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Conserved domains on  [gi|1958801504|ref|XP_038939150|]
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semaphorin-4C isoform X3 [Rattus norvegicus]

Protein Classification

semaphorin( domain architecture ID 10336824)

semaphorin, containing Sema, PSI, and Ig domains, is a regulatory molecule that functions in the development of the nervous system and in axonal guidance; similar to Bos taurus semaphorin-4A, the cell surface receptor for plexins PLXNB1, PLXNB2, PLXNB3 and PLXND1, that plays an important role in cell-cell signaling

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema super family cl15693
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
1-357 0e+00

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.


The actual alignment was detected with superfamily member cd11258:

Pssm-ID: 472829 [Multi-domain]  Cd Length: 458  Bit Score: 709.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   1 MLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLAFWLNEPHFVGSAFV 80
Cdd:cd11258   101 MLTFTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMKTEYLAFWLNEPHFVGSAFV 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  81 PESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAVH 160
Cdd:cd11258   181 PESVGSFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKARLLCSIPEWQLYFNQLKAVF 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 161 TLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNGYT 240
Cdd:cd11258   261 TLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDPVPSPRPGSCINNWHRDHGYT 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 241 SSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMV 320
Cdd:cd11258   341 SSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSVLFIGTLDGWLIKAVSLGSWVHMI 420
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958801504 321 EELQVFDQEPVESLVLSQS-KKVLFAGSRSQLVQLSLA 357
Cdd:cd11258   421 EELQVFDQEPPESLVVSQSsKKLLFAGSRSELLQLPWA 458
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
423-507 1.08e-19

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: 84.03  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 423 KNITVVAGTDLVLPCHLSSNLAHALWTFRGRDLPAEQPGsflYDTGLQALVVMAAQSRHSGPYHCYSEEQGTKLAAESYL 502
Cdd:cd05872     4 KFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSY---LRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYS 80

                  ....*
gi 1958801504 503 VSVVA 507
Cdd:cd05872    81 LNVVE 85
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
358-387 1.17e-08

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 51.39  E-value: 1.17e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958801504  358 DCTKYRFCVDCVLARDPYCAWNVNTSRCVA 387
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRCTS 30
 
Name Accession Description Interval E-value
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
1-357 0e+00

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: 709.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   1 MLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLAFWLNEPHFVGSAFV 80
Cdd:cd11258   101 MLTFTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMKTEYLAFWLNEPHFVGSAFV 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  81 PESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAVH 160
Cdd:cd11258   181 PESVGSFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKARLLCSIPEWQLYFNQLKAVF 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 161 TLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNGYT 240
Cdd:cd11258   261 TLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDPVPSPRPGSCINNWHRDHGYT 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 241 SSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMV 320
Cdd:cd11258   341 SSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSVLFIGTLDGWLIKAVSLGSWVHMI 420
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958801504 321 EELQVFDQEPVESLVLSQS-KKVLFAGSRSQLVQLSLA 357
Cdd:cd11258   421 EELQVFDQEPPESLVVSQSsKKLLFAGSRSELLQLPWA 458
Sema smart00630
semaphorin domain;
33-331 1.08e-103

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 321.63  E-value: 1.08e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   33 GELYSATLNNFLGTEPVILRNMGPHH-------PIKTEYLAF-WLNEPHFVGSafvpesvgsFTgDDDKIYFFFSERAVE 104
Cdd:smart00630  92 GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTVLYDSkWLNEPNFVYA---------FE-SGDFVYFFFRETAVE 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  105 YDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWK-VYFNQLRAVHTLLGASWHNTTFFAVFQARWGDM 183
Cdd:smart00630 162 DDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDpFYFNELQAAFLLPPGSESDDVLYGVFSTSSNPI 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  184 DLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARY-TDPVPTPRPGSCINNWHrdngytSSLELPDNTLNFIKKHPLMEEQ 262
Cdd:smart00630 242 PGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYsRGKVPYPRPGTCPNKPP------SSKDLPDETLNFIKSHPLMDEV 315
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801504  263 VKPRLGRPLLVKKNTN--FTHVVADRILGldGATYTVLFIGTGDGWLLKAVSLGP----WIHMVEELQVF-DQEPV 331
Cdd:smart00630 316 VQPLTGRPLFVKTDSNylLTSIAVDRVAT--DGNYTVLFLGTSDGRILKVVLSESssssESVVLEEISVFpDGSPI 389
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
156-338 1.85e-69

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: 224.46  E-value: 1.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 156 LRAVHTL--LGASWHNTTFFAVFQARWGD-MDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINN 232
Cdd:pfam01403   1 LQDVFVLkpGAGDALDTVLYGVFTTQWSNsIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 233 WHRdngytssLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVS 312
Cdd:pfam01403  81 PLR-------LDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDG-NYTVLFLGTDDGRLHKVVL 152
                         170       180
                  ....*....|....*....|....*...
gi 1958801504 313 LGP-WIHMVEELQVFDQ-EPVESLVLSQ 338
Cdd:pfam01403 153 VGSeESHIIEEIQVFPEpQPVLNLLLSS 180
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
423-507 1.08e-19

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: 84.03  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 423 KNITVVAGTDLVLPCHLSSNLAHALWTFRGRDLPAEQPGsflYDTGLQALVVMAAQSRHSGPYHCYSEEQGTKLAAESYL 502
Cdd:cd05872     4 KFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSY---LRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYS 80

                  ....*
gi 1958801504 503 VSVVA 507
Cdd:cd05872    81 LNVVE 85
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
358-387 1.17e-08

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 51.39  E-value: 1.17e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958801504  358 DCTKYRFCVDCVLARDPYCAWNVNTSRCVA 387
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRCTS 30
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
358-386 3.01e-07

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: 47.70  E-value: 3.01e-07
                          10        20
                  ....*....|....*....|....*....
gi 1958801504 358 DCTKYRFCVDCVLARDPYCAWNVNTSRCV 386
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCV 29
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
422-496 6.14e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 6.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  422 PKNITVVAGTDLVLPCHLSSNLAHAL-WTFRGRDLPAEQPG-SFLYDTGLQALVVMAAQSRHSGPYHC------YSEEQG 493
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVtWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCaatnssGSASSG 80

                   ...
gi 1958801504  494 TKL 496
Cdd:smart00410  81 TTL 83
I-set pfam07679
Immunoglobulin I-set domain;
421-487 3.25e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 37.24  E-value: 3.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801504 421 VPKNITVVAGTDLVLPCHLSSN-LAHALWTFRGRDLPAEQPGSFLYDTGLQALVVMAAQSRHSGPYHC 487
Cdd:pfam07679   6 KPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
 
Name Accession Description Interval E-value
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
1-357 0e+00

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: 709.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   1 MLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLAFWLNEPHFVGSAFV 80
Cdd:cd11258   101 MLTFTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMKTEYLAFWLNEPHFVGSAFV 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  81 PESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAVH 160
Cdd:cd11258   181 PESVGSFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKARLLCSIPEWQLYFNQLKAVF 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 161 TLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNGYT 240
Cdd:cd11258   261 TLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDPVPSPRPGSCINNWHRDHGYT 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 241 SSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMV 320
Cdd:cd11258   341 SSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSVLFIGTLDGWLIKAVSLGSWVHMI 420
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958801504 321 EELQVFDQEPVESLVLSQS-KKVLFAGSRSQLVQLSLA 357
Cdd:cd11258   421 EELQVFDQEPPESLVVSQSsKKLLFAGSRSELLQLPWA 458
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
1-357 0e+00

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: 639.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   1 MLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLAFWLNEPHFVGSAFV 80
Cdd:cd11240   100 LSDFSLSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEGNVLKTENTLRWLNEPAFVGSAHI 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  81 PESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAVH 160
Cdd:cd11240   180 RESIDSPDGDDDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGGQRTLQKKWTTFLKAQLVCSQPDSGLPFNVLRDVF 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 161 TLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNGYT 240
Cdd:cd11240   260 VLSPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRYTGPVPDPRPGACITNSARSQGIT 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 241 SSLELPDNTLNFIKKHPLMEEQVKPRlGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMV 320
Cdd:cd11240   340 SSLNLPDNVLTFVKDHPLMDEQVHPI-NRPLLVKSGVNYTRIAVHRVQALDGQTYTVLFLGTEDGFLHKAVSLDGGMHII 418
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958801504 321 EELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLA 357
Cdd:cd11240   419 EEIQLFDQpQPVKNLLLSSSKGVLYVGSSSGVVQVPLS 456
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
3-356 2.98e-157

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: 461.92  E-value: 2.98e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   3 TFTLDrAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTePVILRNMgPHHPIKTEYLAF-WLNEPHFVGSAFVP 81
Cdd:cd11262   103 RFTLS-SQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQYEFRSF-PDIRRNS-PQPTLRTEEAPTrWLNDADFVGSVLVR 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  82 ESVGSFTGDDDKIYFFFSERAVE-YDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAVH 160
Cdd:cd11262   180 ESMNSSVGDDDKIYFFFTERSQEeTAYFSQSRVARVARVCKGDRGGKKTLQRKWTSFLKARLVCYIPEYEFLFNVLRSVF 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 161 TLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNGYT 240
Cdd:cd11262   260 VLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYTGKVPEPRPGSCITDEHRSQGIN 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 241 SSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMV 320
Cdd:cd11262   340 SSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDGRVYDVLFLGTDEGWLHKAVVIGSAVHII 419
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1958801504 321 EELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSL 356
Cdd:cd11262   420 EELQVFREpQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
12-357 3.28e-130

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: 393.07  E-value: 3.28e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  12 EDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMgPHHPIKTEYLAFWLNEPHFVGSAFVPESVGSFTGDD 91
Cdd:cd11259   120 EDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRNS-SQSPLRTEYAIPWLNEPSFVFADVIRADPDSPDGED 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  92 DKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAVHTLLGASWHNTT 171
Cdd:cd11259   199 DKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSIPDKNLVFNVVNDVFILKSPTLKEPV 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 172 FFAVFQARWGDMDLSAVCEYQLEHIQQVF-EGPFKEYS--EQAQ-KWARYTDPVPTPRPGSCINNWHRDNGYTSSLELPD 247
Cdd:cd11259   279 IYGVFTPQLNNVGLSAVCAYNLSTVEEVFsKGKYMQSAtvEQSHtKWVRYNGEVPKPRPGACINNEARAANYTSSLNLPD 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 248 NTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMVEELQVF- 326
Cdd:cd11259   359 KTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDGTIYDVMFISTDRGALHKAISLENEVHIIEETQLFp 438
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1958801504 327 DQEPVESLVLS--QSKKVLFAGSRSQLVQLSLA 357
Cdd:cd11259   439 DFEPVQTLLLSskKGRRFLYAGSNSGVVQSPLA 471
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
1-357 3.94e-128

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: 387.68  E-value: 3.94e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   1 MLTFTLDRAE-----FEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLAFWLNEPHFV 75
Cdd:cd11257   102 MTNFSLERDEkgeplLEDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIYRSLGSGTPLKTENSLNWLQDPAFV 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  76 GSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQ 155
Cdd:cd11257   182 GSAYIQESLPKLVGDDDKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGGERVLQKRWTTFLKAQLLCSLPDDGFPFNV 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 156 LRAVHTLLGAS--WHNTTFFAVFQARW--GDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCIN 231
Cdd:cd11257   262 LQDVFVLTPSPedWKDTLFYGVFTSQWhkGTAGSSAVCVFTMDQVQRAFNGLYKEVNRETQQWYTYTHPVPEPRPGACIT 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 232 NWHRDNGYTSSLELPDNTLNFIKKHPLMEEQVKprlGRPLLVKKNTNFTHVVADRILGLDgATYTVLFIGTGDGWLLKAV 311
Cdd:cd11257   342 NSARERKINSSLHMPDRVLNFVKDHFLMDGQVR---SQPLLLQPQVRYTQIAVHRVKGLH-KTYDVLFLGTDDGRLHKAV 417
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801504 312 SLGPWIHMVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 357
Cdd:cd11257   418 SVGPMVHIIEELQIFsEGQPVQNLLLDTHKGLLYASSHSGVVQVPVA 464
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
12-357 5.99e-125

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: 378.87  E-value: 5.99e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  12 EDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNmgPHHPIKTEYLAFWLNEPHFVGSAFVPESVGSFTGDD 91
Cdd:cd11260   111 EDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRS--SPITIRTEFKSSWLNEPNFIYMAAVPESEDSPEGDD 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  92 DKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFnQLRAVHTLLGASWHNTT 171
Cdd:cd11260   189 DKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQKKWTSFLKARLDCSVPEPSLPY-VIQDVFHVCHQDWRKCV 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 172 FFAVFQARWGDMDLSAVCEYQLEHIQQVF-EGPFK-----EYSEqaQKWARYTDPVPTPRPGSCINNWHRDNGYTSSLEL 245
Cdd:cd11260   268 FYAVFTSQSDSSQSSAVCAYNVTDISNVFsRGKFKtpvavETSF--VKWVMYSGELPVPRPGACINNAARTSGIKKSLNL 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 246 PDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMVEELQV 325
Cdd:cd11260   346 PDKTLQFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADGQSYPVMFIGTANGYVLKAVNYDGEMHIIEEVQL 425
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1958801504 326 FD-QEPVESLVLSQskKVLFAGSRSQLVQLSLA 357
Cdd:cd11260   426 FEpEEPIDILRLSQ--NQLYAGSASGVVQMPVS 456
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
11-357 6.55e-116

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: 355.18  E-value: 6.55e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  11 FEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEY-LAFWLNEPHFVGSAFVPesvgsftg 89
Cdd:cd11235   100 EESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYhDSKWLNEPQFVGAFDIG-------- 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  90 ddDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP-DWKVYFNQLRAVHTLLGASWH 168
Cdd:cd11235   172 --DYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPgEFPFYFNELQDVFDLPSPSNK 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 169 NTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTD-PVPTPRPGSCinnwhrdngYTSSLELPD 247
Cdd:cd11235   250 EKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDeRVPEPRPGTC---------VDDSSPLPD 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 248 NTLNFIKKHPLMEEQVKPRLGRPLLVKK--NTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPW----IHMVE 321
Cdd:cd11235   321 DTLNFIKSHPLMDEAVTPILNRPLFIKTdvNYRFTKIAVDRVQAKLGQTYDVLFVGTDRGIILKVVSLPEQglqaSNILE 400
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1958801504 322 ELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLA 357
Cdd:cd11235   401 EMPVGPPpEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
3-359 6.58e-109

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: 338.18  E-value: 6.58e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   3 TFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTE-YLAFWLNEPHFVGSAFVP 81
Cdd:cd11239   108 IFKLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLGHRHYIRTEqYDSRWLNEPKFVGAYLIP 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  82 ESvgsFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPD---WKVYFNQLRA 158
Cdd:cd11239   188 DS---DNPDDDKVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLKARLVCSVPGpdgIDTYFDELED 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 159 VHTLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHrDNG 238
Cdd:cd11239   265 VFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVEYQGKVPYPRPGTCPSKTY-GPL 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 239 YTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTN--FTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVSL--G 314
Cdd:cd11239   344 YKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPyrLTQIAVDRVEAEDG-QYDVLFIGTDSGTVLKVVSLpkE 422
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801504 315 PWIH---MVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11239   423 NWEMeevILEELQVFkHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
12-354 5.03e-108

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: 335.32  E-value: 5.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  12 EDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMG-PHHPIKTEYLAFWLNEPHFVGSAFVPESVGSFTGD 90
Cdd:cd11261   113 ESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAVGrAEEWIRTETLPSWLNAPAFVAAVFLSPAEWGDEDG 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  91 DDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAVHTLLGASWHNT 170
Cdd:cd11261   193 DDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGPEHGRASSILQDVTTLRPLPGAGT 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 171 T-FFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDP-VPTPRPGSCINNWHRDNGYTSSLELPDN 248
Cdd:cd11261   273 PiFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGLPVMDSdVPQPRPGECITNNMKLLGFGSSLSLPDR 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 249 TLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMVEELQVF-D 327
Cdd:cd11261   353 VLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFpE 432
                         330       340
                  ....*....|....*....|....*..
gi 1958801504 328 QEPVESLVLSQSkkVLFAGSRSQLVQL 354
Cdd:cd11261   433 PQPVENLQLHHN--WLLVGSDTEVTQI 457
Sema smart00630
semaphorin domain;
33-331 1.08e-103

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 321.63  E-value: 1.08e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   33 GELYSATLNNFLGTEPVILRNMGPHH-------PIKTEYLAF-WLNEPHFVGSafvpesvgsFTgDDDKIYFFFSERAVE 104
Cdd:smart00630  92 GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTVLYDSkWLNEPNFVYA---------FE-SGDFVYFFFRETAVE 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  105 YDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWK-VYFNQLRAVHTLLGASWHNTTFFAVFQARWGDM 183
Cdd:smart00630 162 DDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDpFYFNELQAAFLLPPGSESDDVLYGVFSTSSNPI 241
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  184 DLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARY-TDPVPTPRPGSCINNWHrdngytSSLELPDNTLNFIKKHPLMEEQ 262
Cdd:smart00630 242 PGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYsRGKVPYPRPGTCPNKPP------SSKDLPDETLNFIKSHPLMDEV 315
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801504  263 VKPRLGRPLLVKKNTN--FTHVVADRILGldGATYTVLFIGTGDGWLLKAVSLGP----WIHMVEELQVF-DQEPV 331
Cdd:smart00630 316 VQPLTGRPLFVKTDSNylLTSIAVDRVAT--DGNYTVLFLGTSDGRILKVVLSESssssESVVLEEISVFpDGSPI 389
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
11-380 1.10e-100

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: 316.08  E-value: 1.10e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  11 FEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLAFWLN-EPHFVGSAFVPEsvgsftg 89
Cdd:cd11256   116 TMDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLGTKVSLKTDGFLRWLNaDAVFVASFNPQG------- 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  90 dDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDwKVYFNQLRAVHTLLGASWHN 169
Cdd:cd11256   189 -DSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQLTCSQQG-HFPFNVIHHVALLNQPDPNN 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 170 TTFFAVFQARW--GDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCinnwhrdNGYTSSlelpD 247
Cdd:cd11256   267 SVFYAVFTSQWqlGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPVSDPRPGSC-------SGGKSS----D 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 248 NTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWI-HMVEELQVF 326
Cdd:cd11256   336 KALNFMKDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSGHNYTVMFLGTDKGFLHKAVLMGGSEsHIIEEIELL 415
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801504 327 -DQEPVESLVLSqskkvlfagsrsqlvqlsladCTKyrfcvDCVLARDPYCAWNV 380
Cdd:cd11256   416 tPPEPVENLLLA---------------------ANE-----GVVYIGYSAGVWRV 444
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
4-359 9.23e-91

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: 290.66  E-value: 9.23e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   4 FTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTE-YLAFWLNEPHFVGSAFVPE 82
Cdd:cd11250   109 FRLDPSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRPSLRTEqHDSRWLNEPKFVKVFWIPE 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  83 SVGSftgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP---DWKVYFNQLRAV 159
Cdd:cd11250   189 SENP---DDDKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCSVPgneGGDTHFDELRDV 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 160 HTLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHrdNGY 239
Cdd:cd11250   266 FLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGKVPYPRPGMCPSKTF--GSF 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 240 TSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTN--FTHVVADRILGLDGAtYTVLFIGTGDGWLLKAVSL--GP 315
Cdd:cd11250   344 ESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPytFTQIAVDRVAAADGH-YDVMFIGTDVGSVLKVISVpkGS 422
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801504 316 WIHM----VEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11250   423 WPSNeellLEELHVFkDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
6-359 3.40e-88

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: 283.07  E-value: 3.40e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   6 LDRAEFeDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNmgphhPIKTE-YLAFWLNEPHFVGSafvpesv 84
Cdd:cd11237    99 RVEREF-DGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYRE-----PLRTErYDLKQLNAPNFVSS------- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  85 gsFTgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP-DWKVYFNQLRAVHTLL 163
Cdd:cd11237   166 --FA-YGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPgEYPFYFNEIQSTSDIV 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 164 GA---SWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARY-TDPVPTPRPGSCINNwhrdngy 239
Cdd:cd11237   243 EGgygGKSAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVpSNKVPEPRPGQCVND------- 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 240 tsSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTN--FTHVVAD-RILGLDGATYTVLFIGTGDGWLLKAV----- 311
Cdd:cd11237   316 --SRTLPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQyrFTQIAVDpQVKALDGKYYDVLFIGTDDGKVLKAVniasa 393
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801504 312 ---SLGPWIHmVEELQVFDQ-EPVESLVLSQSKKV--LFAGSRSQLVQLSLADC 359
Cdd:cd11237   394 dtvDKVSPVV-IEETQVFPRgVPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
4-359 7.93e-88

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: 283.34  E-value: 7.93e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   4 FTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGP---HHPIKTEYLA-FWLNEPHFVGSAF 79
Cdd:cd11252   109 FLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLGPtpdHHYIRTDISEhYWLNGAKFIGTFP 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  80 VPESvgsFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWK---VYFNQL 156
Cdd:cd11252   189 IPDT---YNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKWTTFLKARLVCSIPGPDgadTHFDEL 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 157 RAVHTLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHrD 236
Cdd:cd11252   266 QDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWVQYEGRIPYPRPGTCPSKTY-D 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 237 NGYTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNF--THVVADRILGLDGaTYTVLFIGTGDGWLLKAVSLG 314
Cdd:cd11252   345 PLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYrlTQIVVDHVAAEDG-QYDVMFLGTDIGTVLKVVSIT 423
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801504 315 P--WIH---MVEELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11252   424 KekWTMeevVLEELQIFKHpSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
3-359 1.39e-87

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: 283.04  E-value: 1.39e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   3 TFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTE-YLAFWLNEPHFVGSAFVP 81
Cdd:cd11249   129 IFRLEDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEqHDSRWLNDPRFISAHLIP 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  82 ESVGSftgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWK---VYFNQLRA 158
Cdd:cd11249   209 ESDNP---EDDKIYFFFRENAIDGEHTGKATHARIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNgidTHFDELQD 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 159 VHTLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHrdNG 238
Cdd:cd11249   286 VFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTF--GG 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 239 YTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTN--FTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVSL--G 314
Cdd:cd11249   364 FDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKTDVDyqFTQIVVDRVEAEDG-QYDVMFIGTDMGTVLKVVSIpkE 442
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801504 315 PWIH----MVEELQVFdQEP--VESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11249   443 TWHDleevLLEEMTVF-REPtaISAMELSTKQQQLYIGSAIGVSQLPLHRC 492
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
4-359 1.01e-86

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: 280.26  E-value: 1.01e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   4 FTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLAFWLNEPHFVGSAFVPES 83
Cdd:cd11255   108 FSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFGTRSPLRTETDQRLLHEPRFVAAHLIPDN 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  84 VGSftgDDDKIYFFFSERAVEYDCYSEQV-VARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP---DWKVYFNQLRAV 159
Cdd:cd11255   188 ADR---DNDKVYFFFTERATETAEDDDGAiHSRVGRLCANDAGGQRVLVNKWSTFIKARLVCSVPgphGIQTHFDQLEDV 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 160 HTLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNG- 238
Cdd:cd11255   265 FLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPYEGKVPYPRPGVCPSKITAQPGr 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 239 -YTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNT--NFTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVSLG- 314
Cdd:cd11255   345 aFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLpyRLTQIVVDRVEAEDG-YYDVMFIGTDSGSVLKVIVLQk 423
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801504 315 -----PWIHMVEELQVFD-QEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11255   424 gnsaaGEEVTLEELQVFKvPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
4-359 5.80e-83

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: 270.16  E-value: 5.80e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   4 FTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTE-YLAFWLNEPHFVGSAFVPE 82
Cdd:cd11254   109 FRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDqYNSRWLNDPAFVHAHLIPD 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  83 SVGSftgDDDKIYFFFSERAVEYDcYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDW---KVYFNQLRAV 159
Cdd:cd11254   189 SSEK---NDDKLYFFFREKSLEAP-QSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGAdgiETHFDELRDV 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 160 HTLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNgY 239
Cdd:cd11254   265 FIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPS-M 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 240 TSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTN--FTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVSLGPWI 317
Cdd:cd11254   344 KSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNyrFTTIAVDQVDAADG-RYEVLFLGTDRGTVQKVIVLPKDD 422
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801504 318 H-----MVEELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11254   423 LeteelTLEEVEVFKVpAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
4-359 2.02e-76

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: 252.85  E-value: 2.02e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   4 FTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKTEYLA-FWLNEPHFVGSAFVPE 82
Cdd:cd11253   108 FQLESDKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMNHLAHIRTEHDDeRLLKEPKFVGSYMIPD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  83 SVGSftgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWK---VYFNQLRAV 159
Cdd:cd11253   188 NEDP---DDNKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLICSVPGPNgidTHFDELEDV 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 160 HTLLGASWHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSC---INNWHrd 236
Cdd:cd11253   265 FLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVYEGKVPYPRPGSCaskVNGGH-- 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 237 ngYTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKN--TNFTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVSlg 314
Cdd:cd11253   343 --YGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDgkYNLKQIAVDRVEAEDG-QYDVLFIGTDNGIVLKVIT-- 417
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801504 315 pwIH----------MVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11253   418 --IYnqetetmeevILEELQVFkVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
14-329 1.35e-74

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: 247.81  E-value: 1.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  14 GKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSAfvpeSVGSFtgddd 92
Cdd:cd11242   114 GMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSLGDSPTLRTvKYDSKWLKEPHFVHAV----EYGDY----- 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  93 kIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQLRAVHTLLGASwHNT 170
Cdd:cd11242   185 -VYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGSpRVLEKQWTSFLKARLNCSVPgDSHFYFDVLQAVTDVIRIN-GRP 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 171 TFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYT-DPVPTPRPGSCINNWHRDnGYTSSLELPDNT 249
Cdd:cd11242   263 VVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPeDRVPKPRPGCCAGSGSAE-KYKTSNDFPDDT 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 250 LNFIKKHPLMEEQVKPRLGRPLLVKKNTNF--THVVADRILGLDGaTYTVLFIGTGDGWLLKAV-----SLGPWIHMVEE 322
Cdd:cd11242   342 LNFIKTHPLMDEAVPSIINRPWFTRTMVRYrlTQIAVDNAAGPYQ-NYTVVFLGSEAGTVLKFLarigpSGSNGSVFLEE 420

                  ....*..
gi 1958801504 323 LQVFDQE 329
Cdd:cd11242   421 IDVYNPA 427
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
12-359 4.26e-71

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: 239.02  E-value: 4.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  12 EDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSAFVPESVGSftgD 90
Cdd:cd11251   116 ESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTdQHNSKWLSEPIFVDAHLIPDGTDP---N 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  91 DDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPD---WKVYFNQLRAVHTLLGASW 167
Cdd:cd11251   193 DAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKARLVCSVMDedgTETHFDELEDVFLLETDNP 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 168 HNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNgYTSSLELPD 247
Cdd:cd11251   273 RTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQGRIPYPRPGTCPGGAFTPN-MQSTKEFPD 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 248 NTLNFIKKHPLMEEQVKPRLGRPLLVKKNTN--FTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVSL-------GPWIh 318
Cdd:cd11251   352 DVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDykYTKIAVDRVNAADG-RYHVLFLGTDKGTVQKVVVLptngslsGELI- 429
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958801504 319 mVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 359
Cdd:cd11251   430 -LEELEVFkNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
156-338 1.85e-69

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: 224.46  E-value: 1.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 156 LRAVHTL--LGASWHNTTFFAVFQARWGD-MDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINN 232
Cdd:pfam01403   1 LQDVFVLkpGAGDALDTVLYGVFTTQWSNsIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 233 WHRdngytssLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGaTYTVLFIGTGDGWLLKAVS 312
Cdd:pfam01403  81 PLR-------LDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDG-NYTVLFLGTDDGRLHKVVL 152
                         170       180
                  ....*....|....*....|....*...
gi 1958801504 313 LGP-WIHMVEELQVFDQ-EPVESLVLSQ 338
Cdd:pfam01403 153 VGSeESHIIEEIQVFPEpQPVLNLLLSS 180
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
2-357 9.25e-68

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: 229.23  E-value: 9.25e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   2 LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDG-------ELYSATLNNFLGTEPVILR------NMGPHHPIKT--EYLA 66
Cdd:cd11238   100 LHLPEYVPGPGNGIGKCPYDPDDNSTAVWVEWgnpgdlpALYSGTRTEFTKANTVIYRpplynnTKGRHESFMRtlKYDS 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  67 FWLNEPHFVGSAfvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSA 146
Cdd:cd11238   180 KWLDEPNFVGSF----DIGDY------VYFFFRETAVEYINCGKVVYSRVARVCKKDTGGKNVLRQNWTTFLKARLNCSI 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 147 P-DWKVYFNQLRAVHTLLGASwhNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVF-EGPFKEYSEQAQKW-ARYTDPVPT 223
Cdd:cd11238   250 SgEFPFYFNEIQSVYKVPGRD--DTLFYATFTTSENGFTGSAVCVFTLSDINAAFdTGKFKEQASSSSAWlPVLSSEVPE 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 224 PRPGSCINNwhrdngytsSLELPDNTLNFIKKHPLMEEQVKPrlGRPLLVKKNTNFTHVVADRILGlDGATYTVLFIGTG 303
Cdd:cd11238   328 PRPGTCVND---------SATLSDTVLHFARTHPLMDDAVSH--GPPLLYLRDVVFTHLVVDKLRI-DDQEYVVFYAGSN 395
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801504 304 DGWLLKAVSlgpWIH-------MVEELQVFDQEPVESLVLSQSKKvLFAGSRSQLVQLSLA 357
Cdd:cd11238   396 DGKVYKIVH---WKDagesksnLLDVFELTPGEPIRAMELLPGEF-LYVASDHRVSQIDLA 452
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
4-309 3.25e-66

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: 225.68  E-value: 3.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   4 FTLDRAEFED----GKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSA 78
Cdd:cd11266   100 YKMDTLEFFGdefsGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTvKHDSKWLKEPYFVQAV 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  79 fvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQL 156
Cdd:cd11266   180 ----DYGDY------IYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGSqRVLEKQWTSFLKARLNCSVPgDSHFYFNIL 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 157 RAVHTLLGASWHNTTfFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDP-VPTPRPGSCINNWHR 235
Cdd:cd11266   250 QAVTDVIHINGRDVV-LATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDErVPKPRPGCCAGSSSL 328
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801504 236 DNgYTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNF--THVVADRILGlDGATYTVLFIGTGDGWLLK 309
Cdd:cd11266   329 EK-YATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYrlTKIAVDNAAG-PYQNHTVVFLGSEKGIILK 402
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
14-309 1.51e-65

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: 223.94  E-value: 1.51e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  14 GKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSAfvpeSVGSftgddd 92
Cdd:cd11267   114 GMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRTvKHDSKWFKEPYFVHAV----EWGS------ 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  93 KIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQLRAVHTLLGASWHNT 170
Cdd:cd11267   184 HVYFFFREIAMEFNYLEKVVVSRVARVCKNDMGGSqRVLEKQWTSFLKARLNCSVPgDSHFYFNVLQAVSDILNLGGRPV 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 171 TfFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDP-VPTPRPGSCINNWHRdngYTSSLELPDNT 249
Cdd:cd11267   264 V-LAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEElVPRPRPGCCAAPGMR---YNSSSTLPDEV 339
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801504 250 LNFIKKHPLMEEQVkPRLG-RPLLVKKNTNF--THVVADRILGLDGaTYTVLFIGTGDGWLLK 309
Cdd:cd11267   340 LNFVKTHPLMDEAV-PSLGhAPWIVRTMTRYqlTHMVVDTEAGPHG-NHTVVFLGSTRGTVLK 400
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
4-357 2.83e-64

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: 220.29  E-value: 2.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   4 FTLDRAEFE----DGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSA 78
Cdd:cd11269   100 YRLSTLEYDgeeiSGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTiKYDSKWIKEPHFLHAI 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  79 fvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQL 156
Cdd:cd11269   180 ----EYGNY------VYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSqRVLEKHWTSFLKARLNCSVPgDSFFYFDVL 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 157 RAVHTLLGASwHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARY-TDPVPTPRPGSCINNWHR 235
Cdd:cd11269   250 QSITDIIEIN-GIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVpEDKVPKPRPGCCAKHGLA 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 236 DnGYTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNF--THVVADRILGlDGATYTVLFIGTGDGWLLKAV-- 311
Cdd:cd11269   329 E-AYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYrlTAIAVDHAAG-PHQNYTVIFVGSEAGVVLKILak 406
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 312 ----SLGPWIhMVEELQVF----------DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 357
Cdd:cd11269   407 tspfSLNDSV-LLEEIEAYnhakcsaeneEDRRVISLQLDRDHHALFVAFSSCVVRIPLS 465
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
3-343 2.11e-62

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: 215.36  E-value: 2.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   3 TFTLDRAEFeDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPI--KTEYLAFWLNEPHFVGSAfv 80
Cdd:cd11270   101 SLEQDGEEV-IGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLGESSPVlrTVKYDSKWLREPHFLHAI-- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  81 peSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQLRA 158
Cdd:cd11270   178 --EYGNY------VYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPgDSFFYFDVLQS 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 159 VHTLLGASwHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARY-TDPVPTPRPGSCInNWHRDN 237
Cdd:cd11270   250 LTNVMQIN-HRPAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVpDEAVPKPRPGSCA-GDGPAA 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 238 GYTSSLELPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNF--THVVADRILGLDGaTYTVLFIGTGDGWLLKAVSLGP 315
Cdd:cd11270   328 GYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFklTQIAVDTAAGPYK-NYTVVFLGSENGHVLKVLASMH 406
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958801504 316 WIHMVEELQVFD---QEPVESLVLSQSKKVL 343
Cdd:cd11270   407 PNSSYSTQVLEDidvYNPNKCNVRGEDRRIL 437
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
2-357 4.67e-62

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: 213.69  E-value: 4.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   2 LTFTLDRAefeDGKGKCPYDPAKGHTGLLVD-GELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVgSAF 79
Cdd:cd11264    99 LSKVIERI---NGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGSVPPLRTaQYNSKWLNEPNFI-AAY 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  80 vpeSVGSFTgdddkiYFFFSERAVEYDCySEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP-DWKVYFNQLRA 158
Cdd:cd11264   175 ---DIGLFT------YFFFRENAVEHDC-GKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPgEIPFYYNELQS 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 159 VHTLLgaswHNTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCINNWHRDNg 238
Cdd:cd11264   245 TFYLP----EQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNEN- 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 239 ytssleLPDNTLNFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDgATYTVLFIGTGDGWLLKAVSL-GPWI 317
Cdd:cd11264   320 ------LTERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKD-TLYHVMYIGTEYGTILKALSTtNRSL 392
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1958801504 318 H--MVEELQVF---DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 357
Cdd:cd11264   393 RscYLEEMQILppgQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
14-356 3.23e-61

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: 211.43  E-value: 3.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  14 GKGKCPYDPAKGHTGLLV-DGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSAfvpeSVGSFTgdd 91
Cdd:cd11263   108 GMARCPYSPQHNSTALLTsSGELYAATAMDFPGRDPAIYRSLGILPPLRTaQYNSKWLNEPNFVSSY----DIGNFT--- 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  92 dkiYFFFSERAVEYDCySEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP-DWKVYFNQLRAVHTLLGASwhnt 170
Cdd:cd11263   181 ---YFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPgEIPFYYNELQSTFFLPELD---- 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 171 TFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYTDPVPTPRPGSCinnwhrDNGytSSLELPDNTL 250
Cdd:cd11263   253 LIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTM------DQG--LYVNLTERNL 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 251 NFIKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDgATYTVLFIGTGDGWLLKAvsLGPWIH-----MVEELQV 325
Cdd:cd11263   325 QDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKD-MLFHIIYLATDYGTIKKV--LAPLNQsssscLLEEIEL 401
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958801504 326 F---DQEPVESLVLSQSKKVLFAGSRSQLVQLSL 356
Cdd:cd11263   402 FpkrQREPIRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
13-357 4.15e-61

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: 210.47  E-value: 4.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  13 DGKGKCPYDPAKGHTGLLVDGELYSaTLNNFLGTEPvILRNMGPHHPIKTEylAFWLNEPHFVGSAFVPESvgsfTGDDD 92
Cdd:cd11243    96 ADRGVAPFLPDENSLVLIEGNNVYS-TISGKKGNIP-RFRRYGGKKELYTS--DTVMQKPQFVKATLLPED----EQYQD 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  93 KIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQ-KKWTTFLKARLVCSAPDWKVYFNQLRAVHTLLGASWHNTT 171
Cdd:cd11243   168 KIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLStSKWSTFLKARLVCGDPATPMNFNRLQDVFLLPKEEWREAV 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 172 FFAVFQARWGDmdlSAVCEYQLEHIQQVFegpfkeyseQAQKWARYTDPVPTPRPGSCInnwhrdngyTSSLELPDNTLN 251
Cdd:cd11243   248 VYGVFSNTWGS---SAVCSYSLGDIDKVF---------RTSSLKGYSGSLPNPRPGTCV---------PPEQTHPSETFS 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 252 FIKKHPLMEEQVKPRLGRPL-LVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIHMVEELQVF-DQE 329
Cdd:cd11243   307 FADEHPELDDRIEPDEPRKLpVFQNKDHYQKVVVDEVRASDGVSYDVLYLATDKGKIHKVVESKGQTHNIMEIQPFkEQE 386
                         330       340
                  ....*....|....*....|....*...
gi 1958801504 330 PVESLVLSQSKKVLFAGSRSQLVQLSLA 357
Cdd:cd11243   387 PIQSMILDAERSHLYVGTKAEVTRLPLD 414
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
13-356 1.44e-58

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: 204.32  E-value: 1.44e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  13 DGKGKCPYDPAKGHTGLLV-DGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSafvpESVGSFTgd 90
Cdd:cd11241   107 SGVARCPYSPAHNSTALISaSGELYAGTVYDFSGRDPAIYRSLGGKPPLRTaQYNSKWLNEPNFVGS----YEIGNHT-- 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  91 ddkiYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP-DWKVYFNQLRavhtllGASWH- 168
Cdd:cd11241   181 ----YFFFRENAVEHQDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPgEFPFYYNEIQ------GTFYLp 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 169 -NTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKeYSEQAQKWARytdPVPTPRPGSCINNWHRDNGYTSSLE--L 245
Cdd:cd11241   251 eTDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFK-YQENNGSAWL---PTPNPHPNFQCTTSIDRGQPANTTErdL 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 246 PDNtlnfiKKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGWLLKAVSLGPWIH--MVEEL 323
Cdd:cd11241   327 QDA-----QKYQLMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRGTQLVHIFYVGTDYGTILKMYQPHRSQKscTLEEI 401
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1958801504 324 QVF---DQEPVESLVLSQSKKVLFAGSRSQLVQLSL 356
Cdd:cd11241   402 KILpamKGEPITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
14-326 1.10e-55

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: 197.23  E-value: 1.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  14 GKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRNMGPHHPIKT-EYLAFWLNEPHFVGSafvpesvgsfTGDDD 92
Cdd:cd11268   113 GQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSaKYDSKWLREPHFVQA----------LEHGD 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  93 KIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQLRAVH---TLLGASw 167
Cdd:cd11268   183 HVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPgDSTFYFDVLQALTgpvNLHGRS- 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 168 hntTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYT-DPVPTPRPGSCINnwhrDNG---YTSSL 243
Cdd:cd11268   262 ---ALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVSeDRVPSPRPGSCAG----VGGaalFSSSR 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 244 ELPDNTLNFIKKHPLMEEQVKPRLGRPLL-VKKNTNFTHVVADRILGlDGATYTVLFIGTGDGWLLKAV-----SLGPWI 317
Cdd:cd11268   335 DLPDDVLTFIKAHPLLDPAVPPVTHQPLLtLTSRALLTQVAVDGMAG-PHSNITVMFLGSNDGTVLKVLppggrSGGPEP 413

                  ....*....
gi 1958801504 318 HMVEELQVF 326
Cdd:cd11268   414 ILLEEIDAY 422
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
2-357 1.38e-51

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: 183.95  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504   2 LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFL-GTEPVILRNMGPHHPIKTEYL-AFWLNEPHFVgSAF 79
Cdd:cd09295    98 VLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNVHYLRIVVDsSTGLDEITFV-YAF 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  80 VpesvgsFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWKVYFNQLRAV 159
Cdd:cd09295   177 V------SGDDDDEVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSRPQSGFAFNLLQDA 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 160 HTLLGASWHNtTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEgpfkeyseqaqkwarytDPVPtprpgscinnwhrdngy 239
Cdd:cd09295   251 TGDTKNLIQD-VKFAIFSSCLNKSVESAVCAYLFTDINNVFD-----------------DPVE----------------- 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 240 tsslelpdntlnfikkhplmeeqvkPRLGRPLLVKKNT--NFTHVVADRILGlDGATYTVLFIGTGDGWLLKAVSLGPWI 317
Cdd:cd09295   296 -------------------------AINNRPLYAHQNQrsRLTSIAVDATKQ-KSVGYQVVFLGLKLGSLGKALAFFFLY 349
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1958801504 318 --HMVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 357
Cdd:cd09295   350 kgHIIEEWKVFkDSSRITNLDLSRPPLYLYVGSESGVLGVPVQ 392
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
10-354 6.65e-50

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: 180.36  E-value: 6.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  10 EFEDGKGKCPYDPAKGHTGLLV-DGELYSATLNNFLGTEPVILRNMGP--HHPIKT-EYLAFWLNEPHFVGSAfvpESvg 85
Cdd:cd11265   104 EWDSGVAKCPYSPHANITALLSsSGQLFVGSPTDFSGSDSAIYRTLGTsnKSFLRTkQYNSKWLNEPQFVGSF---ET-- 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  86 sftgdDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQK-KWTTFLKARLVCSAP-DWKVYFNQLRavhtll 163
Cdd:cd11265   179 -----GNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLLKdNWTTFLKARLNCSLPgEYPFYFDEIQ------ 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 164 GASWH--NTTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKEYSEQAQKWARYtdpvptprpgsciNNWHRDN---- 237
Cdd:cd11265   248 GMTYLpdEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERV-------------NVNHRDHfnqc 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 238 GYTSSLELPDNTlnfikKHPLMEEQVKPRLGRPLLVKKNTNFTHVVADRILGLDGATYTVLFIGTGDGwLLKAVSLGPWI 317
Cdd:cd11265   315 SSSSSSHLLESS-----RYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKIHQSVHVLYVATTGG-LIKKISVLPRT 388
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958801504 318 H---MVEELQVFDQ--EPVESLVLSQSKKVLFAGSRSQLVQL 354
Cdd:cd11265   389 QetcLVEIWQPLPTpdSPIKTMQYLKVTDSLYVGTELALMRI 430
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
423-507 1.08e-19

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: 84.03  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 423 KNITVVAGTDLVLPCHLSSNLAHALWTFRGRDLPAEQPGsflYDTGLQALVVMAAQSRHSGPYHCYSEEQGTKLAAESYL 502
Cdd:cd05872     4 KFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSY---LRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYS 80

                  ....*
gi 1958801504 503 VSVVA 507
Cdd:cd05872    81 LNVVE 85
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
90-421 6.36e-16

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: 80.33  E-value: 6.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  90 DDDKIYFFFSERAVeydcyseqVVARVARVCKGDMGGARTLqkkwttflkarLVCSAPDWKVYFNQLRAVHTLLGAS-WH 168
Cdd:cd09295     1 DDDKILVSFRKDTI--------YVGAIARIYKVDGGGTRLL-----------LSCISPELNFGFNEDQKAFCPLRRGkWT 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 169 NTTFFAVFQARWGDMDLSAVCEY-----QLEHiqqvFEGPFKEYSEQAQKwarytdpvPTPRPGSCINNWHRDNGYTSsl 243
Cdd:cd09295    62 ECINYIKVLQQKGDLDILAVCGSnaaqpSCGS----YRLDVLVELGKVRW--------PSGRPRCPIDNKHSNMGVNV-- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 244 elpDNTLNFIKKHPLMEEQvkprlgRPLLVKK--NTNFTHVVADRILGLDGATYTVLFIGTGDgwllkavslgpwihmVE 321
Cdd:cd09295   128 ---DSKLYSATDHDFKDGD------RPALSRRssNVHYLRIVVDSSTGLDEITFVYAFVSGDD---------------DD 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 322 ELQVF-DQEPVESLvlsqSKKVLFAGSRSQLVQLSLADCTKYRFCVDCVLARDPYCAWnvntsrcvATGGHSGSLLVQHV 400
Cdd:cd09295   184 EVYFFfRQEPVEYL----KKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSR--------PQSGFAFNLLQDAT 251
                         330       340
                  ....*....|....*....|...
gi 1958801504 401 ANLDPSKMCIQYAI--KKARPVV 421
Cdd:cd09295   252 GDTKNLIQDVKFAIfsSCLNKSV 274
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
422-505 1.31e-12

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


Pssm-ID: 409368  Cd Length: 88  Bit Score: 64.02  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 422 PKNITVVAGTDLVLPCHLSSNLAHALWTFRGRDLPAEQPGSfLYDTGLQALVVMAAQSRHSGPYHCYSEEQGTKLAAESY 501
Cdd:cd04979     3 FKQISVKEGDTVILSCSVKSNNAPVTWIHNGKKVPRYRSPR-LVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSV 81

                  ....
gi 1958801504 502 LVSV 505
Cdd:cd04979    82 TLHV 85
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
358-387 1.17e-08

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 51.39  E-value: 1.17e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958801504  358 DCTKYRFCVDCVLARDPYCAWNVNTSRCVA 387
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRCTS 30
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
422-492 4.23e-08

Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. Sema4D is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4D has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4D plays a part in the development of GABAergic synapses. Sema4D in addition is an immune semaphorin. It is abundant on resting T cells; its expression is weak on resting B cells and antigen presenting cells (APCs), but is upregulated by various stimuli. The receptor used by Sema4D in the immune system is CD72. Sem4D enhances the activation of B cells and DCs through binding CD72, perhaps by reducing CD72s inhibitory signals. The receptor used by Sema4D in the non-lymphatic tissues is plexin-B1. Sem4D is anchored to the cell surface but its extracellular domain can be released from the cell surface by a metalloprotease-dependent process. Sem4D may mediate its effects in its membrane-bound form and/or its cleaved form.


Pssm-ID: 409457  Cd Length: 87  Bit Score: 50.97  E-value: 4.23e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801504 422 PKNITVVAGTDLVLPCHLSSNLAHALWTFRGRDLPAEQPGSFLYDtglQALVVMAAQSRHSGPYHCYSEEQ 492
Cdd:cd05873     3 PRQRTFKLGGNAELKCSPKSNLARVVWKFQGKVLKAESPKYGLYG---DGLLIFNASEADAGRYQCLSVEK 70
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
358-386 3.01e-07

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: 47.70  E-value: 3.01e-07
                          10        20
                  ....*....|....*....|....*....
gi 1958801504 358 DCTKYRFCVDCVLARDPYCAWNVNTSRCV 386
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCV 29
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
295-385 2.39e-06

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: 50.70  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 295 YTVLFIGTGDGWLLKAVSLGPWIHMV--EELQVF-DQEPV-ESLVLSQSKKVLFAGSRSQLVQLSLADCTKYRFCVDCVL 370
Cdd:cd11272   406 YSVVFVGTKSGKLKKIRADGPPHGGVqyEMVSVFkDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLS 485
                          90
                  ....*....|....*
gi 1958801504 371 ARDPYCAWNVNTSRC 385
Cdd:cd11272   486 SGDPHCGWCALHNMC 500
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
75-355 7.83e-06

The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor plays important roles in neural tube closure and cerebellar granule cell development. Mice lacking Plexin B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C-Plexin B2 signaling modulates ureteric branching. Plexin B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin B2 results in renal hypoplasia and occasional double ureters. 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: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 49.00  E-value: 7.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  75 VGSAFVPESVGSFT---GDDDKIYFFFSERaveyDCYSEQVVARVARVCKGDMGgartlqkkWTTFLKARLVCSAPDWKv 151
Cdd:cd11276   180 VKSAYVSRYTQQFRyafEDNNYVYFLFNQQ----LGHPDKNRTLIARLCENDHH--------YYSYTEMDLNCRDGANA- 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 152 yFNQLRAVHT-----LLGASWHN-----TTFFAVFQARWGDMDLSAVCEYQLEHIQQVFEGPFKE-YSEQAQKWARYTDP 220
Cdd:cd11276   247 -YNKCQAAYVstpgkELAQNYGNsilsdKVLFAVFSRDEKDSGESALCMFPLKSINAKMEANREAcYTGTIDDRDVFYKP 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 221 VPTPRPGSCINnwHRDNGYTS----SLELPdntlnfikkHPLMEEQvKPRLGRPLLVKKNTNFTHVVADRILGldgatYT 296
Cdd:cd11276   326 FHSQKDIICGS--HQQKNSKSfpcgSEHLP---------YPLGSRD-ELALTAPVLQRGGLNLTAVTVAVENG-----HT 388
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801504 297 VLFIGTGDGWLLKavslgpwIHMVEELQVFDQEPVE-------SLVLSQSKKVLFAGSRSQLVQLS 355
Cdd:cd11276   389 VAFLGTSDGRILK-------VHLSPDPEEYNSILIEknkpvnkDLVLDKTLEHLYIMTEDKVFRLP 447
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
422-496 6.14e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 6.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504  422 PKNITVVAGTDLVLPCHLSSNLAHAL-WTFRGRDLPAEQPG-SFLYDTGLQALVVMAAQSRHSGPYHC------YSEEQG 493
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVtWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCaatnssGSASSG 80

                   ...
gi 1958801504  494 TKL 496
Cdd:smart00410  81 TTL 83
Ig6_Contactin-4 cd05853
Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth ...
420-503 6.64e-05

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


Pssm-ID: 409439  Cd Length: 102  Bit Score: 42.30  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 420 VVPKNITVVAGTDLVLPCHLSSNlaHAL-----WTFRGRDLPAEQPGSFLYDTGLQA----LVVMAAQSRHSGPYHCYSE 490
Cdd:cd05853     7 VPPSSMDVTVGESIVLPCQVSHD--HSLdivftWSFNGHLIDFQKDGDHFERVGGQDsagdLMIRSIQLKHAGKYVCMVQ 84
                          90
                  ....*....|...
gi 1958801504 491 EQGTKLAAESYLV 503
Cdd:cd05853    85 TSVDKLSAAADLI 97
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
420-508 1.87e-03

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


Pssm-ID: 409359  Cd Length: 102  Bit Score: 38.30  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801504 420 VVPKNITVVAGTDLVLPCHLSSNLAHAL---WTFRGRDLPAEQPGSFLYDTGLQA----LVVMAAQSRHSGPYHCYSEEQ 492
Cdd:cd04970     7 LAPSNADITVGENATLQCHASHDPTLDLtftWSFNGVPIDLEKIEGHYRRRYGKDsngdLEIVNAQLKHAGRYTCTAQTV 86
                          90
                  ....*....|....*.
gi 1958801504 493 GTKLAAESYLvsVVAG 508
Cdd:cd04970    87 VDSDSASATL--VVRG 100
I-set pfam07679
Immunoglobulin I-set domain;
421-487 3.25e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 37.24  E-value: 3.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801504 421 VPKNITVVAGTDLVLPCHLSSN-LAHALWTFRGRDLPAEQPGSFLYDTGLQALVVMAAQSRHSGPYHC 487
Cdd:pfam07679   6 KPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
418-487 5.50e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.39  E-value: 5.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801504 418 RPVV---PKNITVVAGTDLVLPCHLSSN-LAHALWTFRGRDLPAEQPGSFLYDTGLQALVVMAAQSRHSGPYHC 487
Cdd:pfam13927   1 KPVItvsPSSVTVREGETVTLTCEATGSpPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTC 74
 
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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