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Conserved domains on  [gi|306991881|pdb|3NVQ|A]
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Chain A, Semaphorin-7A

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
28-447 0e+00

The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); Sema7A plays regulatory roles in both immune and nervous systems. Unlike other semaphorins, which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Sema7A also plays a critical role in the negative regulation of T cell activation and function. Sema7A is a membrane-anchored member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


:

Pssm-ID: 200504 [Multi-domain]  Cd Length: 414  Bit Score: 740.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       28 TEPHTVLFHEPGSSSVWVGGRGKVYLFDFPeGKNASVRTVNIGSTKGSCLDKR---DCENYITLLERRSEGLLACGTNAR 104
Cdd:cd11243   1 KESYPVFFHEAGSSSVYVGGQGALYLLDFT-GSAVIVKKIPDEKTEKDCKKRAtldDCENYITLIKKLDYRLLVCGTNAG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      105 HPSCWNLVNGTVVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNgkIPRFRRIRGESELYTSDTVMQNPQFIKAT 184
Cdd:cd11243  80 SPKCWFLVNQTLVTLSADRGVAPFLPDENSLVLIEGNNVYSTISGKKGN--IPRFRRYGGKKELYTSDTVMQKPQFVKAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      185 IVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCSDAATNKNFNRLQDVFL 264
Cdd:cd11243 158 LLPEDEQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLSTSKWSTFLKARLVCGDPATPMNFNRLQDVFL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      265 LPDPSgqWRDTRVYGVFSNPWNYSAVCVYSLGDIDKVFRTSSLKGYHSSLPNPRPGKCLPDQQPIPTETFQVADRHPEVA 344
Cdd:cd11243 238 LPKEE--WREAVVYGVFSNTWGSSAVCSYSLGDIDKVFRTSSLKGYSGSLPNPRPGTCVPPEQTHPSETFSFADEHPELD 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      345 QRVEPMGPLKTPLFHSKYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGEQEHsfafNIMEIQPFRRAAAIQTM 424
Cdd:cd11243 316 DRIEPDEPRKLPVFQNKDHYQKVVVDEVRASDGVSYDVLYLATDKGKIHKVVESKGQTH----NIMEIQPFKEQEPIQSM 391
                       410       420
                ....*....|....*....|...
3NVQ_A      425 SLDAERRKLYVSSQWEVSQVPLD 447
Cdd:cd11243 392 ILDAERSHLYVGTKAEVTRLPLD 414
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
449-476 4.30e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 38.46  E-value: 4.30e-04
                          10        20        30
                  ....*....|....*....|....*....|
3NVQ_A        449 CEVYGGgCHGCLMSRDPYCGWD--QGRCIS 476
Cdd:pfam01437   2 CSQYTS-CSSCLAARDPYCGWCssEGRCVR 30
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
505-575 1.08e-03

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


The actual alignment was detected with superfamily member cd05872:

Pssm-ID: 472250  Cd Length: 86  Bit Score: 38.19  E-value: 1.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3NVQ_A      505 APLQKVSLAPNSRYYLSCPMESRHATYSWRHKENVEQSCEPGHQSPNCILFIENLTAQQYGHYFCEAQEGS 575
Cdd:cd05872   1 LPVKFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSYLRLGTDGLLILVTSPEHSGTYRCYSEEEG 71
 
Name Accession Description Interval E-value
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
28-447 0e+00

The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); Sema7A plays regulatory roles in both immune and nervous systems. Unlike other semaphorins, which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Sema7A also plays a critical role in the negative regulation of T cell activation and function. Sema7A is a membrane-anchored member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200504 [Multi-domain]  Cd Length: 414  Bit Score: 740.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       28 TEPHTVLFHEPGSSSVWVGGRGKVYLFDFPeGKNASVRTVNIGSTKGSCLDKR---DCENYITLLERRSEGLLACGTNAR 104
Cdd:cd11243   1 KESYPVFFHEAGSSSVYVGGQGALYLLDFT-GSAVIVKKIPDEKTEKDCKKRAtldDCENYITLIKKLDYRLLVCGTNAG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      105 HPSCWNLVNGTVVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNgkIPRFRRIRGESELYTSDTVMQNPQFIKAT 184
Cdd:cd11243  80 SPKCWFLVNQTLVTLSADRGVAPFLPDENSLVLIEGNNVYSTISGKKGN--IPRFRRYGGKKELYTSDTVMQKPQFVKAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      185 IVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCSDAATNKNFNRLQDVFL 264
Cdd:cd11243 158 LLPEDEQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLSTSKWSTFLKARLVCGDPATPMNFNRLQDVFL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      265 LPDPSgqWRDTRVYGVFSNPWNYSAVCVYSLGDIDKVFRTSSLKGYHSSLPNPRPGKCLPDQQPIPTETFQVADRHPEVA 344
Cdd:cd11243 238 LPKEE--WREAVVYGVFSNTWGSSAVCSYSLGDIDKVFRTSSLKGYSGSLPNPRPGTCVPPEQTHPSETFSFADEHPELD 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      345 QRVEPMGPLKTPLFHSKYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGEQEHsfafNIMEIQPFRRAAAIQTM 424
Cdd:cd11243 316 DRIEPDEPRKLPVFQNKDHYQKVVVDEVRASDGVSYDVLYLATDKGKIHKVVESKGQTH----NIMEIQPFKEQEPIQSM 391
                       410       420
                ....*....|....*....|...
3NVQ_A      425 SLDAERRKLYVSSQWEVSQVPLD 447
Cdd:cd11243 392 ILDAERSHLYVGTKAEVTRLPLD 414
Sema smart00630
semaphorin domain;
31-422 8.75e-96

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 298.13  E-value: 8.75e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A          31 HTVLFHEPGSSSVWVGGRGKVYLFDFPEGKNASVRTVNIGSTKG--SCLDK-----RDCENYITLLERRSEG-LLACGTN 102
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDceECVSKgkdppTDCVNYIRLLLDYNEDrLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         103 ARHPSCWNLVNGtvvplgemrgyapfspdenslvlfegdEVYSTIRKqEYNGKIPRFRRIRGESEL-----YTSDTV--- 174
Cdd:smart00630  81 AFQPVCRLRNLG---------------------------ELYVGTVA-DFSGSDPAIPRSLSVRRLkgtsgVSLRTVlyd 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         175 ---MQNPQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTFLKAMLVCSDAA 251
Cdd:smart00630 133 skwLNEPNFVYAF------ESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLD-KKWTSFLKARLECSVPG 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         252 T-NKNFNRLQDVFLLpdPSGQWRDTRVYGVFS---NPWNYSAVCVYSLGDIDKVFR---------TSSLKGY-HSSLPNP 317
Cdd:smart00630 206 EdPFYFNELQAAFLL--PPGSESDDVLYGVFStssNPIPGSAVCAFSLSDINAVFNgpfkecetsTSQWLPYsRGKVPYP 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         318 RPGKCL---PDQQPIPTETFQVADRHPEVAQRVEPMGPlkTPLFH---SKYHYQKVAVHRMQASHGetFHVLYLTTDRGT 391
Cdd:smart00630 284 RPGTCPnkpPSSKDLPDETLNFIKSHPLMDEVVQPLTG--RPLFVktdSNYLLTSIAVDRVATDGN--YTVLFLGTSDGR 359
                          410       420       430
                   ....*....|....*....|....*....|.
3NVQ_A         392 IHKVVEPGEQEHSFAFNIMEIQPFRRAAAIQ 422
Cdd:smart00630 360 ILKVVLSESSSSSESVVLEEISVFPDGSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
259-427 2.75e-46

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 160.90  E-value: 2.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A        259 LQDVFLLPDPSGQWRDTRVYGVFS----NPWNYSAVCVYSLGDIDKVFR---------TSSLKGYHSSLPNPRPGKCLPD 325
Cdd:pfam01403   1 LQDVFVLKPGAGDALDTVLYGVFTtqwsNSIGGSAVCAFSLSDINAVFEgpfkeqeksDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A        326 --QQPIPTETFQVADRHPEVAQRVEPMGplKTPLFHSK-YHYQKVAVHRMQASHGEtFHVLYLTTDRGTIHKVVEPGEQE 402
Cdd:pfam01403  81 plRLDLPDSVLNFVKDHPLMDEAVQPVG--GRPLLVRTgVRLTSIAVDRVQALDGN-YTVLFLGTDDGRLHKVVLVGSEE 157
                         170       180
                  ....*....|....*....|....*
3NVQ_A        403 hsfAFNIMEIQPFRRAAAIQTMSLD 427
Cdd:pfam01403 158 ---SHIIEEIQVFPEPQPVLNLLLS 179
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
449-476 4.30e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 38.46  E-value: 4.30e-04
                          10        20        30
                  ....*....|....*....|....*....|
3NVQ_A        449 CEVYGGgCHGCLMSRDPYCGWD--QGRCIS 476
Cdd:pfam01437   2 CSQYTS-CSSCLAARDPYCGWCssEGRCVR 30
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
505-575 1.08e-03

Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are composed of the immunoglobulin (Ig)-like domain of Sema4B and similar proteins. Sema4B is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4B has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4B has been shown to preferentially regulate the development of the postsynaptic specialization at the glutamatergic synapses. This cytoplasmic domain includes a PDZ-binding motif upon which the synaptic localization of Sem4B is dependent. Sema4B is a ligand of CLCP1. CLCP1 was identified in an expression profiling analysis, which compared a highly metastic lung cancer subline with its low metastic parental line. Sema4B was shown to promote CLCP1 endocytosis and their interaction is a potential target for therapeutic intervention of metastasis.


Pssm-ID: 409456  Cd Length: 86  Bit Score: 38.19  E-value: 1.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3NVQ_A      505 APLQKVSLAPNSRYYLSCPMESRHATYSWRHKENVEQSCEPGHQSPNCILFIENLTAQQYGHYFCEAQEGS 575
Cdd:cd05872   1 LPVKFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSYLRLGTDGLLILVTSPEHSGTYRCYSEEEG 71
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
449-498 1.38e-03

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 36.75  E-value: 1.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
3NVQ_A         449 CEVYGGgCHGCLMSRDPYCGWD--QGRCISiYSSERSVLQSINpaepHKECP 498
Cdd:smart00423   2 CSKYTS-CSECLLARDPYCAWCssQGRCTS-GERCDSRRQNWL----SGGCP 47
 
Name Accession Description Interval E-value
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
28-447 0e+00

The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); Sema7A plays regulatory roles in both immune and nervous systems. Unlike other semaphorins, which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Sema7A also plays a critical role in the negative regulation of T cell activation and function. Sema7A is a membrane-anchored member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200504 [Multi-domain]  Cd Length: 414  Bit Score: 740.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       28 TEPHTVLFHEPGSSSVWVGGRGKVYLFDFPeGKNASVRTVNIGSTKGSCLDKR---DCENYITLLERRSEGLLACGTNAR 104
Cdd:cd11243   1 KESYPVFFHEAGSSSVYVGGQGALYLLDFT-GSAVIVKKIPDEKTEKDCKKRAtldDCENYITLIKKLDYRLLVCGTNAG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      105 HPSCWNLVNGTVVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNgkIPRFRRIRGESELYTSDTVMQNPQFIKAT 184
Cdd:cd11243  80 SPKCWFLVNQTLVTLSADRGVAPFLPDENSLVLIEGNNVYSTISGKKGN--IPRFRRYGGKKELYTSDTVMQKPQFVKAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      185 IVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCSDAATNKNFNRLQDVFL 264
Cdd:cd11243 158 LLPEDEQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLSTSKWSTFLKARLVCGDPATPMNFNRLQDVFL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      265 LPDPSgqWRDTRVYGVFSNPWNYSAVCVYSLGDIDKVFRTSSLKGYHSSLPNPRPGKCLPDQQPIPTETFQVADRHPEVA 344
Cdd:cd11243 238 LPKEE--WREAVVYGVFSNTWGSSAVCSYSLGDIDKVFRTSSLKGYSGSLPNPRPGTCVPPEQTHPSETFSFADEHPELD 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      345 QRVEPMGPLKTPLFHSKYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGEQEHsfafNIMEIQPFRRAAAIQTM 424
Cdd:cd11243 316 DRIEPDEPRKLPVFQNKDHYQKVVVDEVRASDGVSYDVLYLATDKGKIHKVVESKGQTH----NIMEIQPFKEQEPIQSM 391
                       410       420
                ....*....|....*....|...
3NVQ_A      425 SLDAERRKLYVSSQWEVSQVPLD 447
Cdd:cd11243 392 ILDAERSHLYVGTKAEVTRLPLD 414
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
28-447 0e+00

The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. They can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted proteins; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. The semaphorins exert their function through their receptors, the neuropilin and plexin families. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200496 [Multi-domain]  Cd Length: 437  Bit Score: 528.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       28 TEPHTVLFHEPGSSsVWVGGRGKVYLFDFP----EGKNASVRTVnigSTKGSCLDKR----DCENYITLLERRS-EGLLA 98
Cdd:cd11235   1 LKYHTKLLHEDRST-LYVGARDRVYLVDLDslytEQKVAWPSSP---DDVDTCYLKGkskdDCRNFIKVLEKNSdDSLLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       99 CGTNARHPSCWNLVNGT---VVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNGKIPRFRRIR---GESELYTSD 172
Cdd:cd11235  77 CGTNAFNPSCRNYNVETfelVGKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGhnpPLRTEYHDS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      173 TVMQNPQFIKATIVHqdqaydDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLsVSKWNTFLKAMLVCSDAA- 251
Cdd:cd11235 157 KWLNEPQFVGAFDIG------DYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSL-EKKWTTFLKARLNCSVPGe 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      252 TNKNFNRLQDVFLLPDPSgqWRDTRVYGVFSNPWN---YSAVCVYSLGDIDKVFRtSSLKGYHSSLPN-----------P 317
Cdd:cd11235 230 FPFYFNELQDVFDLPSPS--NKEKIFYAVFTTPYNsipGSAVCAYSLSDIEAVFN-GPFKEQHSSNSAwlpvpdervpeP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      318 RPGKCLPDQQPIPTETFQVADRHPEVAQRVEPMgpLKTPLFHSK---YHYQKVAVHRMQASHGETFHVLYLTTDRGTIHK 394
Cdd:cd11235 307 RPGTCVDDSSPLPDDTLNFIKSHPLMDEAVTPI--LNRPLFIKTdvnYRFTKIAVDRVQAKLGQTYDVLFVGTDRGIILK 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
3NVQ_A      395 VVEPGEQEhSFAFNIMEIQPFRR-AAAIQTMSLDAERRKLYVSSQWEVSQVPLD 447
Cdd:cd11235 385 VVSLPEQG-LQASNILEEMPVGPpPEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema smart00630
semaphorin domain;
31-422 8.75e-96

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 298.13  E-value: 8.75e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A          31 HTVLFHEPGSSSVWVGGRGKVYLFDFPEGKNASVRTVNIGSTKG--SCLDK-----RDCENYITLLERRSEG-LLACGTN 102
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDceECVSKgkdppTDCVNYIRLLLDYNEDrLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         103 ARHPSCWNLVNGtvvplgemrgyapfspdenslvlfegdEVYSTIRKqEYNGKIPRFRRIRGESEL-----YTSDTV--- 174
Cdd:smart00630  81 AFQPVCRLRNLG---------------------------ELYVGTVA-DFSGSDPAIPRSLSVRRLkgtsgVSLRTVlyd 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         175 ---MQNPQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTFLKAMLVCSDAA 251
Cdd:smart00630 133 skwLNEPNFVYAF------ESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLD-KKWTSFLKARLECSVPG 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         252 T-NKNFNRLQDVFLLpdPSGQWRDTRVYGVFS---NPWNYSAVCVYSLGDIDKVFR---------TSSLKGY-HSSLPNP 317
Cdd:smart00630 206 EdPFYFNELQAAFLL--PPGSESDDVLYGVFStssNPIPGSAVCAFSLSDINAVFNgpfkecetsTSQWLPYsRGKVPYP 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A         318 RPGKCL---PDQQPIPTETFQVADRHPEVAQRVEPMGPlkTPLFH---SKYHYQKVAVHRMQASHGetFHVLYLTTDRGT 391
Cdd:smart00630 284 RPGTCPnkpPSSKDLPDETLNFIKSHPLMDEVVQPLTG--RPLFVktdSNYLLTSIAVDRVATDGN--YTVLFLGTSDGR 359
                          410       420       430
                   ....*....|....*....|....*....|.
3NVQ_A         392 IHKVVEPGEQEHSFAFNIMEIQPFRRAAAIQ 422
Cdd:smart00630 360 ILKVVLSESSSSSESVVLEEISVFPDGSPIS 390
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
35-446 1.18e-77

The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 semaphorins (Sema4s) are transmembrane regulator molecules involved in the development of the nervous system, immune response, cytoskeletal organization, angiogenesis, and cell-cell interactions. There are 7 distinct subfamilies in class 4 semaphorins, named 4A to 4G. Several class 4 subfamilies play important roles in the immune system and are called "immune semaphorins". Sema4A plays critical roles in T cell-DC interactions in the immune response. Sema4D/CD100, expressed by lymphocytes, promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. It is required for normal activation of B and T lymphocytes. Sema4B negatively regulates basophil functions through T cell-basophil contacts and significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. Sema4s not only influence the activation state of cells but also modulate their migration and survival. The effects of Sema4s on nonlymphoid cells are mediated by plexin D1 and plexin Bs. The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex and are involved in neural tube closure and development of cerebellar granules cells through receptor plexin B2. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200501 [Multi-domain]  Cd Length: 456  Bit Score: 253.10  E-value: 1.18e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       35 FHEPGSS------------SVWVGGRGKVYLFDF----PEGKN-----ASVRTVNIGSTKGSCLdKRDCENYITLLERRS 93
Cdd:cd11240   1 FSQEGIQnystlllsedegTLYVGAREALFALNVsdisTELKDkikweASEDKKKECANKGKDN-QTDCFNFIRILQFYN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       94 EG-LLACGTNARHPSC--WNLVNGTVvPLGEM---RGYAPFSPDENSLVLFEGDEVYSTIrKQEYNGKIPRFRRIRGESE 167
Cdd:cd11240  80 SThLYVCGTFAFSPRCtyINLSDFSL-SSIKFedgKGRCPFDPAQRYTAIMVDGELYSAT-VNNFLGSEPVISRNHSEGN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      168 LYTSDTVM---QNPQFIKATIVHQDQAY----DDKIYYFFRE-----DNPDKnpeapLNVSRVAQLCRGDQGGESSLSvS 235
Cdd:cd11240 158 VLKTENTLrwlNEPAFVGSAHIRESIDSpdgdDDKIYFFFTEtaveyDFYEK-----VTVSRVARVCKGDLGGQRTLQ-K 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      236 KWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSgqWRDTRVYGVFSNPWN---YSAVCVYSLGDIDKVF---------R 303
Cdd:cd11240 232 KWTTFLKAQLVCSQPDSGLPFNVLRDVFVLSPDS--WDATIFYGVFTSQWNvsgLSAVCAYSLEDIKKVFsgkykefnrE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      304 TSSLKGYHSSLPNPRPGKCLPDQQ---------PIPTETFQVADRHPEVAQRVEPMG-PLktpLFHSKYHYQKVAVHRMQ 373
Cdd:cd11240 310 TSKWSRYTGPVPDPRPGACITNSArsqgitsslNLPDNVLTFVKDHPLMDEQVHPINrPL---LVKSGVNYTRIAVHRVQ 386
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3NVQ_A      374 ASHGETFHVLYLTTDRGTIHKVVEPGEQEHSfafnIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11240 387 ALDGQTYTVLFLGTEDGFLHKAVSLDGGMHI----IEEIQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
81-449 6.42e-63

The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins (Sema3s) are secreted regulator molecules involved in the development of the nervous system, vasculogenesis, angiogenesis,and tumorigenesis. There are 7 distinct subfamilies named Sema3A to 3G. Sema3s function as repellent signals during axon guidance by repelling neurons away from the source of Sema3s. However, Sema3s that are secreted by tumor cells play an inhibitory role in tumor growth and angiogenesis (specifically Sema3B and Sema3F). Sema3s functions by forming complexes with neuropilins and A-type plexins, where neuropilins serve as the ligand binding moiety and the plexins function as signal transduction component. Sema3s primarily inhibit the cell motility and migration of tumor and endothelial cells by inducing collapse of the actin cytoskeleton via neuropilins and plexins. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200500 [Multi-domain]  Cd Length: 471  Bit Score: 214.53  E-value: 6.42e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       81 DCENYITLLER-RSEGLLACGTNARHPSCwnlvngTVVPLGEM----------------RGYAPFSPDENSLVLFEGDEV 143
Cdd:cd11239  67 ECANFVRVLQPyNRTHLYACGTGAFHPIC------AFINVGRRledpifklddsslesgRGKCPFDPNQPFASVLIDGEL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      144 YSTIrKQEYNGKIPRFRRIRGES-----ELYTSdTVMQNPQFIKAT-IVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSR 217
Cdd:cd11239 141 YSGT-AIDFMGRDAAIFRSLGHRhyirtEQYDS-RWLNEPKFVGAYlIPDSDNPDDDKVYFFFREKAVEAEGSGKAIYSR 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      218 VAQLCRGDQGGESSLsVSKWNTFLKAMLVCS---DAATNKNFNRLQDVFLLP--DPsgqwRDTRVYGVF---SNPWNYSA 289
Cdd:cd11239 219 VGRICKNDVGGQRSL-VNKWSTFLKARLVCSvpgPDGIDTYFDELEDVFLLPtrDP----KNPLIYGVFttsSNVFKGSA 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      290 VCVYSLGDIDKVFR---------TSSLKGYHSSLPNPRPGKC--------LPDQQPIPTETFQVADRHPEVAQRVEPMGp 352
Cdd:cd11239 294 VCVYSMADIRAAFNgpfahkegpNYQWVEYQGKVPYPRPGTCpsktygplYKSTKDFPDDVISFARSHPLMYNPVYPLH- 372
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      353 lKTPLF---HSKYHYQKVAVHRMQASHGEtFHVLYLTTDRGTIHKVVE-PGEQEHSFAFNIMEIQPFRRAAAIQTMSLDA 428
Cdd:cd11239 373 -GRPLLirtNVPYRLTQIAVDRVEAEDGQ-YDVLFIGTDSGTVLKVVSlPKENWEMEEVILEELQVFKHPSPITSMEISS 450
                       410       420
                ....*....|....*....|.
3NVQ_A      429 ERRKLYVSSQWEVSQVPLDLC 449
Cdd:cd11239 451 KRQQLYVGSAEGVVQLPLHRC 471
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
81-449 4.97e-59

The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is coexpressed with semaphorin 3F and both proteins are candidate tumor suppressors. Both Sema3B and Sema3F show high levels of expression in normal tissues and low-grade tumors but are down-regulated in highly metastatic tumors in the lung, melanoma cells, bladder carcinoma cells and prostate carcinoma. They are upregulated by estrogen and inhibit cell motility and invasiveness through decreased FAK phosphorylation and inhibition of MMP-2 and MMP-9 expression. Two receptor families, the neuropilins (NP) and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3B is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200511 [Multi-domain]  Cd Length: 471  Bit Score: 204.38  E-value: 4.97e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       81 DCENYITLLERRSEG-LLACGTNARHPSCWNLVNGTVVP----------LGEMRGYAPFSPDENSLVLFEGDEVYSTIRK 149
Cdd:cd11250  67 DCMNYVKILHHYNRThLYACGTGAFHPTCAFVEVGQRMEdhvfrldpsrVEDGKGKSPYDPRHTAASVLVGDELYSGVAT 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      150 QEYNGKIPRFRRIRGESELYTS--DTVMQN-PQFIKAT-IVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGD 225
Cdd:cd11250 147 DLMGRDFTIFRSLGQRPSLRTEqhDSRWLNePKFVKVFwIPESENPDDDKIYFFFRETAVEAAGLGKQSYSRIGQICRND 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      226 QGGESSLsVSKWNTFLKAMLVCS---DAATNKNFNRLQDVFLLpdPSGQWRDTRVYGVF---SNPWNYSAVCVYSLGDID 299
Cdd:cd11250 227 MGGQRSL-VNKWTTFLKARLVCSvpgNEGGDTHFDELRDVFLL--QTRDKRNPLIYAVFstsSSVFQGSAVCVYTMNDVR 303
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      300 KVF---------RTSSLKGYHSSLPNPRPGKC-------LPDQQPIPTETFQVADRHPEVAQRVEPMGplKTPLF---HS 360
Cdd:cd11250 304 RAFlgpfahkegPNYQWVSYQGKVPYPRPGMCpsktfgsFESTKDFPDDVIQFARNHPLMFNPVLPLG--GRPLFlrtGI 381
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      361 KYHYQKVAVHRMQASHGEtFHVLYLTTDRGTIHKV--VEPGEQEHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQ 438
Cdd:cd11250 382 PYTFTQIAVDRVAAADGH-YDVMFIGTDVGSVLKVisVPKGSWPSNEELLLEELHVFKDSSPITSMQISSKRQQLYVGSR 460
                       410
                ....*....|.
3NVQ_A      439 WEVSQVPLDLC 449
Cdd:cd11250 461 SGVSQLPLHRC 471
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
26-446 3.25e-58

The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex. Sema4G and Sema4C proteins specifically bind to Plexin B2 expressed in the cerebellar granule cells. Sema4G and Sema4C are involved in neural tube closure and cerebellar granule cell development through Plexin B2.Sema4G belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200523 [Multi-domain]  Cd Length: 457  Bit Score: 201.53  E-value: 3.25e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       26 GQTEPHTVLFHEPGSSSVWVGGRGKVYlfdfpegknaSVRTVNIGST-------------KGSCLDK-----RDCENYIT 87
Cdd:cd11262   5 GPAQNYSTLLLEDESGRLYVGARGAIF----------SLNASDISDSsaltidweaspeqKHQCLKKgknnqTECFNHVR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       88 LLER-RSEGLLACGTNARHPSCWNL-VNGTVVPLG--EMRGYAPFSPDENSLVLFEGDEVYSTIRKQEYNgkIPRFRRIR 163
Cdd:cd11262  75 FLQRfNSTHLYTCGTHAFRPLCAYIdAERFTLSSQfeEGKEKCPYDPAKGYTGLIVDGQLYTASQYEFRS--FPDIRRNS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      164 GESELYTSDTVMQ---NPQFIKATIVHQDQAY----DDKIYYFFREDNPDKNPE-APLNVSRVAQLCRGDQGGESSLSvS 235
Cdd:cd11262 153 PQPTLRTEEAPTRwlnDADFVGSVLVRESMNSsvgdDDKIYFFFTERSQEETAYfSQSRVARVARVCKGDRGGKKTLQ-R 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      236 KWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSGQwrDTRVYGVFSNPW---NYSAVCVYSLGDIDKVFR--------- 303
Cdd:cd11262 232 KWTSFLKARLVCYIPEYEFLFNVLRSVFVLWGSTPQ--DTVFYGIFGLEWknvKASAICRYSLSDIQTAFEgpymeyqds 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      304 TSSLKGYHSSLPNPRPGKCLPDQ---------QPIPTETFQVADRHPEVAQRVEPMG--PLktpLFHSKYHYQKVAVHRM 372
Cdd:cd11262 310 SSKWSRYTGKVPEPRPGSCITDEhrsqginssQDLPDNVLDFVRRHPLMAEQVLPVEgrPL---LFKRNVIYTKIAVQTV 386
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3NVQ_A      373 QASHGETFHVLYLTTDRGTIHKVVEPGEQEHSfafnIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11262 387 RGLDGRVYDVLFLGTDEGWLHKAVVIGSAVHI----IEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
79-446 5.85e-58

The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in T and B cells, is an immune semaphorin. It functions as a negative regulatory of basophils through T cell-basophil contacts and it significantly inhibits IL-4 and IL-6 production from basophils in response to various stimuli, including IL-3 and papain. In addition, T cell-derived Sema4B suppresses basophil-mediated Th2 skewing and humoral memory responses. Sema4B may be also involved in lung cancer cell mobility by inducing the degradation of CLCP1 (CUB, LCCL-homology, coagulation factor V/VIII homology domains protein). Sema4B is characterized by a PDZ-binding motif at the carboxy-terminus, which mediates interaction with the post-synaptic density protein PSD-95/SAP90, which is thought to play a central role during synaptogenesis and in the structure and function of post-synaptic specializations of excitatory synapses. Sema4B belongs to class 4 transmembrane semaphorin family proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200518 [Multi-domain]  Cd Length: 464  Bit Score: 201.24  E-value: 5.85e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       79 KRDCENYITLLER-RSEGLLACGTNARHPSCWNLVN----------GTVVpLGEMRGYAPFSPDENSLVLFEGDEVYsTI 147
Cdd:cd11257  67 QRDCQNYIKILLRlNSTHLFTCGTYAFSPICTYIVMtnfslerdekGEPL-LEDGKGRCPFDPEYKSTAIMVDGELY-TG 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      148 RKQEYNGKIPRFRRIRGE-SELYTSDTV--MQNPQFIKATIVHQD----QAYDDKIYYFFREDNPDKNPEAPLNVSRVAQ 220
Cdd:cd11257 145 TVSNFQGNDPIIYRSLGSgTPLKTENSLnwLQDPAFVGSAYIQESlpklVGDDDKIYFFFSETGKEFDFFENTIVSRIAR 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      221 LCRGDQGGESSLSvSKWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSGQWRDTRVYGVFSNPWNY-----SAVCVYSL 295
Cdd:cd11257 225 VCKGDEGGERVLQ-KRWTTFLKAQLLCSLPDDGFPFNVLQDVFVLTPSPEDWKDTLFYGVFTSQWHKgtagsSAVCVFTM 303
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      296 GDIDKVF---------RTSSLKGYHSSLPNPRPGKCLPD---QQPIpTETFQVADR-------H--PEVAQRVEPMgplk 354
Cdd:cd11257 304 DQVQRAFnglykevnrETQQWYTYTHPVPEPRPGACITNsarERKI-NSSLHMPDRvlnfvkdHflMDGQVRSQPL---- 378
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      355 tpLFHSKYHYQKVAVHRMQASHgETFHVLYLTTDRGTIHKVVEPGEQEHSfafnIMEIQPFRRAAAIQTMSLDAERRKLY 434
Cdd:cd11257 379 --LLQPQVRYTQIAVHRVKGLH-KTYDVLFLGTDDGRLHKAVSVGPMVHI----IEELQIFSEGQPVQNLLLDTHKGLLY 451
                       410
                ....*....|..
3NVQ_A      435 VSSQWEVSQVPL 446
Cdd:cd11257 452 ASSHSGVVQVPV 463
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
25-446 8.23e-57

The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); Sema4D/CD100 is expressed in immune cells and plays critical roles in immune response; it is thus termed an "immune semaphorin". It is expressed by lymphocytes and promotes the aggregation and survival of B lymphocytes and inhibits cytokine-induced migration of immune cells in vitro. Sema4D/CD100 knock-out mice demonstrate that Sema4D is required for normal activation of B and T lymphocytes. Sema4D increases B-cell and DC function using either Plexin B1 or CD72 as receptors. The function of Sema4D in immune response implicates its role in infectious and noninfectious diseases. Sema4D belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200520 [Multi-domain]  Cd Length: 471  Bit Score: 198.16  E-value: 8.23e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       25 FGQTEPHTVLFHEPGSSS------------VWVGGRGKVY--------------LFDFPEGKNASVrtvnigSTKGSClD 78
Cdd:cd11259   2 WEHKEVQLVHFHEPDVSNystlllsedkdvLYVGAREAVFalnalnisekqhelYWKVSEDKRTKC------AVKGKS-K 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       79 KRDCENYITLLERRSEGLL-ACGTNARHPSCwNLVNGTVVPLGEM----RGYAPFSPDENSLVLFEGDEVYStirKQEYN 153
Cdd:cd11259  75 QTECRNYIRVLQPLNDTFLyVCGTNAFQPTC-DYLNLTSFRLLGKnedgKGRCPFDPAQSYTSVMVDGELYS---GTSYN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      154 --GKIPRFRRIRGESELYTSDTV--MQNPQFIKATIVHQDQ----AYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGD 225
Cdd:cd11259 151 flGSEPIISRNSSQSPLRTEYAIpwLNEPSFVFADVIRADPdspdGEDDKIYFFFTEVSVEYEFVGKLLIPRIARVCKGD 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      226 QGGESSLSvSKWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSgqWRDTRVYGVFSNPWN---YSAVCVYSLGDIDKVF 302
Cdd:cd11259 231 QGGLRTLQ-KKWTSFLKARLICSIPDKNLVFNVVNDVFILKSPT--LKEPVIYGVFTPQLNnvgLSAVCAYNLSTVEEVF 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      303 -----------RTSSLK--GYHSSLPNPRPGKCLPDQQ---------PIPTETFQVADRHPEVAQRVEPMGPlKTPLFHS 360
Cdd:cd11259 308 skgkymqsatvEQSHTKwvRYNGEVPKPRPGACINNEAraanytsslNLPDKTLQFVKDHPLMDDSVTPIGN-RPRLIKK 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      361 KYHYQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGEQEHSfafnIMEIQPFRRAAAIQT--MSLDAERRKLYVSSQ 438
Cdd:cd11259 387 DVNYTQIVVDRVQALDGTIYDVMFISTDRGALHKAISLENEVHI----IEETQLFPDFEPVQTllLSSKKGRRFLYAGSN 462

                ....*...
3NVQ_A      439 WEVSQVPL 446
Cdd:cd11259 463 SGVVQSPL 470
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
80-450 3.39e-56

The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been reported to inhibit the growth of certain experimental tumors and to regulate endothelial cell migration and apoptosis in vitro, as well as arteriogenesis in the muscle, skin vessel permeability, and tumor angiogenesis in vivo. The function of Sema3A is mediated through receptors neuropilin-1 (NP1) and plexins, although little is known about the requirement of specific plexins in its receptor complex. It is known however that Plexin-A4 is the receptor for Sema3A in the Toll-like receptor- and sepsis-induced cytokine storm during immune response. Sema3A is a member of the Class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200510 [Multi-domain]  Cd Length: 493  Bit Score: 197.14  E-value: 3.39e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       80 RDCENYITLLERRSEG-LLACGTNARHPSCWNLVNG-----TVVPLGEM-----RGYAPFSPDENSLVLFEGDEVYSTIR 148
Cdd:cd11249  87 KECANFIKVLKAYNQThLYACGTGAFHPVCTYIEVGhhpedNIFRLEDShfengRGKSPYDPKLLTASLLIDGELYSGTA 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      149 KQEYNGKIPRFRRIRGESELYTS---DTVMQNPQFIKATIV-HQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRG 224
Cdd:cd11249 167 ADFMGRDFAIFRTLGHHHPIRTEqhdSRWLNDPRFISAHLIpESDNPEDDKIYFFFRENAIDGEHTGKATHARIGQLCKN 246
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      225 DQGGESSLsVSKWNTFLKAMLVCSDAATN---KNFNRLQDVFLL--PDPsgqwRDTRVYGVF---SNPWNYSAVCVYSLG 296
Cdd:cd11249 247 DFGGHRSL-VNKWTTFLKARLICSVPGPNgidTHFDELQDVFLMnsKDP----KNPIVYAVFttsSNIFKGSAVCMYSMT 321
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      297 DIDKVF---------RTSSLKGYHSSLPNPRPGKClPDQ--------QPIPTETFQVADRHPEVAQRVEPMGP----LKT 355
Cdd:cd11249 322 DIRRVFlgpyahrdgPNYQWVPFQGRVPYPRPGTC-PSKtfggfdstKDLPDDVITFARSHPAMYNPVFPINNrpiiIKT 400
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      356 PLfhsKYHYQKVAVHRMQASHGEtFHVLYLTTDRGTIHKVVE-PGEQEHSFAFNIM-EIQPFRRAAAIQTMSLDAERRKL 433
Cdd:cd11249 401 DV---DYQFTQIVVDRVEAEDGQ-YDVMFIGTDMGTVLKVVSiPKETWHDLEEVLLeEMTVFREPTAISAMELSTKQQQL 476
                       410
                ....*....|....*..
3NVQ_A      434 YVSSQWEVSQVPLDLCE 450
Cdd:cd11249 477 YIGSAIGVSQLPLHRCD 493
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
81-449 7.26e-54

The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is coexpressed with semaphorin3B. Both Sema3B and Sema3F proteins are candidate tumor suppressors that are down-regulated in highly metastatic tumors. Two receptor families, the neuropilins and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3F is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200515 [Multi-domain]  Cd Length: 470  Bit Score: 190.42  E-value: 7.26e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       81 DCENYITLLE--RRSEgLLACGTNARHPSC-------------WNLVNGTVVPlgeMRGYAPFSPDENSLVLFEGDEVYS 145
Cdd:cd11254  67 ECGNFIRLIQpwNRTH-LYVCGTGAYNPVCayinrgrraedymFRLEPDKLES---GKGKCPYDPKQDSVSALINGELYA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      146 TIRKqEYNGKIPRFRRIRGE-----SELYTSdTVMQNPQFIKATIVhQDQAY--DDKIYYFFREDNPDkNPEAPLNVSRV 218
Cdd:cd11254 143 GVYI-DFMGTDAAIFRTMGKqpamrTDQYNS-RWLNDPAFVHAHLI-PDSSEknDDKLYFFFREKSLE-APQSPAVLSRI 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      219 AQLCRGDQGGESSLsVSKWNTFLKAMLVCS---DAATNKNFNRLQDVFLLPDpsgqwRDTR---VYGVFSNP---WNYSA 289
Cdd:cd11254 219 GRVCLNDDGGHCCL-VNKWSTFLKARLVCSvpgADGIETHFDELRDVFIQPT-----QDTKnpvIYAVFSTSgsvFKGSA 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      290 VCVYSLGDIDKVFR---------TSSLKGYHSSLPNPRPGKC--------LPDQQPIPTETFQVADRHPEVAQRVEPMGp 352
Cdd:cd11254 293 VCVYSMADIRMVFNgpfahkegpNYQWMPYTGKIPYPRPGTCpggtftpsMKSTKDYPDEVINFMRTHPLMYNAVYPVH- 371
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      353 lKTPLF---HSKYHYQKVAVHRMQASHGEtFHVLYLTTDRGTIHKV-VEPGEQEHSFAFNIMEIQPFRRAAAIQTMSLDA 428
Cdd:cd11254 372 -RRPLVvrtNVNYRFTTIAVDQVDAADGR-YEVLFLGTDRGTVQKViVLPKDDLETEELTLEEVEVFKVPAPIKTMKISS 449
                       410       420
                ....*....|....*....|.
3NVQ_A      429 ERRKLYVSSQWEVSQVPLDLC 449
Cdd:cd11254 450 KRQQLYVSSAVGVTHLSLHRC 470
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
42-449 2.84e-49

The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a transmembrane protein. It has been shown to mediate the defasciculation of motor axon bundles at specific choice points. Sema1A binds to its receptor plexin A (PlexA), which in turn triggers downstream signaling events involving the receptor tyrosine kinase Otk, the evolutionarily conserved flavoprotein monooxygenase molecule interacting with CasL (MICAL), and the A kinase anchoring protein Nervy, leading to repulsive growth-cone response. Sema1A has also been shown to be involved in synaptic formation. It is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200498 [Multi-domain]  Cd Length: 446  Bit Score: 177.14  E-value: 2.84e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       42 SVWVGGRGKVY---LFDFPEGK----NASVRTVNIGSTKGSclDKRDCENYITLLERRSEG-LLACGTNARHPSC--WNL 111
Cdd:cd11237  16 SLLVGARNAVYnisLSDLTENQriewPSSDAHREMCLLKGK--SEDDCQNYIRVLAKKSAGrLLVCGTNAYKPLCreYTV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      112 VNGTVVPLGEM--RGYAPFSPDENSLVLFEGDEVYS-TIrkQEYNGKIPRFRRIRGESELYTSdTVMQNPQFIKATivhq 188
Cdd:cd11237  94 KDGGYRVEREFdgQGLCPYDPKHNSTAVYADGQLYSaTV--ADFSGADPLIYREPLRTERYDL-KQLNAPNFVSSF---- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      189 dqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTFLKAMLVCS-DAATNKNFNRLQDVF-LLP 266
Cdd:cd11237 167 --AYGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFR-DRWTSFLKARLNCSvPGEYPFYFNEIQSTSdIVE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      267 DPSGQWRDTRVYGVFSNPWNY---SAVCVYSLGDIDKVFRTSSLK---------GYHSS-LPNPRPGKCLPDQQPIPTET 333
Cdd:cd11237 244 GGYGGKSAKLIYGVFTTPVNSisgSAVCAFSLQDILEVFDGSFKEqqdinsnwlPVPSNkVPEPRPGQCVNDSRTLPDVT 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      334 FQVADRHPEVAQRVepmgplktPLFHSK---------YHYQKVAVH-RMQASHGETFHVLYLTTDRGTIHKVVEPGEQEH 403
Cdd:cd11237 324 VNFIKSHPLMDEAV--------PSFFGRpilvrtslqYRFTQIAVDpQVKALDGKYYDVLFIGTDDGKVLKAVNIASADT 395
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
3NVQ_A      404 SF---AFNIMEIQPFRRAAAIQTMSL--DAERRKLYVSSQWEVSQVPLDLC 449
Cdd:cd11237 396 VDkvsPVVIEETQVFPRGVPIRNLLIvrGKDDGRLVVVSDDEIVSIPLHRC 446
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
82-449 1.10e-48

The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted semaphorin expressed in and adjacent to cardiac neural crest cells, and causes impaired migration of neural crest cells to the developing cardiac outflow tract, resulting in the interruption of the aortic arch and persistent truncus arteriosus. It has been proposed that Sema3C acts as a guidance molecule, regulating migration of neural crest cells that express semaphorin receptors such as plexin A2. Sema3C may also participate in tumor progression. The cleavage of Sema3C induced by ADAMTS1 promotes the migration of breast cancer cells. Sema3C is a member of the class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200512 [Multi-domain]  Cd Length: 470  Bit Score: 176.23  E-value: 1.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       82 CENYITLLERRSEG-LLACGTNARHPSCwNLVNGTVVPLGEM----------RGYAPFSPDENSLVLFEGDEVYSTIRKQ 150
Cdd:cd11251  68 CGNFVRVIQPYNRThLYVCGSGAFSPVC-VYVNRGRRSEEQVfhidskaesgKGRCSFNPNVNTVSVMINEELFSGMYID 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      151 EYNGKIPRFRRIRGESELYT---SDTVMQNPQFIKATIVHQ-DQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQ 226
Cdd:cd11251 147 FMGTDAAIFRSLTKRNAVRTdqhNSKWLSEPIFVDAHLIPDgTDPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDT 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      227 GGESSLsVSKWNTFLKAMLVCS---DAATNKNFNRLQDVFLLPdpSGQWRDTRVYGVF---SNPWNYSAVCVYSLGDIDK 300
Cdd:cd11251 227 GGQRSL-VNKWTTFLKARLVCSvmdEDGTETHFDELEDVFLLE--TDNPRTTLVYGIFttsSSVFKGSAVCVYHMSDIQT 303
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      301 VFR---------TSSLKGYHSSLPNPRPGKC-----LPDQQP---IPTETFQVADRHPEVAQRVEPMGplKTPLF---HS 360
Cdd:cd11251 304 VFNgpfahkegpNHQLIAYQGRIPYPRPGTCpggafTPNMQStkeFPDDVVTFIRNHPLMFNPIYPIG--RRPLLvrtGT 381
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      361 KYHYQKVAVHRMQASHGEtFHVLYLTTDRGTIHKV-VEPGEQEHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQW 439
Cdd:cd11251 382 DYKYTKIAVDRVNAADGR-YHVLFLGTDKGTVQKVvVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEE 460
                       410
                ....*....|
3NVQ_A      440 EVSQVPLDLC 449
Cdd:cd11251 461 GISQVSLHRC 470
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
32-449 2.64e-47

The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted semaphorin expressed during the development of the nervous system. In zebrafish, Sema3D is expressed in the ventral tectum. It guides retinal axons along the dorsoventral axis of the tectum and guides the laterality of retinal ganglion cell (RGC) projections. Both Sema3D knockdown or its ubiquitous overexpression induced aberrant ipsilateral projections. Proper balance of Sema3D is needed at the midline for the progression of RGC axons from the chiasm midline into the contralateral optic tract. Sema3D is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200513 [Multi-domain]  Cd Length: 474  Bit Score: 172.40  E-value: 2.64e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       32 TVLFHEPgSSSVWVGGRGKVYLFDfPEGKNASVRTVNIGSTKGSC-LDKR-------DCENYITLLERRSEG-LLACGTN 102
Cdd:cd11252  12 TLLLDEE-RGRLLLGAKDHIYLLD-LVDLNKNPKKIYWPAAKERVeLCKLagkdantECANFIRVLHPYNRThVYVCGTG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      103 ARHPSC------------WNLVNGTVVPLGEMRgyAPFSPDENSLVLFEGDEVYSTIrKQEYNGKIPRFRRIRGESELY- 169
Cdd:cd11252  90 AFHPTCgyielgthkedrIFLLDTQNLESGRLK--CPFDPQQPFASVMTDEYLYAGT-ASDFLGKDTTFTRSLGPTPDHh 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      170 ------TSDTVMQNPQFIKA-TIVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLsVSKWNTFLK 242
Cdd:cd11252 167 yirtdiSEHYWLNGAKFIGTfPIPDTYNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSL-INKWTTFLK 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      243 AMLVCS----DAAtNKNFNRLQDVFLLPDpsgqwRDTR---VYGVF---SNPWNYSAVCVYSLGDIDKVFRTSSLKG--- 309
Cdd:cd11252 246 ARLVCSipgpDGA-DTHFDELQDIFLLPT-----RDERnpvVYGVFtttSSIFKGSAVCVYSMADIRAVFNGPYAHKesp 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      310 ------YHSSLPNPRPGKC--------LPDQQPIPTETFQVADRHPEVAQRVEPM--GPLKTPLfHSKYHYQKVAVHRMQ 373
Cdd:cd11252 320 dhrwvqYEGRIPYPRPGTCpsktydplIKSTKDFPDEVISFIKRHPLMYKSVYPLtgGPVFTRI-NVDYRLTQIVVDHVA 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3NVQ_A      374 ASHGEtFHVLYLTTDRGTIHKVVEPGEQEHSFAFNIM-EIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPLDLC 449
Cdd:cd11252 399 AEDGQ-YDVMFLGTDIGTVLKVVSITKEKWTMEEVVLeELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
27-445 3.94e-47

The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in heterotypic cell-cell contacts and controls cell proliferation and suppresses tumorigenesis. In neurofibromatosis type 1 (NF1) patients, reduced Sema4F level disrupts Schwann cell/axonal interactions. Experiments using a yeast two-hybrid system show that the extreme C-terminus of Sema4F interacts with the PDZ domains of post-synaptic density protein SAP90/PSD-95, indicating possible functional involvement of Semas4F at glutamatergic synapses. Recent work also suggests a role for Sema4F in the injury response of intramedullary axotomized motoneuron. Sema4F belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulator molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200522 [Multi-domain]  Cd Length: 460  Bit Score: 171.61  E-value: 3.94e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       27 QTEPHTVLFHEPGSSSVWVGGRGKVYLFDFP--EGKNASVRTVNIGSTKGSCLDK----RDCENYITLLE-RRSEGLLAC 99
Cdd:cd11261  10 HTYNYSVLLVDPASHTLYVGARDAIFALTLPfsGERPRRIDWMVPEAHRQNCRKKgkkeAECHNFIRILAiANASHLLTC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      100 GTNARHPSCWNLVNGT---VVPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRKQeYNGKIPRFRRIRGESELY----TSD 172
Cdd:cd11261  90 GTFAFDPKCGVIDVSSfqqVERLESGRGKCPFEPAQRSAAIMAGGVLYAATVKN-FLGTEPIISRAVGRAEEWirteTLP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      173 TVMQNPQFIKATIVHQ----DQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTFLKAMLVCS 248
Cdd:cd11261 169 SWLNAPAFVAAVFLSPaewgDEDGDDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTLQ-QRWTTFLKADLLCP 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      249 DAATNKNFNRLQDVFLLPDPSGQwRDTRVYGVFSNPWN---YSAVCVYSLGDIDKV-------FRTSSLKGY---HSSLP 315
Cdd:cd11261 248 GPEHGRASSILQDVTTLRPLPGA-GTPIFYGIFSSQWEgasISAVCAFRPQDIRRVmngpfreFKHDCNRGLpvmDSDVP 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      316 NPRPGKCLPDQQ---------PIPTETFQVADRHPEVAQRVEPM--GPLktpLFHSKYHYQKVAVHRMQASHGETFHVLY 384
Cdd:cd11261 327 QPRPGECITNNMkllgfgsslSLPDRVLTFVRDHPLMDRPVFPAdgHPL---LVTTDTAYLRVAAHRVTSLSGKEYDVLY 403
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3NVQ_A      385 LTTDRGTIHKVVEPGEQehsfaFNIME-IQPFRRAAAIQTMSLdaERRKLYVSSQWEVSQVP 445
Cdd:cd11261 404 LGTEDGHLHRAVRIGAQ-----LSVLEdLALFPEPQPVENLQL--HHNWLLVGSDTEVTQIN 458
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
81-449 1.49e-46

The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is identified as a primarily endothelial cell- expressed class 3 semaphorin that controls endothelial and smooth muscle cell functions in autocrine and paracrine manners, respectively. It is mainly expressed in the lung and kidney, and a little in the brain. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200516 [Multi-domain]  Cd Length: 474  Bit Score: 170.48  E-value: 1.49e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       81 DCENYITLLE--RRSEgLLACGTNARHPSCwNLVNgtVVPLGEM------------RGYAPFSPDENSLVLFEGDEVYST 146
Cdd:cd11255  67 ECANFVRVLQpfNRTH-LLACGTGAFQPVC-ALIN--VGHRGEHvfsldpttvesgRGRCPHEPKRPFASTFTGGELYTG 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      147 IrKQEYNGKIPRFRRIRGESELYTSDT---VMQNPQFIKATIV-HQDQAYDDKIYYFFREDNPDknPEAPLN---VSRVA 219
Cdd:cd11255 143 L-TADFLGRDSVIFRGFGTRSPLRTETdqrLLHEPRFVAAHLIpDNADRDNDKVYFFFTERATE--TAEDDDgaiHSRVG 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      220 QLCRGDQGGESSLsVSKWNTFLKAMLVCS---DAATNKNFNRLQDVFLLPDPSGqwRDTRVYGVFS---NPWNYSAVCVY 293
Cdd:cd11255 220 RLCANDAGGQRVL-VNKWSTFIKARLVCSvpgPHGIQTHFDQLEDVFLLRTKDG--KSPEIYALFStisNVFQGFAVCVY 296
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      294 SLGDIDKVFR---------TSSLKGYHSSLPNPRPGKClPDQ---QP---------IPTETFQVADRHPEVAQRVEPMGp 352
Cdd:cd11255 297 SMADIWEVFNgpfahkdgpDHQWGPYEGKVPYPRPGVC-PSKitaQPgrafrstkdYPDEVLQFARAHPLMWRPVYPSH- 374
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      353 lKTPLF---HSKYHYQKVAVHRMQASHGeTFHVLYLTTDRGTIHKVVEPGEQEHSFAFNIM--EIQPFRRAAAIQTMSLD 427
Cdd:cd11255 375 -RRPVLvktGLPYRLTQIVVDRVEAEDG-YYDVMFIGTDSGSVLKVIVLQKGNSAAGEEVTleELQVFKVPTPITEMEIS 452
                       410       420
                ....*....|....*....|..
3NVQ_A      428 AERRKLYVSSQWEVSQVPLDLC 449
Cdd:cd11255 453 VKRQMLYVGSRTGVAQVPLHRC 474
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
45-446 2.31e-46

The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed in the epithelial cells that line the pharyngeal arches in zebrafish. It may act as a guidance molecule to restrict the branchiomotor axons to the mesenchymal cells. Gain-of-function and loss-of-function studies demonstrate that Sema4E is essential for the guidance of facial axons from the hindbrain into their pharyngeal arch targets and is sufficient for guidance of gill motor axons. Sema4E guides facial motor axons by a repulsive action. Sema4E belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200521 [Multi-domain]  Cd Length: 456  Bit Score: 169.32  E-value: 2.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       45 VGGRGKVYLFDFPE--GKNASVRTVNIGSTKGSCLDK-----RDCENYITLLERRSEGLL-ACGTNARHPSCWNLV--NG 114
Cdd:cd11260  23 LGAREAVFALDLNDisVKRAKVLWEVTEEKQKDCTNKgkhadIDCHNYIRILHKMNDSRMyVCGTNAFSPTCDYISydDG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      115 TVVPLGEM---RGYAPFSPDENSLVLFEGDEVYSTIrKQEYNGKIPRFRRIRGES--ELYTSdTVMQNPQFIKATIVHQD 189
Cdd:cd11260 103 QLTLEGKQedgKGKCPFDPFQRYSSVMVDQDLYSAT-SMNFLGSEPVIMRSSPITirTEFKS-SWLNEPNFIYMAAVPES 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      190 QAY----DDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTFLKAMLVCSDAATNKNFnRLQDVF-L 264
Cdd:cd11260 181 EDSpegdDDKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQ-KKWTSFLKARLDCSVPEPSLPY-VIQDVFhV 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      265 LPDpsgQWRDTRVYGVF---SNPWNYSAVCVYSLGDIDKVF-----------RTSSLK--GYHSSLPNPRPGKCLPDQQ- 327
Cdd:cd11260 259 CHQ---DWRKCVFYAVFtsqSDSSQSSAVCAYNVTDISNVFsrgkfktpvavETSFVKwvMYSGELPVPRPGACINNAAr 335
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      328 --------PIPTETFQVADRHPEVAQRVEPMG--PL---KTPLFhskyhyQKVAVHRMQASHGETFHVLYLTTDRGTIHK 394
Cdd:cd11260 336 tsgikkslNLPDKTLQFVKDKPLMDQAVHPITgkPLlvkRGALF------TRIVVDMVTAADGQSYPVMFIGTANGYVLK 409
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
3NVQ_A      395 VVE-PGEQehsfaFNIMEIQPFRRAAAIQTMSLdaERRKLYVSSQWEVSQVPL 446
Cdd:cd11260 410 AVNyDGEM-----HIIEEVQLFEPEEPIDILRL--SQNQLYAGSASGVVQMPV 455
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
259-427 2.75e-46

Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor and Swiss:P51805


Pssm-ID: 460197 [Multi-domain]  Cd Length: 180  Bit Score: 160.90  E-value: 2.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A        259 LQDVFLLPDPSGQWRDTRVYGVFS----NPWNYSAVCVYSLGDIDKVFR---------TSSLKGYHSSLPNPRPGKCLPD 325
Cdd:pfam01403   1 LQDVFVLKPGAGDALDTVLYGVFTtqwsNSIGGSAVCAFSLSDINAVFEgpfkeqeksDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A        326 --QQPIPTETFQVADRHPEVAQRVEPMGplKTPLFHSK-YHYQKVAVHRMQASHGEtFHVLYLTTDRGTIHKVVEPGEQE 402
Cdd:pfam01403  81 plRLDLPDSVLNFVKDHPLMDEAVQPVG--GRPLLVRTgVRLTSIAVDRVQALDGN-YTVLFLGTDDGRLHKVVLVGSEE 157
                         170       180
                  ....*....|....*....|....*
3NVQ_A        403 hsfAFNIMEIQPFRRAAAIQTMSLD 427
Cdd:pfam01403 158 ---SHIIEEIQVFPEPQPVLNLLLS 179
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
25-449 6.19e-44

The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted molecule implicated in axonal path finding and inhibition of developmental and postischemic angiogenesis. It is also highly expressed in metastatic cancer cells. Sema3E signaling, through its high affinity functional receptor Plexin D1, drives cancer cell invasiveness and metastatic spreading. Sema3E is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200514 [Multi-domain]  Cd Length: 471  Bit Score: 163.10  E-value: 6.19e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       25 FGQTEPHTVLFHEPgSSSVWVGGRGKVYLFDFpEGKNASVRTVNIGSTK---GSCL----DKRDCENYITLLER-RSEGL 96
Cdd:cd11253   5 FGFLDLHTMLLDEY-QERLFVGGRDLLYSLSL-ERISANYKEIHWPSTQlqvEDCImkgrDKPECANYIRVLHHyNRTHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       97 LACGTNARHPSCW--NLVNGTVVPLGEM--------RGYAPFSPDENSLVLFEGDEVYSTIRKQEYNGKIPRFRRIRGES 166
Cdd:cd11253  83 LACGTGAFDPVCAfiRVGRGSEDHLFQLesdkfergRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMNHLA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      167 ELYT---SDTVMQNPQFI-KATIVHQDQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLsVSKWNTFLK 242
Cdd:cd11253 163 HIRTehdDERLLKEPKFVgSYMIPDNEDPDDNKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRML-VNKWSTFLK 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      243 AMLVCSDAATN---KNFNRLQDVFLLPDpsgqwRDTR---VYGVF---SNPWNYSAVCVYSLGDIDKVFR---------T 304
Cdd:cd11253 242 TRLICSVPGPNgidTHFDELEDVFLLRT-----RDNKnpeIFGLFsttSNIFKGYAICVYHMASIRAAFNgpfahkegpE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      305 SSLKGYHSSLPNPRPGKC--------LPDQQPIPTETFQVADRHPEVAQRVEPMGplKTPLF---HSKYHYQKVAVHRMQ 373
Cdd:cd11253 317 YHWSVYEGKVPYPRPGSCaskvngghYGTTKDYPDEALRFARSHPLMYQAVKPVH--KRPILvktDGKYNLKQIAVDRVE 394
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3NVQ_A      374 ASHGEtFHVLYLTTDRGTIHKVVEPGEQEHSFAFNIM--EIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPLDLC 449
Cdd:cd11253 395 AEDGQ-YDVLFIGTDNGIVLKVITIYNQETETMEEVIleELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
81-446 1.08e-43

The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a Plexin B2 ligand to regulate the development of cerebellar granule cells and to modulate ureteric branching in the developing kidney. The binding of Sema4C to Plexin B2 results the phosphorylation of downstream regulator ErbB-2 and the plexin protein itself. The cytoplasmic region of Sema4C binds a neurite-outgrowth-related protein SFAP75, suggesting that Sema4C may also play a role in neural function. Sema4C belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200519 [Multi-domain]  Cd Length: 458  Bit Score: 162.28  E-value: 1.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       81 DCENYITLLER-RSEGLLACGTNARHPSCW--NLVNGTV--VPLGEMRGYAPFSPDENSLVLFEGDEVYSTIRkqeYN-- 153
Cdd:cd11258  68 ECFNYIRFLQPyNQSHLYTCGTYAFQPKCAyiNMLTFTLdrAEFEDGKGKCPYDPAKGHTGLIVDGELYSATL---NNfl 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      154 GKIPRFRRIRGESELYTSD---TVMQNPQFIKATIVHQ----DQAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQ 226
Cdd:cd11258 145 GTEPVILRNLGQHYSMKTEylaFWLNEPHFVGSAFVPEsvgsFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDL 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      227 GGESSLSvSKWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSgqWRDTRVYGVFSNPW---NYSAVCVYSLGDIDKVF- 302
Cdd:cd11258 225 GGARTLQ-KKWTTFLKARLLCSIPEWQLYFNQLKAVFTLEGAS--WRNTTFFAVFQARWgdmDVSAVCEYQLGEIQQVFe 301
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      303 ------RTSSLK--GYHSSLPNPRPGKCLPD---------QQPIPTETFQVADRHPEVAQRVEPMGPlkTPLFHSK-YHY 364
Cdd:cd11258 302 gpykeySEQAQKwgRYTDPVPSPRPGSCINNwhrdhgytsSLELPDNTLNFVKKHPLMEDRVKPRLG--RPLLVPCnSNF 379
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      365 QKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPGeqehSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQV 444
Cdd:cd11258 380 THVVWTRVLGLDGETYSVLFIGTLDGWLIKAVSLG----SWVHMIEELQVFDQEPPESLVVSQSSKKLLFAGSRSELLQL 455

                ..
3NVQ_A      445 PL 446
Cdd:cd11258 456 PW 457
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
33-446 1.44e-40

The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted semaphorin, signals through its receptor plexin B (PlexB) to regulate central and peripheral axon pathfinding. In the Drosophila embryo, Sema2A secreted by oenocytes interacts with PlexB to guide sensory axons. Sema2A is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200499 [Multi-domain]  Cd Length: 452  Bit Score: 153.35  E-value: 1.44e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       33 VLFHEPGSSSVWVGGRGKVYLFdfpegkNASvrtvNIGSTKGSCLDK--------------------RDCENYITLLERR 92
Cdd:cd11238   5 TLLLDEKRNALYVGAMDRVFRL------NLY----NINDTGNNCARDeltlspsdvsecvskgkdeeYECRNHVRVIQPM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       93 SEG--LLACGTNARHPSCW-----NLVNGTVVPLGEMR-GYAPFSPDENSL-VLFE----GD--EVYSTIRKqEYNG--- 154
Cdd:cd11238  75 GDGqtLYVCSTNAMNPKDRvldanLLHLPEYVPGPGNGiGKCPYDPDDNSTaVWVEwgnpGDlpALYSGTRT-EFTKant 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      155 ---KIPRFRRIRGESE-----LYTSDTVMQNPQFIKATIVhqdqayDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQ 226
Cdd:cd11238 154 viyRPPLYNNTKGRHEsfmrtLKYDSKWLDEPNFVGSFDI------GDYVYFFFRETAVEYINCGKVVYSRVARVCKKDT 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      227 GGESSLSvSKWNTFLKAMLVCSDAATNK-NFNRLQDVFLLPDPSgqwrDTRVYGVFSNPWNY---SAVCVYSLGDIDKVF 302
Cdd:cd11238 228 GGKNVLR-QNWTTFLKARLNCSISGEFPfYFNEIQSVYKVPGRD----DTLFYATFTTSENGftgSAVCVFTLSDINAAF 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      303 RTSSLKGYHSSL-----------PNPRPGKCLPDQQPIPTETFQVADRHPEVAQRVEPMGPLktpLFHSKYHYQKVAVHR 371
Cdd:cd11238 303 DTGKFKEQASSSsawlpvlssevPEPRPGTCVNDSATLSDTVLHFARTHPLMDDAVSHGPPL---LYLRDVVFTHLVVDK 379
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3NVQ_A      372 MQASHGEtFHVLYLTTDRGTIHKVVEPGEQEHSFAfNIMEIQPFRRAAAIQTMSLdAERRKLYVSSQWEVSQVPL 446
Cdd:cd11238 380 LRIDDQE-YVVFYAGSNDGKVYKIVHWKDAGESKS-NLLDVFELTPGEPIRAMEL-LPGEFLYVASDHRVSQIDL 451
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
33-469 1.97e-38

The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed in immune cells and is thus termed an "immune semaphorin". It plays critical roles in T cell-DC interactions in the immune response. It has been reported to enhance activation and differentiation of T cells in vitro and generation of antigen-specific T cells in vivo. The function of Sema4A in the immune response implicates its role in infectious and noninfectious diseases. Sema4A exerts its function through three receptors, namely Plexin B, Plexin D1, and Tim-2. Sema4A belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. TThe Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200517 [Multi-domain]  Cd Length: 447  Bit Score: 146.98  E-value: 1.97e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       33 VLFHEPGSSSVWVGGRGKVYLFDFpeGKNASVRTVNI------GSTKGSCLDKR-----DCENYITLLERRSEG-LLACG 100
Cdd:cd11256  12 QLLLSPDETTLYVGARDNILALGI--RTPGPIRLKHQipwpanDSKISECAFKKksnetECFNFIRVLVPVNGThLYTCG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      101 TNARHPSCW--NLVNGTVVPLG------EMRGYAPFSPDENSLVLFEGDEVYSTIRKQeYNGKIPRFRRIRGeselytSD 172
Cdd:cd11256  90 TYAFSPACTyiELDHFSLPPPNgtiitmDGKGQSPFDPQHNYTAILVDGELYTGTMNN-FRGNEPIIFRNLG------TK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      173 TVMQNPQFIKAtiVHQDQAY--------DDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTFLKAM 244
Cdd:cd11256 163 VSLKTDGFLRW--LNADAVFvasfnpqgDSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQ-KKWTTFLKAQ 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      245 LVCSDAAtNKNFNRLQDVFLLPDPSgqwrDTR--VYGVFSNPWNY-----SAVCVYSLGDIDKVFR---------TSSLK 308
Cdd:cd11256 240 LTCSQQG-HFPFNVIHHVALLNQPD----PNNsvFYAVFTSQWQLggrrsSAVCAYKLNDIEKVFNgkykelnkeSSRWT 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      309 GYHSSLPNPRPGKClpDQQPIPTETFQVADRHPEVAQRVEPMGplKTPLF-HSKYHYQKVAVHRMQASHGETFHVLYLTT 387
Cdd:cd11256 315 RYMGPVSDPRPGSC--SGGKSSDKALNFMKDHFLMDEVVLPGA--GRPLLvKSNVQYTRIAVDSVQGVSGHNYTVMFLGT 390
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      388 DRGTIHKVVEPGEQEhsfafnimeiqpfrraaaiqtmsldaerrkLYVSSQWEVSQVPLDLCEVYGGGCHGCLMSRDPYC 467
Cdd:cd11256 391 DKGFLHKAVLMGGSE------------------------------SHIIEEIELLTPPEPVENLLLAANEGVVYIGYSAG 440

                ..
3NVQ_A      468 GW 469
Cdd:cd11256 441 VW 442
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
42-446 1.36e-37

The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 semaphorins (Sema6s) are membrane associated semaphorins. There are 6 subfamilies named 6A to 6D. Sema6s bind to plexin As in a neuropilin independent fashion. Sema6-plexin A signaling plays important roles in lamina-specific axon projections. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. Interactions between Sema6C, Sema6D and plexin A1 shape the stereotypic trajectories of sensory axons in the spinal cord. In addition to axon targeting, Sema6D-plexin A1 interactions influence a wide range of other biological processes. During cardiac development, Sema6D attracts or repels endothelial cells in the cardiac tube depending on the expression patterns of specific coreceptors in addition to plexin A1. Furthermore, Sema6D binds a receptor complex comprising of plexin A1, Trem2 (triggering receptor expressed on myeloid cells 2), and DAP12 on dendritic cells and osteoclasts to mediate T-cell-DC interactions and to control bone development, respectively. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200503 [Multi-domain]  Cd Length: 465  Bit Score: 144.97  E-value: 1.36e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       42 SVWVGGRGKVYLFDFPEGKNASVR------------TVNIGSTKGSCLDkrDCENYI-TLLERRSEGLLACGTNARHPSC 108
Cdd:cd11242  20 TLYIAARDHVYTVDLDASHTEEIVpskkltwrsrqaDVENCRMKGKHKD--ECHNFIkVLVPRNDETLFVCGTNAFNPVC 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      109 WNLVNGTVVPLG-EMRGYA--PFSPDENSLVLFEGDEVYST-------IRKQEYN--GKIPRFRRIRGESELytsdtvMQ 176
Cdd:cd11242  98 RNYRIDTLEQDGeEISGMArcPFDAKQANVALFADGKLYSAtvtdflaSDAVIYRslGDSPTLRTVKYDSKW------LK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      177 NPQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCS-DAATNKN 255
Cdd:cd11242 172 EPHFVHAV------EYGDYVYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGSPRVLEKQWTSFLKARLNCSvPGDSHFY 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      256 FNRLQDVFLLPDPSGqwRDTrVYGVFSNPWNY---SAVCVYSLGDIDKVFrTSSLKGYHSS-----------LPNPRPGK 321
Cdd:cd11242 246 FDVLQAVTDVIRING--RPV-VLGVFTTQYNSipgSAVCAFDMDDIEKVF-EGRFKEQKSPdsawtpvpedrVPKPRPGC 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      322 CLPD--------QQPIPTETFQVADRHPEVAQRVEPMGplKTPLF---HSKYHYQKVAVHRMQASHGeTFHVLYLTTDRG 390
Cdd:cd11242 322 CAGSgsaekyktSNDFPDDTLNFIKTHPLMDEAVPSII--NRPWFtrtMVRYRLTQIAVDNAAGPYQ-NYTVVFLGSEAG 398
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3NVQ_A      391 TIHKVVEPGeqeHSFAFN----IMEIQPFRRAAA---------IQTMSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11242 399 TVLKFLARI---GPSGSNgsvfLEEIDVYNPAKCsydgeedrrIIGLELDRASHALFVAFSGCVIRVPL 464
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
20-446 1.45e-37

The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse Sema5A was identified as a protein that induces inhibitory responses during optic nerve development. Recent studies show that Sema5A controls innate immunity in mice. It also has been identified as a candidate gene for causing idiopathic autism in humans. Plexin B3 functions as a binding partner and receptor for Sema5A. Furthermore, Sema5A is also implicated in cancer. The role of the Drosophila Sema5A ortholog, Dsema-5C, in tumorigenicity and metastasis has been reported. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Sema5A belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200524 [Multi-domain]  Cd Length: 436  Bit Score: 144.40  E-value: 1.45e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       20 QDRVDFGQtephtvLFHEPGSSSVWVGGRGkvYLFDFPEGKNASVRTVNIG---STKGSCLDK----RDCENYITLLERR 92
Cdd:cd11263   4 ENAVDFSQ------LTFDPGQKELIVGARN--YLFRLQLEDLSLIQAVEWEcdeATKKACYSKgkskEECQNYIRVLLVG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       93 SEGLLACGTNARHPSCWN--LVNGTVVPlGEMRGYA--PFSPDENSLVLFEGD-EVYSTIrKQEYNGKIPRFRRIRG--- 164
Cdd:cd11263  76 GDRLFTCGTNAFTPICTNrtLNNLTEIH-DQISGMArcPYSPQHNSTALLTSSgELYAAT-AMDFPGRDPAIYRSLGilp 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      165 --ESELYTSDTvMQNPQFIkativhqdQAYD--DKIYYFFREdNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTF 240
Cdd:cd11263 154 plRTAQYNSKW-LNEPNFV--------SSYDigNFTYFFFRE-NAVEHDCGKTVFSRAARVCKNDIGGRFLLE-DTWTTF 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      241 LKAMLVCSDAATNK-NFNRLQDVFLLPDPSgqwrdtRVYGVFSNPWN---YSAVCVYSLGDIDKVFrTSSLKGYHSS--- 313
Cdd:cd11263 223 MKARLNCSRPGEIPfYYNELQSTFFLPELD------LIYGIFTTNVNsiaASAVCVFNLSAISQAF-NGPFKYQENSrsa 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      314 ---LPNPRPG-KCLPDQQPIpteTFQVADRHPEVAQR-------VEPMGPLktPLF-HSKYHYQKVAVHRMQASHgETFH 381
Cdd:cd11263 296 wlpYPNPNPNfQCGTMDQGL---YVNLTERNLQDAQKfilmhevVQPVTPV--PYFmEDNSRFSHVAVDVVQGKD-MLFH 369
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3NVQ_A      382 VLYLTTDRGTIHKVVEPGEQ-EHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11263 370 IIYLATDYGTIKKVLAPLNQsSSSCLLEEIELFPKRQREPIRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
37-446 7.84e-37

The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. There are three subfamilies in class 5 semaphorins, namely 5A, 5B and 5C. Sema5A and Sema5B function as guidance cues for optic and corticofugal nerve development, respectively. Sema5A-induced cell migration requires Met signaling. Sema5C is an early development gene and may play a role in odor-guided behavior. Sema5A is also implicated in cancer. In a screening model for metastasis, the Drosophila Sema5A ortholog, Dsema-5C, has been found to be required in tumorigenicity and metastasis. Sema5A is highly expressed in human pancreatic cancer cells and is associated with tumor growth, invasion and metastasis. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200502 [Multi-domain]  Cd Length: 438  Bit Score: 142.31  E-value: 7.84e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       37 EPGSSSVWVGGRGkvYLFDFPEGKNASVRTVNIGS---TKGSCLDK----RDCENYITLLERRSEGLLACGTNARHPSC- 108
Cdd:cd11241  15 DPTHDQLIVGARN--YLFRLRLQSLSLLQAVPWNSdedTKRQCQSKgksvEECQNYVRVLLVVGKNLFTCGTYAFSPVCt 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      109 WNLVNGTVVPLGEMRGYA--PFSPDENSLVLFEGD-EVYSTIrKQEYNGKIPR-FRRIRGESELYT---SDTVMQNPQFI 181
Cdd:cd11241  93 IRKLSNLTQILDTISGVArcPYSPAHNSTALISASgELYAGT-VYDFSGRDPAiYRSLGGKPPLRTaqyNSKWLNEPNFV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      182 KAtivhqdqaYD--DKIYYFFREdNPDKNPEAPLNV-SRVAQLCRGDQGGESSLSvSKWNTFLKAMLVCSDAATNK-NFN 257
Cdd:cd11241 172 GS--------YEigNHTYFFFRE-NAVEHQDCGKTVySRIARVCKNDIGGRFLLE-DTWTTFMKARLNCSLPGEFPfYYN 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      258 RLQDVFLLPDpsgqwRDTrVYGVFSNPWNY---SAVCVYSLGDIDKVF-----RTSSLKGYHSSLPNPRPGKC----LPD 325
Cdd:cd11241 242 EIQGTFYLPE-----TDL-IYAVFTTNVNGiagSAICAFNLSAINQAFngpfkYQENNGSAWLPTPNPHPNFQcttsIDR 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      326 QQPIPTETFQVADrhpevAQRVEPMGPLKTPLFHSKYH------YQKVAVHRMQASHGETFHVLYLTTDRGTIHKVVEPG 399
Cdd:cd11241 316 GQPANTTERDLQD-----AQKYQLMAEVVQPVTKIPLVtmddvrFSKLAVDVVQGRGTQLVHIFYVGTDYGTILKMYQPH 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
3NVQ_A      400 EQEHSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11241 391 RSQKSCTLEEIKILPAMKGEPITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
79-446 5.57e-32

The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, Sema6A-plexin A2 signaling modulates granule cell migration by controlling centrosome positioning. Besides plexin A2, plexin A4 is also found to be a receptor of Sema6A. Interactions between plexin A2, plexin A4, and Sema6A control lamina-restricted projection of hippocampal mossy fibers. It is required for the clustering of boundary cap cells at the PNS/CNS interface and thus, prevents motoneurons from streaming out of the ventral spinal cord. At the dorsal root entry site, it organizes the segregation of dorsal roots. Sema6A may also be involved in axonal pathfinding processes in the periinfarct and homotopic contralateral cortex. Sema6A is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200527 [Multi-domain]  Cd Length: 466  Bit Score: 128.99  E-value: 5.57e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       79 KRDCENYITLLERRSEG-LLACGTNARHPSCWNLVNGTVVPLG-EMRGYA--PFSPDENSLVLFEGDEVYST-------I 147
Cdd:cd11266  67 KDECHNFIKVLLKRNDDtLFVCGTNAFNPSCRNYKMDTLEFFGdEFSGMArcPYDAKHANVALFADGKLYSAtvtdflaI 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      148 RKQEYN--GKIPRFRRIRGESELytsdtvMQNPQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGD 225
Cdd:cd11266 147 DAVIYRslGDSPTLRTVKHDSKW------LKEPYFVQAV------DYGDYIYFFFREIAVEYNSMGKVVFPRVAQVCKND 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      226 QGGESSLSVSKWNTFLKAMLVCS-DAATNKNFNRLQDVFLLPDPSGqwRDTrVYGVFSNPWNY---SAVCVYSLGDIDKV 301
Cdd:cd11266 215 MGGSQRVLEKQWTSFLKARLNCSvPGDSHFYFNILQAVTDVIHING--RDV-VLATFSTPYNSipgSAVCAYDMLDIASV 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      302 FrTSSLKGYHS-----------SLPNPRPGKC--------LPDQQPIPTETFQVADRHPEVAQRVEPMgpLKTPLF---H 359
Cdd:cd11266 292 F-TGRFKEQKSpdstwtpvpdeRVPKPRPGCCagssslekYATSNEFPDDTLNFIKTHPLMDEAVPSI--INRPWFlrtM 368
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      360 SKYHYQKVAVHRMQASHgETFHVLYLTTDRGTIHKVV----EPGEQEHSFAFNIMEIQPFRRAA-------AIQTMSLDA 428
Cdd:cd11266 369 VRYRLTKIAVDNAAGPY-QNHTVVFLGSEKGIILKFLartgNSGFLNDSLFLEEMNVYNSEKCSydgvedkRIMGMQLDK 447
                       410
                ....*....|....*...
3NVQ_A      429 ERRKLYVSSQWEVSQVPL 446
Cdd:cd11266 448 ASSALYVAFSTCVIKVPL 465
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
24-447 1.46e-30

The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed in regions of the basal telencephalon in rat. Sema5B is an inhibitory cue for corticofugal axons and acts as a source of repulsion for the appropriate guidance of cortical axons away from structures such as the ventricular zone as they navigate toward and within subcortical regions. In addition to its role as a guidance cue, Sema5B regulates the development and maintenance of synapse size and number in hippocampal neurons. In addition, the sema domain of Sema5B can be cleaved of the whole protein and exerts its function in regulation of synapse morphology. Sema5B belongs to the class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200525 [Multi-domain]  Cd Length: 437  Bit Score: 124.32  E-value: 1.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       24 DFGQtephtvLFHEPGSSSVWVGGRGkvYLFDFPEGKNASVRTVNIGS---TKGSCLDK----RDCENYITLLERRSEGL 96
Cdd:cd11264   8 DFSQ------LALDLNRNQLIVGARN--YLFRLSLHNVSLIQATEWGSdedTRRSCQSKgkteEECQNYVRVLIVYGKKV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       97 LACGTNARHPSCWNLVNGTVVPLGE-MRGYA--PFSPDENSL-VLFEGDEVYSTIrKQEYNGKIPR-FRRIRGESELYTS 171
Cdd:cd11264  80 FTCGTNAFSPVCTSRQVGNLSKVIErINGVArcPYDPRHNSTaVITSRGELYAAT-VIDFSGRDPAiYRSLGSVPPLRTA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      172 ---DTVMQNPQFIKativhqdqAYDDKIY-YFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSvSKWNTFLKAMLVC 247
Cdd:cd11264 159 qynSKWLNEPNFIA--------AYDIGLFtYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLE-DTWTTFMKARLNC 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      248 SDAATNK-NFNRLQDVFLLPDpsgqwrDTRVYGVFSNPWNY---SAVCVYSLGDIDKVFrtsslKGYHSSLPNPRpGKCL 323
Cdd:cd11264 230 SRPGEIPfYYNELQSTFYLPE------QDLIYGVFTTNVNSiaaSAVCAFNLSAITQAF-----NGPFRYQENPR-SAWL 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      324 PDQQPIPteTFQ------------VADRHPEVAQRVEPMGPLKTP------LFHSKYHYQKVAVHRMQASHgETFHVLYL 385
Cdd:cd11264 298 PTANPIP--NFQcgtlsddspnenLTERSLQDAQRLFLMNDVVQPvtvdplVTQDSVRFSKLVVDIVQGKD-TLYHVMYI 374
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3NVQ_A      386 TTDRGTIHKVVEPGEQE-HSFAFNIMEIQPFRRAAAIQTMSLDAERRKLYVSSQWEVSQVPLD 447
Cdd:cd11264 375 GTEYGTILKALSTTNRSlRSCYLEEMQILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
16-446 1.16e-29

The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed predominantly in the nervous system during embryogenesis and it uses Plexin-A1 as a receptor. It displays repellent activity for dorsal root ganglion axons. Sema6D also acts as a regulator of late phase primary immune responses. In addition, Sema6D is overexpressed in gastric carcinoma, indicating that it may have an important role in the occurrence and development of the cancer. Sema6D is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200530 [Multi-domain]  Cd Length: 465  Bit Score: 122.06  E-value: 1.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       16 GHVGQDRVDFG-QTEPHTVLFhepgsssvwVGGRGKVYLFDFPEGKNASV---RTVNIGSTKG---SCL----DKRDCEN 84
Cdd:cd11269   2 GNESQHRLDFQlMLKIRDTLY---------IAGRDQVYTVNLNEVPKTEVtpsRKLTWRSRQQdreNCAmkgkHKDECHN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       85 YI-TLLERRSEGLLACGTNARHPSC-WNLVNGTVVPLGEMRGYA--PFSPDENSLVLFEGDEVYSTIRKQEYNGKIPRFR 160
Cdd:cd11269  73 FIkVFVPRNDEMVFVCGTNAFNPMCrYYRLSTLEYDGEEISGLArcPFDARQTNVALFADGKLYSATVADFLASDAVIYR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      161 RIRGESELYT---SDTVMQNPQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKW 237
Cdd:cd11269 153 SMGDGSALRTikyDSKWIKEPHFLHAI------EYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHW 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      238 NTFLKAMLVCSDAATN-KNFNRLQDVFLLPDPSGQwrdTRVYGVFSNPWNY---SAVCVYSLGDIDKVF--RTSSLKGYH 311
Cdd:cd11269 227 TSFLKARLNCSVPGDSfFYFDVLQSITDIIEINGI---PTVVGVFTTQLNSipgSAVCAFSMDDIEKVFkgRFKEQKTPD 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      312 S--------SLPNPRPGKC--------LPDQQPIPTETFQVADRHPEVAQRVEPMGplKTPLFHS---KYHYQKVAVHRM 372
Cdd:cd11269 304 SvwtavpedKVPKPRPGCCakhglaeaYKTSIDFPDETLSFIKSHPLMDSAVPSII--EEPWFTKtrvRYRLTAIAVDHA 381
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      373 QASHgETFHVLYLTTDRGTIHKVVepgEQEHSFAFN----IMEIQPFRRAAA---------IQTMSLDAERRKLYVSSQW 439
Cdd:cd11269 382 AGPH-QNYTVIFVGSEAGVVLKIL---AKTSPFSLNdsvlLEEIEAYNHAKCsaeneedrrVISLQLDRDHHALFVAFSS 457

                ....*..
3NVQ_A      440 EVSQVPL 446
Cdd:cd11269 458 CVVRIPL 464
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
67-394 8.45e-29

The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as repellents for axon growth; this repulsive activity is mediated by its receptor Plexin A4. Sema6B is expressed in CA3, and repels mossy fibers in a Plexin A4 dependent manner. In human, it was shown that peroxisome proliferator-activated receptors (PPARs) and 9-cis-retinoic acid receptor (RXR) regulate human semaphorin 6B (Sema6B) gene expression. Sema6B is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200528 [Multi-domain]  Cd Length: 466  Bit Score: 119.55  E-value: 8.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       67 VNIGSTKGSclDKRDCENYI-TLLERRSEGLLACGTNARHPSCWNLVNGTVVPLGE-MRGYA--PFSPDENSLVLFEGDE 142
Cdd:cd11267  57 INVCRMKGK--HEGECRNFIkVLLLRDYGTLFVCGTNAFNPVCANYSIDTLEPVGDnISGMArcPYDPKHANVALFADGM 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      143 VYS-------TIRKQEYN--GKIPRFRRIRGESELYtsdtvmQNPQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPL 213
Cdd:cd11267 135 LFTatvtdflAIDAVIYRslGDSPALRTVKHDSKWF------KEPYFVHAV------EWGSHVYFFFREIAMEFNYLEKV 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      214 NVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCS-DAATNKNFNRLQDVFLLPDPSGqwRDTrVYGVFSNPWNY---SA 289
Cdd:cd11267 203 VVSRVARVCKNDMGGSQRVLEKQWTSFLKARLNCSvPGDSHFYFNVLQAVSDILNLGG--RPV-VLAVFSTPTNSipgSA 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      290 VCVYSLGDIDKVF--RTSSLKGYHS--------SLPNPRPGKCLPDQQP------IPTETFQVADRHPEVAQRVEPMG-- 351
Cdd:cd11267 280 VCAFDMTQVAAVFegRFREQKSPESiwtpvpeeLVPRPRPGCCAAPGMRynssstLPDEVLNFVKTHPLMDEAVPSLGha 359
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
3NVQ_A      352 P--LKTplfHSKYHYQKVAVHRMQASHGETfHVLYLTTDRGTIHK 394
Cdd:cd11267 360 PwiVRT---MTRYQLTHMVVDTEAGPHGNH-TVVFLGSTRGTVLK 400
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
76-445 9.44e-29

The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, Sema5C was identified as an early development gene, which is expressed in stage 2 embryos with a striped pattern emerging at later stages. Sema5c may play a role in odor-guided behavior and in tumorigenesis. Sema5C belongs to class 5 semaphorin family of proteins, which are transmembrane glycoproteins characterized by unique thrombospondin specific repeats in the extracellular region of the protein. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200526 [Multi-domain]  Cd Length: 433  Bit Score: 119.12  E-value: 9.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       76 CLDK----RDCENYITLLERRSEGLLACGTNARHPSC-WNLVNGTVVPLGEMRGYA--PFSPDENSLVLFEGDEVYSTIR 148
Cdd:cd11265  55 CQNKgqseEDCHNYVKVLLSYGKQLFACGTNAFSPRCsWREMENLTSVTEWDSGVAkcPYSPHANITALLSSSGQLFVGS 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      149 KQEYNGKIPRFRRIRGESELYTSDTVMQN------PQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLC 222
Cdd:cd11265 135 PTDFSGSDSAIYRTLGTSNKSFLRTKQYNskwlnePQFVGSF------ETGNFVYFLFRESAVEYMNCGKVIYSRIARVC 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      223 RGDQGGESSLSVSKWNTFLKAMLVCSDAATNK-NFNRLQDVFLLPDPSgqwrdtRVYGVFSNPWNY---SAVCVYSLGDI 298
Cdd:cd11265 209 KNDVGGGTMLLKDNWTTFLKARLNCSLPGEYPfYFDEIQGMTYLPDEG------ILYATFTTPENSiagSAVCAFNLSSI 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      299 DKVF---------RTSSLKGYHSSLPNPRPGKCLPD-QQPIPTETFQVADrhpevaQRVEPMGplKTPLFHSKYH-YQKV 367
Cdd:cd11265 283 NAAFdgpfkhqesSGAAWERVNVNHRDHFNQCSSSSsSHLLESSRYQLMD------EAVQPIT--LEPLHHAKLErFSHI 354
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      368 AVHRMQASHGETFHVLYLTTDRGTIHKV-VEPGEQEhsfAFNIMEIQPFRRAAA-IQTMSLDAERRKLYVSSQWEVSQVP 445
Cdd:cd11265 355 AVDVIPTKIHQSVHVLYVATTGGLIKKIsVLPRTQE---TCLVEIWQPLPTPDSpIKTMQYLKVTDSLYVGTELALMRIP 431
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
79-446 7.34e-28

The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins and plexins have a Sema domain on their N-termini. Plexins function as receptors for the semaphorins. Evolutionarily, plexins may be the ancestor of semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems, and cancer. Semaphorins can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. Plexins are a large family of transmembrane proteins, which are divided into four types (A-D) according to sequence similarity. In vertebrates, type A plexins serve as co-receptors for neuropilins to mediate the signalling of class 3 semaphorins. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B plexins. This family also includes the MET and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves to recognize and bind receptors.


Pssm-ID: 200495 [Multi-domain]  Cd Length: 392  Bit Score: 115.77  E-value: 7.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       79 KRDCENYITLLERRSEG--LLACGTNARHPSCWNLVNGTVVPLGEM-----RGYAPFSPDENSLVLFEGDEVYSTIRKQE 151
Cdd:cd09295  60 WTECINYIKVLQQKGDLdiLAVCGSNAAQPSCGSYRLDVLVELGKVrwpsgRPRCPIDNKHSNMGVNVDSKLYSATDHDF 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      152 YNGKIPRFRRIRGESE----LYTSDTVMQNPQFIKATIVHQDqayDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQG 227
Cdd:cd09295 140 KDGDRPALSRRSSNVHylriVVDSSTGLDEITFVYAFVSGDD---DDEVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVG 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      228 GESSLSvSKWNTFLKAMLVCSDAATNKNFNRLQDVFLLPDPSGQwrdTRVYGVFSNPWNY---SAVCVYSLGDIDKVFRT 304
Cdd:cd09295 217 GCHRLK-KKLTSFLKADLNCSRPQSGFAFNLLQDATGDTKNLIQ---DVKFAIFSSCLNKsveSAVCAYLFTDINNVFDD 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      305 SslkgyhsslpnprpgkclpdqqpiptetfqvadrhpevaqrVEPMGPLktPLFHSK---YHYQKVAVHRMQAShGETFH 381
Cdd:cd09295 293 P-----------------------------------------VEAINNR--PLYAHQnqrSRLTSIAVDATKQK-SVGYQ 328
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3NVQ_A      382 VLYLTTDRGTIHKVVepgEQEHSFAFNIME----IQPFRRaaaIQTMSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd09295 329 VVFLGLKLGSLGKAL---AFFFLYKGHIIEewkvFKDSSR---ITNLDLSRPPLYLYVGSESGVLGVPV 391
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
40-446 5.76e-26

The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed predominantly in the nervous system during embryogenesis. It binds Plexin A1 and might utilize it as a receptor to repel axons of specific types during development. Sema6E acts as a repellent to dorsal root ganglion axons as well as sympathetic axons. Sema6E is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200531 [Multi-domain]  Cd Length: 462  Bit Score: 111.35  E-value: 5.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       40 SSSVWVGGRGKVYLFDFPEGKNASV-------RTVNIGSTKGSCLDKRDCENYI-TLLERRSEGLLACGTNARHPSCWNL 111
Cdd:cd11270  18 NHMVYIAARDHVFAINLSASLERIVpqqkltwKTKDVEKCTVRGKNSDECYNYIkVLVPRNDETLFACGTNAFNPTCRNY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      112 VNGTVVPLGE-MRGYA--PFSPDENSLVLFEGDEVYST----------IRKQEYNGKIPRFRRIRGESELytsdtvMQNP 178
Cdd:cd11270  98 KMSSLEQDGEeVIGQArcPFESRQSNVGLFAGGDFYSAtmtdflasdaVIYRSLGESSPVLRTVKYDSKW------LREP 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      179 QFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLSVSKWNTFLKAMLVCSDAATN-KNFN 257
Cdd:cd11270 172 HFLHAI------EYGNYVYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSPRVLERYWTSFLKARLNCSVPGDSfFYFD 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      258 RLQDVFLLPDPSGQWRDTRVYGVFSNPWNYSAVCVYSLGDIDKVF--RTSSLKGYHSS--------LPNPRPGKC----- 322
Cdd:cd11270 246 VLQSLTNVMQINHRPAVLGVFTTQANSITGSAVCAFYMDDIEKVFngKFKEQRNSESAwtpvpdeaVPKPRPGSCagdgp 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      323 ---LPDQQPIPTETFQVADRHPEVAQRVepMGPLKTPLF---HSKYHYQKVAVHRMQASHGeTFHVLYLTTDRGTIHKVV 396
Cdd:cd11270 326 aagYKSSTNFPDETLTFIKSYPLMDEAV--PSVNNRPCFtrtTSRFKLTQIAVDTAAGPYK-NYTVVFLGSENGHVLKVL 402
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      397 EpGEQEHSFAFNIM--EIQPFRRAAA--------IQTMSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11270 403 A-SMHPNSSYSTQVleDIDVYNPNKCnvrgedrrILGLELDKDHHALFVAFTGCVIRVPL 461
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
81-446 3.26e-24

The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called semaphorin Y); Sema6C is highly expressed in adult brain and skeletal muscle and it shows growth cone collapsing activity. It may play a role in the maintenance and remodelling of neuronal connections. In adult skeletal muscle, this role includes prevention of motor neuron sprouting and uncontrolled motor neuron growth. The expression of Sema6C in adult skeletal muscle is down-regulated following denervation. Sema6C is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200529 [Multi-domain]  Cd Length: 465  Bit Score: 105.94  E-value: 3.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       81 DCENYI-TLLERRSEGLLACGTNARHPSCWNLVNGTVVPLGE-MRGYA--PFSPDENSLVLFEGDEVYSTIRKQEYNGKI 156
Cdd:cd11268  68 ECYNYIrVLVPWDSQTLLACGTNSFSPVCRSYGITSLQQEGEeLSGQArcPFDATQSNVAIFAEGSLYSATAADFQASDA 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      157 PRFRRIRGESELYTS---DTVMQNPQFIKATivhqdqAYDDKIYYFFREDNPDKNPEAPLNVSRVAQLCRGDQGGESSLS 233
Cdd:cd11268 148 VVYRSLGPQPPLRSAkydSKWLREPHFVQAL------EHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSPRAL 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      234 VSKWNTFLKAMLVCS-DAATNKNFNRLQdvfLLPDPSGQWRDTRVYGVFSNPWNY---SAVCVYSLGDIDKVF-----RT 304
Cdd:cd11268 222 DRHWTSFLKLRLNCSvPGDSTFYFDVLQ---ALTGPVNLHGRSALFGVFTTQTNSipgSAVCAFYLDEIERGFegkfkEQ 298
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      305 SSLKG-----YHSSLPNPRPGKC--------LPDQQPIPTETFQVADRHPEVAQRVEPMGPLKTPLFHSKYHYQKVAVHR 371
Cdd:cd11268 299 RSLDGawtpvSEDRVPSPRPGSCagvggaalFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLTLTSRALLTQVAVDG 378
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      372 MQASHgETFHVLYLTTDRGTIHKVVEPGEQ----EHSFAFNIMEIQPFR----RAAA----IQTMSLDAERRKLYVSSQW 439
Cdd:cd11268 379 MAGPH-SNITVMFLGSNDGTVLKVLPPGGRsggpEPILLEEIDAYSPARcsgkRTAQtarrIIGLELDTEGHRLFVAFSG 457

                ....*..
3NVQ_A      440 EVSQVPL 446
Cdd:cd11268 458 CIVYLPL 464
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
75-446 6.53e-09

The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine kinases; Plexins form a conserved family of transmembrane receptors for semaphorins and may be the ancestor of semaphorins. Ligand binding activates signal transduction pathways controlling axon guidance in the nervous system and other developmental processes including cell migration and morphogenesis, immune function, and tumor progression. Plexins are divided into four types (A-D) according to sequence similarity. In vertebrates, type A Plexins serve as the co-receptors for neuropilins to mediate the signalling of class 3 semaphorins except Sema3E, which signals through Plexin D1. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B. Plexin C1 serves as the receptor of Sema7A and plays regulation roles in both immune and nervous systems. This family also includes the Met and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 58.11  E-value: 6.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A       75 SCLDKRDCENY--ITLLERRSEGLLACGT-------------------NARHPSCWNLVNGTVVPLgemrgYAPFSPDEN 133
Cdd:cd11236  54 CDHPRSPTDNYnkILLIDYSSGRLITCGSlyqgvcqlrnlsnisvvveRSSTPVAANDPNASTVGF-----VGPGPYNNE 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      134 SlVLFegdeVYSTIRKQEYNGKIPRF--RRIRgeselytSDTVMQNPQFIKATIVHQDQAYDDK-----IYYFFRED--- 203
Cdd:cd11236 129 N-VLY----VGATYTNNGYRDYRPAVssRSLP-------PDDDFNAGSLTGGSAISIDDEYRDRysikyVYGFSSGGfsy 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      204 ---NPDKNPEAPLN-VSRVAQLCRGDQGGESSLSVSkwntflkamLVCsDAATNKNFNRLQDVFL------LPDPSGQWR 273
Cdd:cd11236 197 fvtVQRKSVDDESPyISRLVRVCQSDSNYYSYTEVP---------LQC-TGGDGTNYNLLQAAYVgkagsdLARSLGIST 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      274 DTRV-YGVFSN-------PWNYSAVCVYSLGDIDKVFRtsslkgyhsslpnprpgkclpdqqpiptetfqvaDRHPEVAQ 345
Cdd:cd11236 267 DDDVlFGVFSKskgpsaePSSKSALCVFSMKDIEAAFN----------------------------------DNCPLGGG 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      346 RvepmgPLKTPLFHSKYHYQKVAVHRMqasHGETfhVLYLTTDRGTIHKV-VEPGEQEHSFA-FNIMEIQPFrraaaIQT 423
Cdd:cd11236 313 V-----PITTSAVLSDSLLTSVAVTTT---RNHT--VAFLGTSDGQLKKVvLESSSSATQYEtLLVDSGSPI-----LPD 377
                       410       420
                ....*....|....*....|...
3NVQ_A      424 MSLDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11236 378 MVFDPDGEHLYVMTPKKVTKVPV 400
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
380-469 2.32e-08

The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 56.86  E-value: 2.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      380 FHVLYLTTDRGTIHKVVEPGEQEHSFAFNIMEIqpFRRAAAI-QTMSLDAERRKLYVSSQWEVSQVPLDLCEVYgGGCHG 458
Cdd:cd11272 406 YSVVFVGTKSGKLKKIRADGPPHGGVQYEMVSV--FKDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQY-TTCGE 482
                        90
                ....*....|.
3NVQ_A      459 CLMSRDPYCGW 469
Cdd:cd11272 483 CLSSGDPHCGW 493
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
218-446 6.65e-06

The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin domains, function as receptors of semaphorins and may be the ancestors of semaphorins. There are three members of the Plexin B subfamily, namely B1, B2 and B3. Plexins B1, B2 and B3 are receptors for Sema4D, Sema4C and Sema4G, and Sema5A, respectively. The activation of plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor is critically involved in neural tube closure and cerebellar granule cell development. Plexin B3, the receptor of Sema5A, is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Small GTPases play important roles in plexin B signaling. Plexin B1 activates Rho through Rho-specific guanine nucleotide exchange factors, leading to neurite retraction. Plexin B1 possesses an intrinsic GTPase-activating protein activity for R-Ras and induces growth cone collapse through R-Ras inactivation. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 48.77  E-value: 6.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      218 VAQLCRGDQggesslsvsKWNTFLKAMLVCSDAATNKnFNRLQDVFLLPdPSGQWRDTRVYGVFS-------NPWNYSAV 290
Cdd:cd11245 215 ISRLCENDH---------HYYSYVELPLNCTVNQENT-YNLVQAAYLAK-PGKVLNGKVLFGVFSadeastaAPDGRSAL 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      291 CVYSLGDIDKVFR-------TSSLKG----------YHS-----SLP--NPRPGKCLPDQQPIPtetfqVADRHPEVAqr 346
Cdd:cd11245 284 CMYPLSSVDARFErtrescyTGEGLEddkpetayieYNVksickTLPdkNVKAYPCGAEHTPSP-----LASRYPLAA-- 356
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      347 vepmgplkTPLFHSKYHYQKVAVhRMQASHGetfhVLYLTTDRGTIHKV-VEPGeqeHSFAFNIMEIQpfRRAAAIQTMS 425
Cdd:cd11245 357 --------KPILTRNDMLTAVAV-AVENGHT----IAFLGDSGGQLHKVyLDPN---HTDFYSTIPGD--QDSAVNKDLL 418
                       250       260
                ....*....|....*....|.
3NVQ_A      426 LDAERRKLYVSSQWEVSQVPL 446
Cdd:cd11245 419 FDSTLNHLYVMTGKKISKVPV 439
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
449-476 4.30e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 38.46  E-value: 4.30e-04
                          10        20        30
                  ....*....|....*....|....*....|
3NVQ_A        449 CEVYGGgCHGCLMSRDPYCGWD--QGRCIS 476
Cdd:pfam01437   2 CSQYTS-CSSCLAARDPYCGWCssEGRCVR 30
Sema_plexin_B3 cd11277
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of ...
216-445 4.38e-04

The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of semaphorin 5A. It is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Furthermore, Sema5A and plexin B3 have been implicated in the progression of various types of cancer. They play an important role in the invasion and metastasis of gastric carcinoma. The stimulation of plexin B3 by Sema5A binding in human glioma cells results in the inhibition of cell migration and invasion. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200538 [Multi-domain]  Cd Length: 434  Bit Score: 42.87  E-value: 4.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      216 SRVAQLCRGDQGGESSLSVSkwntflkamLVCSDAatnknFNRLQDVFLLPDPSGqwrdtrVYGVFS-------NPWNYS 288
Cdd:cd11277 215 TYVARVCLGDTNLYSYVEVP---------LVCQGG-----YNLAQAAYLAPGQGT------LFVVFAagqgstpTPTDQT 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      289 AVCVYSLGDIDKVFRTSSLKGYHSSLPNPRPG-----------KC--LPDQQPiptETFQVADRH-PE-VAQRVepmgPL 353
Cdd:cd11277 275 ALCAYPLVELDSAMERARRLCYTAGGGGPNGKeeatieygvtsRCvnLPKDSP---ESYPCGDEHtPSpIASRQ----PL 347
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NVQ_A      354 K-TPLFHSKYHYQKVAvhrmqASHGETFHVLYLTTDRGTIHKVVEPGEQEHsfAFNIMEIQPfRRAAAIQTMSLDAERRK 432
Cdd:cd11277 348 EaEPLLTLTPPLTAVA-----ALQEDGHTIAFLGDTQGQLHKVFLNGSAGQ--VYSSQPVGP-PGSAVNPDLLLDATGSH 419
                       250
                ....*....|...
3NVQ_A      433 LYVSSQWEVSQVP 445
Cdd:cd11277 420 LYVLTARQVTKVP 432
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
505-575 1.08e-03

Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are composed of the immunoglobulin (Ig)-like domain of Sema4B and similar proteins. Sema4B is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4B has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4B has been shown to preferentially regulate the development of the postsynaptic specialization at the glutamatergic synapses. This cytoplasmic domain includes a PDZ-binding motif upon which the synaptic localization of Sem4B is dependent. Sema4B is a ligand of CLCP1. CLCP1 was identified in an expression profiling analysis, which compared a highly metastic lung cancer subline with its low metastic parental line. Sema4B was shown to promote CLCP1 endocytosis and their interaction is a potential target for therapeutic intervention of metastasis.


Pssm-ID: 409456  Cd Length: 86  Bit Score: 38.19  E-value: 1.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3NVQ_A      505 APLQKVSLAPNSRYYLSCPMESRHATYSWRHKENVEQSCEPGHQSPNCILFIENLTAQQYGHYFCEAQEGS 575
Cdd:cd05872   1 LPVKFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSYLRLGTDGLLILVTSPEHSGTYRCYSEEEG 71
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
449-498 1.38e-03

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 36.75  E-value: 1.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
3NVQ_A         449 CEVYGGgCHGCLMSRDPYCGWD--QGRCISiYSSERSVLQSINpaepHKECP 498
Cdd:smart00423   2 CSKYTS-CSECLLARDPYCAWCssQGRCTS-GERCDSRRQNWL----SGGCP 47
 
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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