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Conserved domains on  [gi|528515868|ref|XP_005161758|]
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MALT paracaspase 2 isoform X1 [Danio rerio]

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 ...
559-699 3.52e-73

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: 234.91  E-value: 3.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  559 AHVLPESRCLQFECGVTVQLGFAAEFSNIMIIYTQILETPTDIVSCSAQLSDFTEGPEVDLKRSNQESLHEAESFLLTID 638
Cdd:pfam18703   1 AHVLPESRCLDFDCGVQVQLGFAAEFSNVMVIYTTIKEKPPEIQDCTAQLTDFPEDLDMDDKFSNQGTSEEMGSLLLSKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528515868  639 DLLplkQPQLFTRISALQRLKKELSFTVCLHYKYGNLDEELLEEKRITVGKPLVSKLNLHE 699
Cdd:pfam18703  81 DLP---DCCLYTRLCSLQKLKESLVFTVCLHYTYSDMDERVTERQEVDIGKPLVAKLKLHR 138
Death_MALT1 cd08783
Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation ...
8-102 3.14e-45

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: 157.19  E-value: 3.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868   8 LENISEAALSRLGYMLDNA-ECGWKQLAKAVAEQPQFCYSDREMTDCSLKVLSPHGSPGRYLLALLADRGCTLAFLLQCL 86
Cdd:cd08783    1 INSLQEPVLRRLCELLDQAsDKGWRKLAEAVGSDPRFKISSQELEQCSLKVLEPEGSPSRCLLKLMGERGCTLKDLTDFL 80
                         90
                 ....*....|....*.
gi 528515868  87 KKIEHREAVGFLTMNV 102
Cdd:cd08783   81 QTMGHTEALQLLKPPG 96
Peptidase_C14 pfam00656
Caspase domain;
319-522 2.71e-29

Caspase domain;


:

Pssm-ID: 425803  Cd Length: 213  Bit Score: 115.88  E-value: 2.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  319 KVALLIGNMNYLHHR-QLRAPMADVHELTNLLRQLDFKVVSLLDLNWQEMHSAVTEFLLLL-----DRGVYGLLYFAGHG 392
Cdd:pfam00656   2 GLALIIGNNNYPGTKaPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARAdhsdgDSFVVVLLYYSGHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  393 YENYGN------SFMVPIDAPasytfKHCLWVQEVLQRMQERQTglnVFLLDMCRKRnpndegipQPDPLRVTANIVFGY 466
Cdd:pfam00656  82 EQVPGGdiygtdEYLVPVDAL-----TNLFTGDDCLPSLVGKPK---LFIIDACRGN--------LEDGGVVEADFLVAY 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528515868  467 ATCVDAEAFEvnkDDLSNGIFMSFLKKRLMEPEK---VTVILDKVAEDMgrCEITRGRQ 522
Cdd:pfam00656 146 STAPGQVSWR---NTGSGSWFIQALCQVLREYGHgldLLSLLTKVRRRV--AEATGKKQ 199
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
207-272 3.42e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 3.42e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528515868  207 ITQQPRPQALMEGDTLCLECSAQANPPPQFQWYFN-KELMPKCIRNF--------LKIPCITTADRGIYACRVYN 272
Cdd:pfam13927   4 ITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNgEPISSGSTRSRslsgsnstLTISNVTRSDAGTYTCVASN 78
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
111-172 1.38e-09

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


:

Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 55.09  E-value: 1.38e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528515868  111 QPQSQRIAEGSPVVLSCKAVGPVELQYQWFkgKDEMPEGNSPDLVFNRASPAQQGYYICRVS 172
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWY--KDGSAISSSPNFFTLSVSAEDSGTYTCVAR 64
 
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 ...
559-699 3.52e-73

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: 234.91  E-value: 3.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  559 AHVLPESRCLQFECGVTVQLGFAAEFSNIMIIYTQILETPTDIVSCSAQLSDFTEGPEVDLKRSNQESLHEAESFLLTID 638
Cdd:pfam18703   1 AHVLPESRCLDFDCGVQVQLGFAAEFSNVMVIYTTIKEKPPEIQDCTAQLTDFPEDLDMDDKFSNQGTSEEMGSLLLSKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528515868  639 DLLplkQPQLFTRISALQRLKKELSFTVCLHYKYGNLDEELLEEKRITVGKPLVSKLNLHE 699
Cdd:pfam18703  81 DLP---DCCLYTRLCSLQKLKESLVFTVCLHYTYSDMDERVTERQEVDIGKPLVAKLKLHR 138
Death_MALT1 cd08783
Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation ...
8-102 3.14e-45

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: 157.19  E-value: 3.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868   8 LENISEAALSRLGYMLDNA-ECGWKQLAKAVAEQPQFCYSDREMTDCSLKVLSPHGSPGRYLLALLADRGCTLAFLLQCL 86
Cdd:cd08783    1 INSLQEPVLRRLCELLDQAsDKGWRKLAEAVGSDPRFKISSQELEQCSLKVLEPEGSPSRCLLKLMGERGCTLKDLTDFL 80
                         90
                 ....*....|....*.
gi 528515868  87 KKIEHREAVGFLTMNV 102
Cdd:cd08783   81 QTMGHTEALQLLKPPG 96
Peptidase_C14 pfam00656
Caspase domain;
319-522 2.71e-29

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 115.88  E-value: 2.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  319 KVALLIGNMNYLHHR-QLRAPMADVHELTNLLRQLDFKVVSLLDLNWQEMHSAVTEFLLLL-----DRGVYGLLYFAGHG 392
Cdd:pfam00656   2 GLALIIGNNNYPGTKaPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARAdhsdgDSFVVVLLYYSGHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  393 YENYGN------SFMVPIDAPasytfKHCLWVQEVLQRMQERQTglnVFLLDMCRKRnpndegipQPDPLRVTANIVFGY 466
Cdd:pfam00656  82 EQVPGGdiygtdEYLVPVDAL-----TNLFTGDDCLPSLVGKPK---LFIIDACRGN--------LEDGGVVEADFLVAY 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528515868  467 ATCVDAEAFEvnkDDLSNGIFMSFLKKRLMEPEK---VTVILDKVAEDMgrCEITRGRQ 522
Cdd:pfam00656 146 STAPGQVSWR---NTGSGSWFIQALCQVLREYGHgldLLSLLTKVRRRV--AEATGKKQ 199
COG4249 COG4249
Uncharacterized conserved protein, contains caspase domain [General function prediction only];
316-522 4.08e-27

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


Pssm-ID: 443391  Cd Length: 238  Bit Score: 110.41  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 316 ATDKVALLIGNMNYLHHRQLRAPMADVHELTNLLRQLDFKVVSLL-DLNWQEMHSAVTEFLLLLDRGVYGLLYFAGHGYE 394
Cdd:COG4249    7 AEKRVALVIGNSAYQDLPPLPNAVNDAEALAEALREAGFDEVILLtDATRAEIRRALRDFFAKAQPGDVALFYFAGHGIQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 395 NYGNSFMVPIDAPASYTFKHCLWVQEVLQRMQERQTGLNVFLLDMCR--------KRNPNDEGIPQPDPLRVTANIVFGY 466
Cdd:COG4249   87 DDGENYLLPVDASPDDLESTAISLSELLDALAESPAKKVLVILDACRsgpfarggRRSAGPSSSRGLAELAAGRGTLVLT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528515868 467 ATCVDAEAFEVnkDDLSNGIFMSFLKKRLMEP----EKVTV--ILDKVAEDMGrcEITRGRQ 522
Cdd:COG4249  167 ASAPGQVALEG--PEGGHGVFTYALLEGLRGPadgdGGITLeeLFKYVRRRVR--ELTGGKQ 224
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
207-272 3.42e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 3.42e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528515868  207 ITQQPRPQALMEGDTLCLECSAQANPPPQFQWYFN-KELMPKCIRNF--------LKIPCITTADRGIYACRVYN 272
Cdd:pfam13927   4 ITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNgEPISSGSTRSRslsgsnstLTISNVTRSDAGTYTCVASN 78
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
111-172 1.38e-09

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 55.09  E-value: 1.38e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528515868  111 QPQSQRIAEGSPVVLSCKAVGPVELQYQWFkgKDEMPEGNSPDLVFNRASPAQQGYYICRVS 172
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWY--KDGSAISSSPNFFTLSVSAEDSGTYTCVAR 64
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
112-181 2.43e-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: 54.82  E-value: 2.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868   112 PQSQRIAEGSPVVLSCKAVGPVELQYQWFKGKDEMP----------EGNSPDLVFNRASPAQQGYYICRVSSGDKYIFSN 181
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
109-173 1.14e-08

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: 53.07  E-value: 1.14e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528515868 109 IQQPQSQRIAEGSPVVLSCKAVGPV-ELQYQWFKGKDEMPEGNSP------------DLVFNRASPAQQGYYICRVSS 173
Cdd:cd05895    3 LKEMKSQEVAAGSKLVLRCETSSEYpSLRFKWFKNGKEINRKNKPenikiqkkkkksELRINKASLADSGEYMCKVSS 80
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
211-275 2.49e-08

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: 51.34  E-value: 2.49e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528515868 211 PRPQALMEGDTLCLECSAQANPPPQFQWYFNkeLMPKCIRNFLKIPCITTADRGIYACRVYNLYH 275
Cdd:cd20948    2 PSDTYYLSGENLNLSCHAASNPPAQYSWTIN--GTFQTSSQELFLPAITENNEGTYTCSAHNSLT 64
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
211-284 4.87e-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: 50.97  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868   211 PRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMPKCIRNF----------LKIPCITTADRGIYACRVYNLYHEMWSD 280
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFsvsrsgststLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 528515868   281 -QVQV 284
Cdd:smart00410  81 tTLTV 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 ...
559-699 3.52e-73

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: 234.91  E-value: 3.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  559 AHVLPESRCLQFECGVTVQLGFAAEFSNIMIIYTQILETPTDIVSCSAQLSDFTEGPEVDLKRSNQESLHEAESFLLTID 638
Cdd:pfam18703   1 AHVLPESRCLDFDCGVQVQLGFAAEFSNVMVIYTTIKEKPPEIQDCTAQLTDFPEDLDMDDKFSNQGTSEEMGSLLLSKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528515868  639 DLLplkQPQLFTRISALQRLKKELSFTVCLHYKYGNLDEELLEEKRITVGKPLVSKLNLHE 699
Cdd:pfam18703  81 DLP---DCCLYTRLCSLQKLKESLVFTVCLHYTYSDMDERVTERQEVDIGKPLVAKLKLHR 138
Death_MALT1 cd08783
Death domain similar to that found in Mucosa-associated lymphoid tissue-lymphoma-translocation ...
8-102 3.14e-45

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: 157.19  E-value: 3.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868   8 LENISEAALSRLGYMLDNA-ECGWKQLAKAVAEQPQFCYSDREMTDCSLKVLSPHGSPGRYLLALLADRGCTLAFLLQCL 86
Cdd:cd08783    1 INSLQEPVLRRLCELLDQAsDKGWRKLAEAVGSDPRFKISSQELEQCSLKVLEPEGSPSRCLLKLMGERGCTLKDLTDFL 80
                         90
                 ....*....|....*.
gi 528515868  87 KKIEHREAVGFLTMNV 102
Cdd:cd08783   81 QTMGHTEALQLLKPPG 96
Peptidase_C14 pfam00656
Caspase domain;
319-522 2.71e-29

Caspase domain;


Pssm-ID: 425803  Cd Length: 213  Bit Score: 115.88  E-value: 2.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  319 KVALLIGNMNYLHHR-QLRAPMADVHELTNLLRQLDFKVVSLLDLNWQEMHSAVTEFLLLL-----DRGVYGLLYFAGHG 392
Cdd:pfam00656   2 GLALIIGNNNYPGTKaPLRGCDNDAEALAKTLKSLGFEVRVFEDLTAEEIRRALRDFAARAdhsdgDSFVVVLLYYSGHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  393 YENYGN------SFMVPIDAPasytfKHCLWVQEVLQRMQERQTglnVFLLDMCRKRnpndegipQPDPLRVTANIVFGY 466
Cdd:pfam00656  82 EQVPGGdiygtdEYLVPVDAL-----TNLFTGDDCLPSLVGKPK---LFIIDACRGN--------LEDGGVVEADFLVAY 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528515868  467 ATCVDAEAFEvnkDDLSNGIFMSFLKKRLMEPEK---VTVILDKVAEDMgrCEITRGRQ 522
Cdd:pfam00656 146 STAPGQVSWR---NTGSGSWFIQALCQVLREYGHgldLLSLLTKVRRRV--AEATGKKQ 199
COG4249 COG4249
Uncharacterized conserved protein, contains caspase domain [General function prediction only];
316-522 4.08e-27

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


Pssm-ID: 443391  Cd Length: 238  Bit Score: 110.41  E-value: 4.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 316 ATDKVALLIGNMNYLHHRQLRAPMADVHELTNLLRQLDFKVVSLL-DLNWQEMHSAVTEFLLLLDRGVYGLLYFAGHGYE 394
Cdd:COG4249    7 AEKRVALVIGNSAYQDLPPLPNAVNDAEALAEALREAGFDEVILLtDATRAEIRRALRDFFAKAQPGDVALFYFAGHGIQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 395 NYGNSFMVPIDAPASYTFKHCLWVQEVLQRMQERQTGLNVFLLDMCR--------KRNPNDEGIPQPDPLRVTANIVFGY 466
Cdd:COG4249   87 DDGENYLLPVDASPDDLESTAISLSELLDALAESPAKKVLVILDACRsgpfarggRRSAGPSSSRGLAELAAGRGTLVLT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528515868 467 ATCVDAEAFEVnkDDLSNGIFMSFLKKRLMEP----EKVTV--ILDKVAEDMGrcEITRGRQ 522
Cdd:COG4249  167 ASAPGQVALEG--PEGGHGVFTYALLEGLRGPadgdGGITLeeLFKYVRRRVR--ELTGGKQ 224
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
207-272 3.42e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 62.58  E-value: 3.42e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528515868  207 ITQQPRPQALMEGDTLCLECSAQANPPPQFQWYFN-KELMPKCIRNF--------LKIPCITTADRGIYACRVYN 272
Cdd:pfam13927   4 ITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNgEPISSGSTRSRslsgsnstLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
207-284 1.17e-10

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 58.42  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868  207 ITQQPRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMP-------KCIRN--FLKIPCITTADRGIYACRVYNLYHEM 277
Cdd:pfam07679   3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssdrfkvTYEGGtyTLTISNVQPDDSGKYTCVATNSAGEA 82

                  ....*...
gi 528515868  278 WSD-QVQV 284
Cdd:pfam07679  83 EASaELTV 90
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
111-172 1.38e-09

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 55.09  E-value: 1.38e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528515868  111 QPQSQRIAEGSPVVLSCKAVGPVELQYQWFkgKDEMPEGNSPDLVFNRASPAQQGYYICRVS 172
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWY--KDGSAISSSPNFFTLSVSAEDSGTYTCVAR 64
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
108-172 1.44e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 55.26  E-value: 1.44e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528515868  108 IIQQPQSQRIAEGSPVVLSCKAVGPVELQYQWFKGKDEMPEGNSPD---------LVFNRASPAQQGYYICRVS 172
Cdd:pfam13927   4 ITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSrslsgsnstLTISNVTRSDAGTYTCVAS 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
112-181 2.43e-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: 54.82  E-value: 2.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868   112 PQSQRIAEGSPVVLSCKAVGPVELQYQWFKGKDEMP----------EGNSPDLVFNRASPAQQGYYICRVSSGDKYIFSN 181
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLaesgrfsvsrSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
109-173 1.14e-08

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: 53.07  E-value: 1.14e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528515868 109 IQQPQSQRIAEGSPVVLSCKAVGPV-ELQYQWFKGKDEMPEGNSP------------DLVFNRASPAQQGYYICRVSS 173
Cdd:cd05895    3 LKEMKSQEVAAGSKLVLRCETSSEYpSLRFKWFKNGKEINRKNKPenikiqkkkkksELRINKASLADSGEYMCKVSS 80
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
211-275 2.49e-08

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: 51.34  E-value: 2.49e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528515868 211 PRPQALMEGDTLCLECSAQANPPPQFQWYFNkeLMPKCIRNFLKIPCITTADRGIYACRVYNLYH 275
Cdd:cd20948    2 PSDTYYLSGENLNLSCHAASNPPAQYSWTIN--GTFQTSSQELFLPAITENNEGTYTCSAHNSLT 64
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
210-272 2.86e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 51.63  E-value: 2.86e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528515868  210 QPRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMPKCiRNFLkIPCITTADRGIYACRVYN 272
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSS-PNFF-TLSVSAEDSGTYTCVARN 65
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
211-284 4.87e-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: 50.97  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868   211 PRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMPKCIRNF----------LKIPCITTADRGIYACRVYNLYHEMWSD 280
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFsvsrsgststLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 528515868   281 -QVQV 284
Cdd:smart00410  81 tTLTV 85
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
113-173 1.97e-06

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: 46.74  E-value: 1.97e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528515868 113 QSQRIAEGSPVVLSCKAVGPV-ELQYQWFKGKDEM----PE----GNSP---DLVFNRASPAQQGYYICRVSS 173
Cdd:cd05750    7 KSQTVQEGSKLVLKCEATSENpSPRYRWFKDGKELnrkrPKnikiRNKKknsELQINKAKLEDSGEYTCVVEN 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
224-282 2.57e-06

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: 45.78  E-value: 2.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528515868 224 LECSAQANPPPQFQWYFNKELMPKCIRNF---------LKIPCITTADRGIYACRVYNLYHEMWSDQV 282
Cdd:cd00096    3 LTCSASGNPPPTITWYKNGKPLPPSSRDSrrselgngtLTISNVTLEDSGTYTCVASNSAGGSASASV 70
I-set pfam07679
Immunoglobulin I-set domain;
108-172 4.60e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 45.33  E-value: 4.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528515868  108 IIQQPQSQRIAEGSPVVLSCKAVGPVELQYQWFKGKDEMP---------EGNSPDLVFNRASPAQQGYYICRVS 172
Cdd:pfam07679   3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRssdrfkvtyEGGTYTLTISNVQPDDSGKYTCVAT 76
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
203-286 5.97e-06

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


Pssm-ID: 409404  Cd Length: 102  Bit Score: 45.61  E-value: 5.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 203 SGLNITQQPRPQALMEGDTLCLECSAQANPPP--QFQW-YFNKE---------------LMPKCIRNFLKIPCITTADRG 264
Cdd:cd05742    1 SDLELSPNAEPTVLPQGETLVLNCTANVNLNEvvDFQWtYPSEKegklallkpdikvdwSEPGEFVSTLTIPEATLKDSG 80
                         90       100
                 ....*....|....*....|..
gi 528515868 265 IYACRVynLYHEMwSDQVQVNI 286
Cdd:cd05742   81 TYTCAA--RSGVM-KKEKQTSV 99
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
123-172 1.35e-05

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.47  E-value: 1.35e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528515868 123 VVLSCKAVGPVELQYQWFKGKDEMPEGNSPD---------LVFNRASPAQQGYYICRVS 172
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSrrselgngtLTISNVTLEDSGTYTCVAS 59
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
205-272 3.29e-05

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: 42.90  E-value: 3.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528515868 205 LNITQQPRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMPK------CIRNFLKIPCITTADRGIYACRVYN 272
Cdd:cd20957    2 LSATIDPPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHssrvqiLSEDVLVIPSVKREDKGMYQCFVRN 75
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
211-272 4.55e-05

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: 42.38  E-value: 4.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528515868 211 PRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMPKC---IR--NFLKIPCITTADRGIYACRVYN 272
Cdd:cd05725    4 PQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGryeILddHSLKIRKVTAGDMGSYTCVAEN 70
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
211-274 7.69e-05

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


Pssm-ID: 319300  Cd Length: 92  Bit Score: 42.19  E-value: 7.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528515868 211 PRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMPKCIRNFLK----------IPCITTADRGIYACRVYNLY 274
Cdd:cd05737    8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKveagrtvyftINGVSSEDSGKYGLVVKNKY 81
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
214-272 7.93e-05

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: 42.16  E-value: 7.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528515868 214 QALMEGDTLCLECSAQANPPPQFQWYFNKELMPKCIR--------------NFLKIPCITTADRGIYACRVYN 272
Cdd:cd20956   11 QTLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRfrvgdyvtsdgdvvSYVNISSVRVEDGGEYTCTATN 83
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
207-272 1.23e-04

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 41.38  E-value: 1.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528515868 207 ITQQPRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMP--KCIRN---FLKIPCITTADRGIYACRVYN 272
Cdd:cd04968    4 KVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVDGSPSsqWEITTsepVLEIPNVQFEDEGTYECEAEN 74
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
109-173 2.58e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 40.64  E-value: 2.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528515868 109 IQQPQSQRIAEGSPVVLSCKAVGPVELQYQWFKGKDEMPegNSPD-----------LVFNRASPAQQGYYICRVSS 173
Cdd:cd20972    5 IQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQ--NSPDiqihqegdlhsLIIAEAFEEDTGRYSCLATN 78
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
112-172 3.60e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 40.26  E-value: 3.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528515868  112 PQSQRIAEGSPVVLSCKAV-GPVELQYQWFKGKDEMPEGN----------SPDLVFNRASPAQQGYYICRVS 172
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGGTLIESLkvkhdngrttQSSLLISNVTKEDAGTYTCVVN 74
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
214-286 6.38e-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: 39.42  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 214 QALMEGDTLCLECSAQA-NPPPQFQWYFN-KELMPKC-----IRNF-----LKIPCITTADRGIYACRVYNLyheMWSDQ 281
Cdd:cd05750    9 QTVQEGSKLVLKCEATSeNPSPRYRWFKDgKELNRKRpknikIRNKkknseLQINKAKLEDSGEYTCVVENI---LGKDT 85

                 ....*
gi 528515868 282 VQVNI 286
Cdd:cd05750   86 VTGNV 90
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
215-273 6.90e-04

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


Pssm-ID: 143259  Cd Length: 88  Bit Score: 39.23  E-value: 6.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528515868 215 ALMeGDTLCLECSAQANPPPQFQWYFNKELMPKCIR-----NFLKIPCITTADRGIYACRVYNL 273
Cdd:cd05851   13 ALK-GQNVTLECFALGNPVPVIRWRKILEPMPATAEismsgAVLKIFNIQPEDEGTYECEAENI 75
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
208-286 7.12e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 39.24  E-value: 7.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 208 TQQPRPQALMEGDTLCLECSAQANPPPQFQWYFNKELMPKCIRNF---------LKIPCITTADRGIYACRVYNLYhEMW 278
Cdd:cd20949    3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASVADMskyriladgLLINKVTQDDTGEYTCRAYQVN-SIA 81

                 ....*...
gi 528515868 279 SDQVQVNI 286
Cdd:cd20949   82 SDMQERTV 89
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
210-272 1.26e-03

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 39.01  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528515868 210 QPRPQALMEGDTLCLECSAQANPPPQFQWYFNK-----ELMPKCIRNF---------LKIPCITTADRGIYACRVYN 272
Cdd:cd05734    7 QPNDQDGIYGKAVVLNCSADGYPPPTIVWKHSKgsgvpQFQHIVPLNGriqllsngsLLIKHVLEEDSGYYLCKVSN 83
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
108-169 1.34e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 38.69  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528515868 108 IIQQPQSQRIAEGSPVVLSCKAVGPVELQYQWFKG-----KDEMPEGNSPDL-----------VFNRASPAQQGYYIC 169
Cdd:cd07693    3 IVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNgqpleTDKDDPRSHRIVlpsgslfflrvVHGRKGRSDEGVYVC 80
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
219-274 1.48e-03

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 38.35  E-value: 1.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528515868 219 GDTLCLECSAQANPPPQFQWYFNKELMPKCIRNF-----LKIPCITTADRGIYACRVYNLY 274
Cdd:cd05728   14 GSSLRWECKASGNPRPAYRWLKNGQPLASENRIEveagdLRITKLSLSDSGMYQCVAENKH 74
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
219-272 1.91e-03

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 38.21  E-value: 1.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 219 GDTLcLECSAQANPPPQFQWYFNKELMPKCIRNF------LKIPCITTADRGIYACRVYN 272
Cdd:cd04969   18 GDVI-IECKPKASPKPTISWSKGTELLTNSSRICilpdgsLKIKNVTKSDEGKYTCFAVN 76
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
210-274 2.26e-03

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 37.91  E-value: 2.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528515868 210 QPRPQALMEGDTLCLECSAQANPPPQFQWYFN-KELMPKC------IRN---FLKIPCITTADRGIYACRVYNLY 274
Cdd:cd05857   10 EKKLHAVPAANTVKFRCPAAGNPTPTMRWLKNgKEFKQEHriggykVRNqhwSLIMESVVPSDKGNYTCVVENEY 84
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
212-277 2.48e-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: 37.97  E-value: 2.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528515868 212 RPQALMEGDTLCLECSAQANPPPQFQWYFN-KELMP-KCIRNF--------LKIPCITTADRGIYACRVYNLYHEM 277
Cdd:cd05729   12 REHALPAANKVRLECGAGGNPMPNITWLKDgKEFKKeHRIGGTkveekgwsLIIERAIPRDKGKYTCIVENEYGSI 87
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
206-239 2.78e-03

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 37.56  E-value: 2.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 528515868 206 NITQQPRPQALMEGDTLCLECSAQANPPPQFQWY 239
Cdd:cd20972    3 QFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWF 36
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
214-272 2.84e-03

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 37.39  E-value: 2.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528515868 214 QALMEGDTLCLECSAQANPPPQFQWY-FNKELMPKCIR--NF---LKIPCITTADRGIYACRVYN 272
Cdd:cd05731    5 TMVLRGGVLLLECIAEGLPTPDIRWIkLGGELPKGRTKfeNFnktLKIENVSEADSGEYQCTASN 69
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
207-274 2.99e-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: 37.79  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528515868 207 ITQQPRPQALMEGDTLCLECSAQANPPPQFQWYFNKELM------PKC-IRNF-----LKIPCITTADRGIYACRVYNLY 274
Cdd:cd20951    3 FIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpssipGKYkIESEygvhvLHIRRVTVEDSAVYSAVAKNIH 82
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
209-245 5.13e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 37.06  E-value: 5.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 528515868 209 QQPRPQALMEGDTLCLECSAQANPPPQFQWYFNKELM 245
Cdd:cd05892    5 QKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEML 41
 
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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