTFQTSSQE--LFLPAITENNEGTYTCSAHNSLTGKNISLVLSV 74
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
 130-201 3.43e-04

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 40.71  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 130 PPglKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPYG---------NSSELVFNTVHVKDAGFYVCRVNN 200
Cdd:cd05762   1 PP--QIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQIQEGegikienteNSSKLTITEGQQEHCGCYTLEVEN 78


                .
gi 27370250 201 S 201
Cdd:cd05762  79 K 79
IgC_CRIg cd16082
Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin ...
 144-197 3.60e-04

Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4)) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. 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 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.


Pssm-ID: 409504  Cd Length: 86  Bit Score: 40.12  E-value: 3.60e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27370250 144 VLAGQFVKLCCRATGHPFVQYQWFKM---NKE-IPYGNSSELVFNTVHVKDAGFYVCR 197
Cdd:cd16082  10 VPQGMRISLQCQAWGSPPISYVWYKEqtnNQEpIKVAALSTLLFKPAVVADSGSYFCT 67
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 135-202 4.75e-04

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: 39.84  E-value: 4.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 135 ITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFK---------MNKEIPYGNS-----SELVFNTVHVKDAGFYVCRVNN 200
Cdd:cd05765   3 LVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvpgkenliMRPNHVRGNVvvtniGQLVIYNAQPQDAGLYTCTARN 82


                ..
gi 27370250 201 SS 202
Cdd:cd05765  83 SG 84
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 242-317 6.69e-04

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


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 39.54  E-value: 6.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 242 PRSQRLVPGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKK--------HYTVPYVDIEHEGTYWCHVYNdRDSQDSKKA 313
Cdd:cd20976   8 PKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRstceagvgELHIQDVLPEDHGTYTCLAKN-AAGQVSCSA 86


                ....
gi 27370250 314 EVTI 317
Cdd:cd20976  87 WVTV 90
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 249-303 7.37e-04

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 409417  Cd Length: 95  Bit Score: 39.53  E-value: 7.37e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27370250 249 PGSMLLLQCVAIGSPMPHYQWFKDESPLTHETKKH--------YTVPYVDIEHEGTYWCHVYN 303
Cdd:cd05760  15 PSSRVTLRCHIDGHPRPTYQWFRDGTPLSDGQGNYsvsskertLTLRSAGPDDSGLYYCCAHN 77
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 128-202 9.47e-04

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.


Pssm-ID: 409418  Cd Length: 102  Bit Score: 39.33  E-value: 9.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 128 LNPPGlKITVNPESKAVLAGQFVKLCCRATG-HPFVQYQWFKMNKEI---PYGN----------SSELVFNtVHVKDAG- 192
Cdd:cd05761   1 LGVPE-KPVITGFTSPVVEGDEITLTCTTSGsKPAADIRWFKNDKELkgvKEVQesgagktftvTSTLRFR-VDRDDDGv 78

                        90
                ....*....|
gi 27370250 193 FYVCRVNNSS 202
Cdd:cd05761  79 AVICRVDHES 88
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 142-200 1.09e-03

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


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 39.13  E-value: 1.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370250 142 KAVLAGQFVKLCCRATGHPFVQYQWFKMNKEI-------PYGNSSE---LVFNTVHVKDAGFYVCRVNN 200
Cdd:cd05729  14 HALPAANKVRLECGAGGNPMPNITWLKDGKEFkkehrigGTKVEEKgwsLIIERAIPRDKGKYTCIVEN 82
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 138-214 1.10e-03

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


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 39.03  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 138 NPESKAVLAGQFVKLCCRATGHPFVQYQWFK--------MNKEIPYGNSSELVFNTVHVKDAGFYVCRVNNSSTFEFSQW 209
Cdd:cd20970   8 PSFTVTAREGENATFMCRAEGSPEPEISWTRngnliiefNTRYIVRENGTTLTIRNIRRSDMGIYLCIASNGVPGSVEKR 87


                ....*
gi 27370250 210 SQLDV 214
Cdd:cd20970  88 ITLQV 92
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 133-200 1.11e-03

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: 38.67  E-value: 1.11e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370250 133 LKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPygNSSE---LVFNTVHVK-----DAGFYVCRVNN 200
Cdd:cd20957   2 LSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLG--HSSRvqiLSEDVLVIPsvkreDKGMYQCFVRN 75
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 133-201 1.30e-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: 38.56  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 133 LKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEI------------PYGNSSELVFNTVHVKDAGFYVCRVNN 200
Cdd:cd20951   1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpssipgkykieSEYGVHVLHIRRVTVEDSAVYSAVAKN 80


                .
gi 27370250 201 S 201
Cdd:cd20951  81 I 81
Ig0_BSG1 cd20940
Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are ...
 242-313 1.35e-03

Immunoglobulin-like Ig0 domain of basigin-1 (BSG1) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of the collagenase stimulatory factor, basigin-1 (BSG1; also known as Cluster of Differentiation 147 (CD147) and Extracellular Matrix Metalloproteinase Inducer (EMMPRIN)) and similar proteins. CD147 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed in nearly all cells including platelets and fibroblasts and is involved in inflammatory diseases, and cancer progression. CD147 is highly expressed in several cancers and used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified: CD147 Ig1-Ig2 (also called Basigin-2) that is ubiquitously expressed in most tissues and CD147 Ig0-Ig1-Ig2 (also called Basigin-1) that is retinal specific and implicated in retinoblastoma. Studies showed that CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 dimer is the functional unit required for activity.


Pssm-ID: 409534  Cd Length: 116  Bit Score: 39.18  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 242 PRSQRLVPGSMLLLQCVAIGSPMPHYQ-WFKDESPL---------THETKKHYTVPYVD------------IEHEGTYWC 299
Cdd:cd20940   7 PLSQQRLVGDSVELHCEAVGSPIPEIQwWFEGQEPNeicsqlwdgARLDRVHINATYHQhatstisidnltEEDTGTYEC 86

                        90
                ....*....|....
gi 27370250 300 HVYNDRDSQDSKKA 313
Cdd:cd20940  87 RASNDPDRNHLTRA 100
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 139-214 1.50e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 38.63  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 139 PESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPY----------GNSSELVFNTVHVKDAGFYVC-RVNNSSTFEFS 207
Cdd:cd05744   7 PGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPdsahkmlvreNGRHSLIIEPVTKRDAGIYTCiARNRAGENSFN 86


                ....*..
gi 27370250 208 qwSQLDV 214
Cdd:cd05744  87 --AELVV 91
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
 135-214 1.58e-03

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


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 38.53  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250 135 ITVNpESKAVLAGQFVKLCCRATGHPfVQYQWFKMNKEIPYG-------NSSELVFNTVHVKDAGFYVCRVNNSSTFEFS 207
Cdd:cd05740   4 ISSN-NSNPVEDKDAVTLTCEPETQN-TSYLWWFNGQSLPVTprltlsnGNRTLTLLNVTREDAGAYQCEISNPVSANRS 81


                ....*..
gi 27370250 208 QWSQLDV 214
Cdd:cd05740  82 DPVTLDV 88
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 46-129 5.33e-03

Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear Factor-KappaB (NF-kB) precursor proteins. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). Two of these, NF-kB1 and NF-kB2 are produced from the processing of the precursor proteins p105 and p100, respectively. In addition to RHD, p105 and p100 contain ANK repeats and a C-terminal DD. NF-kBs are regulated by the Inhibitor of NF-kB (IkB) Kinase (IKK) complex through classical and non-canonical pathways, which differ in the IKK subunits involved and downstream targets. IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. The precursor proteins p105 and p100 function as IkBs and as NF-kB proteins after being processed by the proteasome. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260024  Cd Length: 72  Bit Score: 36.45  E-value: 5.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250  46 RLSESLDRapeGRGWRQLAELagsrgrLRLSGLD--LEQCSlkvlepegSPSLCLLKLMGEKGCTVTELSDFLQALEHTE 123
Cdd:cd08310   4 RLCKLLDV---GKDWRELAEL------LGLGHLVesIEQSS--------SPTKLLLDYYEAQGGTLEKLREALRALGETD 66


                ....*.
gi 27370250 124 VLPLLN 129
Cdd:cd08310  67 AVELID 72
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 139-201 6.56e-03

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: 36.60  E-value: 6.56e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370250 139 PESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPYGNSSELVFNTVHVK-----DAGFYVCRVNNS 201
Cdd:cd05725   4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGRYEILDDHSLKIRkvtagDMGSYTCVAENM 71
Death_Pelle cd08307
Death domain of the protein kinase Pelle; Death domain (DD) of the protein kinase Pelle from ...
 39-130 9.27e-03

Death domain of the protein kinase Pelle; Death domain (DD) of the protein kinase Pelle from Drosophila melanogaster and similar proteins. In Drosophila, interaction between the DDs of Tube and Pelle is an important component of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and in mediating innate immune responses to pathogens. Tube and Pelle transmit the signal from the Toll receptor to the Dorsal/Cactus complex. Pelle also functions in photoreceptor axon targeting. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260021  Cd Length: 97  Bit Score: 36.50  E-value: 9.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370250  39 LPEPLLRRLSESLDrapEGRGWRQLAELagsrgRLRLSGLDLEQCSLKVLEPEgSPSLCLLKLMGEKGCTVTELSDFLQA 118
Cdd:cd08307   6 LPFTERKQLCALLD---QDNKWEELAGV-----MMGYDPDDVEGIRRCCLRGR-SPTEELLTKWGNKNHTITELFVLLYR 76

                        90
                ....*....|..
gi 27370250 119 LEHTEVLPLLNP 130
Cdd:cd08307  77 MKLYRAMRILKD 88
 
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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