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Conserved domains on  [gi|8134699|sp|Q64151|]
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RecName: Full=Semaphorin-4C; AltName: Full=M-Sema F; AltName: Full=Semaphorin-C-like 1; Short=Sema I; Short=Semaphorin I; Flags: Precursor

Protein Classification

immunoglobulin domain-containing protein( domain architecture ID 10181376)

immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and pattern recognition; similar to Drosophila melanogaster DIP/Dpr cell recognition proteins, which are members of the Wirin family of IgSF proteins with neuronal wiring functions, and human IgLON proteins, a family of cell adhesion molecules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
42-498 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: 933.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   42 VRRFSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYN 121
Cdd:cd11258   1 VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQTECFNYIRFLQPYN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  122 SSHLYVCGTYAFQPKCTYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSI 201
Cdd:cd11258  81 QSHLYTCGTYAFQPKCAYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  202 KTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKA 281
Cdd:cd11258 161 KTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  282 RLVCSAPDWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDP 361
Cdd:cd11258 241 RLLCSIPEWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  362 VPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGATYTVLFI 441
Cdd:cd11258 321 VPSPRPGSCINNWHRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSVLFI 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  442 GTGDGWLLKAVSLGPWIHMVEELQVFDQEPVESLVLSQS-KKVLFAGSRSQLVQLSLA 498
Cdd:cd11258 401 GTLDGWLIKAVSLGSWVHMIEELQVFDQEPPESLVVSQSsKKLLFAGSRSELLQLPWA 458
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
564-648 2.27e-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: 83.26  E-value: 2.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  564 KNITVVSGTDLVLPCHLSSNLAHAHWTFGSQDLPAEQPGsflYDTGLQALVVMAAQSRHSGPYRCYSEEQGTRLAAESYL 643
Cdd:cd05872   4 KFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSY---LRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYS 80

                ....*
gi 8134699  644 VAVVA 648
Cdd:cd05872  81 LNVVE 85
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
499-528 2.02e-08

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 51.01  E-value: 2.02e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 8134699     499 DCTKYRFCVDCVLARDPYCAWNVNTSRCVA 528
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 ...
42-498 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: 933.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   42 VRRFSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYN 121
Cdd:cd11258   1 VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQTECFNYIRFLQPYN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  122 SSHLYVCGTYAFQPKCTYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSI 201
Cdd:cd11258  81 QSHLYTCGTYAFQPKCAYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  202 KTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKA 281
Cdd:cd11258 161 KTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  282 RLVCSAPDWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDP 361
Cdd:cd11258 241 RLLCSIPEWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  362 VPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGATYTVLFI 441
Cdd:cd11258 321 VPSPRPGSCINNWHRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSVLFI 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  442 GTGDGWLLKAVSLGPWIHMVEELQVFDQEPVESLVLSQS-KKVLFAGSRSQLVQLSLA 498
Cdd:cd11258 401 GTLDGWLIKAVSLGSWVHMIEELQVFDQEPPESLVVSQSsKKLLFAGSRSELLQLPWA 458
Sema smart00630
semaphorin domain;
53-472 1.55e-139

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 418.70  E-value: 1.55e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699      53 FLTLTLTEHSGLLYVGAREALFAFSVEALELQGA-ISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYVCGTY 131
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELkTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     132 AFQPKCTYINMltftldraefedgkgkcpydpakghtgllvdGELYSATLNNFLGTEPVILRYMGTHH-------SIKTE 204
Cdd:smart00630  81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTV 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     205 YLAF-WLNEPHFVGSafvpesvgsFTgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARL 283
Cdd:smart00630 130 LYDSkWLNEPNFVYA---------FE-SGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARL 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     284 VCSAPDWK-VYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY-TDP 361
Cdd:smart00630 200 ECSVPGEDpFYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYsRGK 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     362 VPSPRPGSCINNWHrdngytSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTN--FTHVVADRVPGldGATYTVL 439
Cdd:smart00630 280 VPYPRPGTCPNKPP------SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNylLTSIAVDRVAT--DGNYTVL 351
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 8134699     440 FIGTGDGWLLKAVSLGP----WIHMVEELQVF-DQEPV 472
Cdd:smart00630 352 FLGTSDGRILKVVLSESssssESVVLEEISVFpDGSPI 389
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
297-479 1.65e-70

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: 229.85  E-value: 1.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699    297 LKAVHTLR--GASWHNTTFFGVFQARWGD-MDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDPVPSPRPGSCINN 373
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQWSNsIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699    374 WHRdngytssLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGaTYTVLFIGTGDGWLLKAVS 453
Cdd:pfam01403  81 PLR-------LDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDG-NYTVLFLGTDDGRLHKVVL 152
                         170       180
                  ....*....|....*....|....*...
gi 8134699    454 LGP-WIHMVEELQVFDQ-EPVESLVLSQ 479
Cdd:pfam01403 153 VGSeESHIIEEIQVFPEpQPVLNLLLSS 180
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
564-648 2.27e-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: 83.26  E-value: 2.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  564 KNITVVSGTDLVLPCHLSSNLAHAHWTFGSQDLPAEQPGsflYDTGLQALVVMAAQSRHSGPYRCYSEEQGTRLAAESYL 643
Cdd:cd05872   4 KFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSY---LRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYS 80

                ....*
gi 8134699  644 VAVVA 648
Cdd:cd05872  81 LNVVE 85
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
499-528 2.02e-08

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 51.01  E-value: 2.02e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 8134699     499 DCTKYRFCVDCVLARDPYCAWNVNTSRCVA 528
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRCTS 30
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
499-527 5.93e-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: 46.93  E-value: 5.93e-07
                          10        20
                  ....*....|....*....|....*....
gi 8134699    499 DCTKYRFCVDCVLARDPYCAWNVNTSRCV 527
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCV 29
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
563-637 1.39e-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: 44.03  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     563 PKNITVVSGTDLVLPCHLSSN-LAHAHWTFGSQDLPAEQPG-SFLYDTGLQALVVMAAQSRHSGPYRC------YSEEQG 634
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSpPPEVTWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCaatnssGSASSG 80

                   ...
gi 8134699     635 TRL 637
Cdd:smart00410  81 TTL 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
558-628 6.08e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 6.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8134699    558 KVRSIPKNITVVSGTDLVLPCHLSSN-LAHAHWTFGSQDLPAEQPGSFLYDTGLQALVVMAAQSRHSGPYRC 628
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSpPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTC 74
 
Name Accession Description Interval E-value
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
42-498 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: 933.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   42 VRRFSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYN 121
Cdd:cd11258   1 VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQTECFNYIRFLQPYN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  122 SSHLYVCGTYAFQPKCTYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSI 201
Cdd:cd11258  81 QSHLYTCGTYAFQPKCAYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  202 KTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKA 281
Cdd:cd11258 161 KTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  282 RLVCSAPDWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDP 361
Cdd:cd11258 241 RLLCSIPEWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  362 VPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGATYTVLFI 441
Cdd:cd11258 321 VPSPRPGSCINNWHRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSVLFI 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  442 GTGDGWLLKAVSLGPWIHMVEELQVFDQEPVESLVLSQS-KKVLFAGSRSQLVQLSLA 498
Cdd:cd11258 401 GTLDGWLIKAVSLGSWVHMIEELQVFDQEPPESLVVSQSsKKLLFAGSRSELLQLPWA 458
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
45-498 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: 830.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   45 FSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEAL--ELQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNS 122
Cdd:cd11240   1 FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDIstELKDKIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  123 SHLYVCGTYAFQPKCTYINMLTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIK 202
Cdd:cd11240  81 THLYVCGTFAFSPRCTYINLSDFSLSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEGNVLK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  203 TEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKAR 282
Cdd:cd11240 161 TENTLRWLNEPAFVGSAHIRESIDSPDGDDDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGGQRTLQKKWTTFLKAQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  283 LVCSAPDWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDPV 362
Cdd:cd11240 241 LVCSQPDSGLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRYTGPV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  363 PSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRlGRPLLVKKNTNFTHVVADRVPGLDGATYTVLFIG 442
Cdd:cd11240 321 PDPRPGACITNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPI-NRPLLVKSGVNYTRIAVHRVQALDGQTYTVLFLG 399
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8134699  443 TGDGWLLKAVSLGPWIHMVEELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11240 400 TEDGFLHKAVSLDGGMHIIEEIQLFDQpQPVKNLLLSSSKGVLYVGSSSGVVQVPLS 456
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
43-497 0e+00

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: 592.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   43 RRFSqTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALE--LQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPY 120
Cdd:cd11262   1 RRFR-GPAQNYSTLLLEDESGRLYVGARGAIFSLNASDISdsSALTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  121 NSSHLYVCGTYAFQPKCTYINMLTFTLDrAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTePVILRYMgTHHS 200
Cdd:cd11262  80 NSTHLYTCGTHAFRPLCAYIDAERFTLS-SQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQYEFRSF-PDIRRNS-PQPT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  201 IKTEYLAF-WLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVE-YDCYSEQVVARVARVCKGDMGGARTLQKKWTTF 278
Cdd:cd11262 157 LRTEEAPTrWLNDADFVGSVLVRESMNSSVGDDDKIYFFFTERSQEeTAYFSQSRVARVARVCKGDRGGKKTLQRKWTSF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  279 LKARLVCSAPDWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY 358
Cdd:cd11262 237 LKARLVCYIPEYEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRY 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  359 TDPVPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGATYTV 438
Cdd:cd11262 317 TGKVPEPRPGSCITDEHRSQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDGRVYDV 396
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  439 LFIGTGDGWLLKAVSLGPWIHMVEELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSL 497
Cdd:cd11262 397 LFLGTDEGWLHKAVVIGSAVHIIEELQVFREpQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
44-498 5.02e-174

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: 510.17  E-value: 5.02e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   44 RFSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEAL---ELQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPY 120
Cdd:cd11257   1 RFEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDIsptGEQQELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  121 NSSHLYVCGTYAFQPKCTYINMLTFTLDRAE-----FEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYM 195
Cdd:cd11257  81 NSTHLFTCGTYAFSPICTYIVMTNFSLERDEkgeplLEDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIYRSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  196 GTHHSIKTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKW 275
Cdd:cd11257 161 GSGTPLKTENSLNWLQDPAFVGSAYIQESLPKLVGDDDKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGGERVLQKRW 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  276 TTFLKARLVCSAPDWKVYFNQLKAVHTLRGAS--WHNTTFFGVFQARW--GDMDLSAVCEYQLEQIQQVFEGPYKEYSEQ 351
Cdd:cd11257 241 TTFLKAQLLCSLPDDGFPFNVLQDVFVLTPSPedWKDTLFYGVFTSQWhkGTAGSSAVCVFTMDQVQRAFNGLYKEVNRE 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  352 AQKWARYTDPVPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKprlGRPLLVKKNTNFTHVVADRVPGL 431
Cdd:cd11257 321 TQQWYTYTHPVPEPRPGACITNSARERKINSSLHMPDRVLNFVKDHFLMDGQVR---SQPLLLQPQVRYTQIAVHRVKGL 397
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  432 DgATYTVLFIGTGDGWLLKAVSLGPWIHMVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11257 398 H-KTYDVLFLGTDDGRLHKAVSVGPMVHIIEELQIFsEGQPVQNLLLDTHKGLLYASSHSGVVQVPVA 464
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
45-498 1.05e-173

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: 509.40  E-value: 1.05e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   45 FSQTGIQDFLTLTLTEHSGLLYVGAREALFAFS-VEALELQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSS 123
Cdd:cd11259  12 FHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNaLNISEKQHELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLNDT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  124 HLYVCGTYAFQPKCTYINMLTFTLDrAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYmgTHHS-IK 202
Cdd:cd11259  92 FLYVCGTNAFQPTCDYLNLTSFRLL-GKNEDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRN--SSQSpLR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  203 TEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKAR 282
Cdd:cd11259 169 TEYAIPWLNEPSFVFADVIRADPDSPDGEDDKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKAR 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  283 LVCSAPDWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVF-EGPYKEYS--EQAQ-KWARY 358
Cdd:cd11259 249 LICSIPDKNLVFNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFsKGKYMQSAtvEQSHtKWVRY 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  359 TDPVPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGATYTV 438
Cdd:cd11259 329 NGEVPKPRPGACINNEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDGTIYDV 408
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8134699  439 LFIGTGDGWLLKAVSLGPWIHMVEELQVF-DQEPVESLVLS--QSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11259 409 MFISTDRGALHKAISLENEVHIIEETQLFpDFEPVQTLLLSskKGRRFLYAGSNSGVVQSPLA 471
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
45-498 1.77e-159

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: 472.47  E-value: 1.77e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   45 FSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGA-ISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSS 123
Cdd:cd11260   1 FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAkVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMNDS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  124 HLYVCGTYAFQPKCTYInmlTFTLDRAEFE----DGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRymGTHH 199
Cdd:cd11260  81 RMYVCGTNAFSPTCDYI---SYDDGQLTLEgkqeDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMR--SSPI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  200 SIKTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFL 279
Cdd:cd11260 156 TIRTEFKSSWLNEPNFIYMAAVPESEDSPEGDDDKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQKKWTSFL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  280 KARLVCSAPDWKVYFnQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVF-EGPYK-----EYSEqaQ 353
Cdd:cd11260 236 KARLDCSVPEPSLPY-VIQDVFHVCHQDWRKCVFYAVFTSQSDSSQSSAVCAYNVTDISNVFsRGKFKtpvavETSF--V 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  354 KWARYTDPVPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDG 433
Cdd:cd11260 313 KWVMYSGELPVPRPGACINNAARTSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADG 392
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8134699  434 ATYTVLFIGTGDGWLLKAVSLGPWIHMVEELQVFD-QEPVESLVLSQskKVLFAGSRSQLVQLSLA 498
Cdd:cd11260 393 QSYPVMFIGTANGYVLKAVNYDGEMHIIEEVQLFEpEEPIDILRLSQ--NQLYAGSASGVVQMPVS 456
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
52-498 3.67e-149

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: 445.31  E-value: 3.67e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   52 DFLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSnQTECFNFIRFLQPYNSSHLYVCGTY 131
Cdd:cd11235   2 KYHTKLLHEDRSTLYVGARDRVYLVDLDSLYTEQKVAWPSSPDDVDTCYLKGKS-KDDCRNFIKVLEKNSDDSLLVCGTN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  132 AFQPKCTYINMLTFTLDrAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKTEY-LAFWL 210
Cdd:cd11235  81 AFNPSCRNYNVETFELV-GKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYhDSKWL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  211 NEPHFVGSAFVPesvgsftgddDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP-D 289
Cdd:cd11235 160 NEPQFVGAFDIG----------DYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPgE 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  290 WKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTD-PVPSPRPG 368
Cdd:cd11235 230 FPFYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDeRVPEPRPG 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  369 SCinnwhrdngYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKK--NTNFTHVVADRVPGLDGATYTVLFIGTGDG 446
Cdd:cd11235 310 TC---------VDDSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTdvNYRFTKIAVDRVQAKLGQTYDVLFVGTDRG 380
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8134699  447 WLLKAVSLGPW----IHMVEELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11235 381 IILKVVSLPEQglqaSNILEEMPVGPPpEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
49-500 1.80e-146

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: 439.49  E-value: 1.80e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   49 GIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQG-AISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYV 127
Cdd:cd11239   6 NSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPkKIYWPASPERIEECKMAGKDPNTECANFVRVLQPYNRTHLYA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  128 CGTYAFQPKCTYINM------LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSI 201
Cdd:cd11239  86 CGTGAFHPICAFINVgrrledPIFKLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLGHRHYI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  202 KTE-YLAFWLNEPHFVGSAFVPESvgsFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLK 280
Cdd:cd11239 166 RTEqYDSRWLNEPKFVGAYLIPDS---DNPDDDKVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  281 ARLVCSAPD---WKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWAR 357
Cdd:cd11239 243 ARLVCSVPGpdgIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVE 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  358 YTDPVPSPRPGSCINNWHrDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTN--FTHVVADRVPGLDGaT 435
Cdd:cd11239 323 YQGKVPYPRPGTCPSKTY-GPLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPyrLTQIAVDRVEAEDG-Q 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8134699  436 YTVLFIGTGDGWLLKAVSL--GPWIH---MVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 500
Cdd:cd11239 401 YDVLFIGTDSGTVLKVVSLpkENWEMeevILEELQVFkHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
44-521 9.34e-144

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: 431.64  E-value: 9.34e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   44 RFSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVE---ALELQGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPY 120
Cdd:cd11256   1 RFRQENVHNYDQLLLSPDETTLYVGARDNILALGIRtpgPIRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  121 NSSHLYVCGTYAFQPKCTYINMLTFTLDRA----EFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMG 196
Cdd:cd11256  81 NGTHLYTCGTYAFSPACTYIELDHFSLPPPngtiITMDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  197 THHSIKTEYLAFWLN-EPHFVGSAFVPEsvgsftgdDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKW 275
Cdd:cd11256 161 TKVSLKTDGFLRWLNaDAVFVASFNPQG--------DSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKW 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  276 TTFLKARLVCSAPDwKVYFNQLKAVHTLRGASWHNTTFFGVFQARW--GDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQ 353
Cdd:cd11256 233 TTFLKAQLTCSQQG-HFPFNVIHHVALLNQPDPNNSVFYAVFTSQWqlGGRRSSAVCAYKLNDIEKVFNGKYKELNKESS 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  354 KWARYTDPVPSPRPGSCinnwhrdNGYTSSlelpDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDG 433
Cdd:cd11256 312 RWTRYMGPVSDPRPGSC-------SGGKSS----DKALNFMKDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSG 380
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  434 ATYTVLFIGTGDGWLLKAVSLGPWI-HMVEELQVF-DQEPVESLVLSqskkvlfagsrsqlvqlsladCTKyrfcvDCVL 511
Cdd:cd11256 381 HNYTVMFLGTDKGFLHKAVLMGGSEsHIIEEIELLtPPEPVENLLLA---------------------ANE-----GVVY 434
                       490
                ....*....|
gi 8134699  512 ARDPYCAWNV 521
Cdd:cd11256 435 IGYSAGVWRV 444
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
44-495 1.87e-141

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: 426.22  E-value: 1.87e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   44 RFSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGA-ISWEAPAEKKIECTQKGKsNQTECFNFIRFLQPYNS 122
Cdd:cd11261   5 RFSAPHTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERPRrIDWMVPEAHRQNCRKKGK-KEAECHNFIRILAIANA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  123 SHLYVCGTYAFQPKCTYINMLTF-TLDRaeFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMG-THHS 200
Cdd:cd11261  84 SHLLTCGTFAFDPKCGVIDVSSFqQVER--LESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAVGrAEEW 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  201 IKTEYLAFWLNEPHFVGSAFVPESVGSFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLK 280
Cdd:cd11261 162 IRTETLPSWLNAPAFVAAVFLSPAEWGDEDGDDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLK 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  281 ARLVCSAPDWKVYFNQLKAVHTLRGASWHNTT-FFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYT 359
Cdd:cd11261 242 ADLLCPGPEHGRASSILQDVTTLRPLPGAGTPiFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGLPVM 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  360 DP-VPSPRPGSCINNWHRDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGATYTV 438
Cdd:cd11261 322 DSdVPQPRPGECITNNMKLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAAHRVTSLSGKEYDV 401
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  439 LFIGTGDGWLLKAVSLGPWIHMVEELQVF-DQEPVESLVLSQSkkVLFAGSRSQLVQL 495
Cdd:cd11261 402 LYLGTEDGHLHRAVRIGAQLSVLEDLALFpEPQPVENLQLHHN--WLLVGSDTEVTQI 457
Sema smart00630
semaphorin domain;
53-472 1.55e-139

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 418.70  E-value: 1.55e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699      53 FLTLTLTEHSGLLYVGAREALFAFSVEALELQGA-ISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYVCGTY 131
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELkTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     132 AFQPKCTYINMltftldraefedgkgkcpydpakghtgllvdGELYSATLNNFLGTEPVILRYMGTHH-------SIKTE 204
Cdd:smart00630  81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTV 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     205 YLAF-WLNEPHFVGSafvpesvgsFTgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARL 283
Cdd:smart00630 130 LYDSkWLNEPNFVYA---------FE-SGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARL 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     284 VCSAPDWK-VYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY-TDP 361
Cdd:smart00630 200 ECSVPGEDpFYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYsRGK 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     362 VPSPRPGSCINNWHrdngytSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTN--FTHVVADRVPGldGATYTVL 439
Cdd:smart00630 280 VPYPRPGTCPNKPP------SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNylLTSIAVDRVAT--DGNYTVL 351
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 8134699     440 FIGTGDGWLLKAVSLGP----WIHMVEELQVF-DQEPV 472
Cdd:smart00630 352 FLGTSDGRILKVVLSESssssESVVLEEISVFpDGSPI 389
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
26-500 8.31e-120

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: 371.25  E-value: 8.31e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   26 NLVPRKTVSSGELVTVVRRFSQTGIQD---FLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQK 102
Cdd:cd11249   2 NNVPRLKLSYKEMLESNNLITFNGLANsssYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKWA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  103 GKSNQTECFNFIRFLQPYNSSHLYVCGTYAFQPKCTYINM------LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGEL 176
Cdd:cd11249  82 GKDILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVghhpedNIFRLEDSHFENGRGKSPYDPKLLTASLLIDGEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  177 YSATLNNFLGTEPVILRYMGTHHSIKTE-YLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDCYSEQVVA 255
Cdd:cd11249 162 YSGTAADFMGRDFAIFRTLGHHHPIRTEqHDSRWLNDPRFISAHLIPESDNP---EDDKIYFFFRENAIDGEHTGKATHA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  256 RVARVCKGDMGGARTLQKKWTTFLKARLVCSAPDWK---VYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEY 332
Cdd:cd11249 239 RIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNgidTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMY 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  333 QLEQIQQVFEGPYKEYSEQAQKWARYTDPVPSPRPGSCINNWHrdNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPL 412
Cdd:cd11249 319 SMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTF--GGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPI 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  413 LVKKNTN--FTHVVADRVPGLDGaTYTVLFIGTGDGWLLKAVSL--GPWIH----MVEELQVFdQEP--VESLVLSQSKK 482
Cdd:cd11249 397 IIKTDVDyqFTQIVVDRVEAEDG-QYDVMFIGTDMGTVLKVVSIpkETWHDleevLLEEMTVF-REPtaISAMELSTKQQ 474
                       490
                ....*....|....*...
gi 8134699  483 VLFAGSRSQLVQLSLADC 500
Cdd:cd11249 475 QLYIGSAIGVSQLPLHRC 492
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
53-500 4.26e-118

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: 366.16  E-value: 4.26e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   53 FLTLTLTEHSGLLYVGAREALFAFSVEALELQG-AISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYVCGTY 131
Cdd:cd11250  10 YDALLLDEERGRLFVGAKNYLASLSLDNISKQEkKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHLYACGTG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  132 AFQPKCTYINM------LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKTE- 204
Cdd:cd11250  90 AFHPTCAFVEVgqrmedHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRPSLRTEq 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  205 YLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLV 284
Cdd:cd11250 170 HDSRWLNEPKFVKVFWIPESENP---DDDKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLV 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  285 CSAP---DWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDP 361
Cdd:cd11250 247 CSVPgneGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGK 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  362 VPSPRPGSCINNWHrdNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTN--FTHVVADRVPGLDGAtYTVL 439
Cdd:cd11250 327 VPYPRPGMCPSKTF--GSFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPytFTQIAVDRVAAADGH-YDVM 403
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  440 FIGTGDGWLLKAVSL--GPWIHM----VEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 500
Cdd:cd11250 404 FIGTDVGSVLKVISVpkGSWPSNeellLEELHVFkDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
51-500 9.38e-118

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: 365.39  E-value: 9.38e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   51 QDFLTLTLTEHSGLLYVGAREALFAFSVEALELQ-GAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYVCG 129
Cdd:cd11252   8 LDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNpKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNRTHVYVCG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  130 TYAFQPKCTYINMLT------FTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGT---HHS 200
Cdd:cd11252  88 TGAFHPTCGYIELGThkedriFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLGPtpdHHY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  201 IKTEYLA-FWLNEPHFVGSAFVPESvgsFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFL 279
Cdd:cd11252 168 IRTDISEhYWLNGAKFIGTFPIPDT---YNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKWTTFL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  280 KARLVCSAPDWK---VYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWA 356
Cdd:cd11252 245 KARLVCSIPGPDgadTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWV 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  357 RYTDPVPSPRPGSCINNWHrDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNF--THVVADRVPGLDGa 434
Cdd:cd11252 325 QYEGRIPYPRPGTCPSKTY-DPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYrlTQIVVDHVAAEDG- 402
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8134699  435 TYTVLFIGTGDGWLLKAVSLGP--WIH---MVEELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLADC 500
Cdd:cd11252 403 QYDVMFLGTDIGTVLKVVSITKekWTMeevVLEELQIFKHpSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
49-500 7.75e-113

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: 352.29  E-value: 7.75e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   49 GIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQG-AISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYV 127
Cdd:cd11255   6 GDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAkEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNRTHLLA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  128 CGTYAFQPKCTYINM-----LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIK 202
Cdd:cd11255  86 CGTGAFQPVCALINVghrgeHVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFGTRSPLR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  203 TEYLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDCYSEQV-VARVARVCKGDMGGARTLQKKWTTFLKA 281
Cdd:cd11255 166 TETDQRLLHEPRFVAAHLIPDNADR---DNDKVYFFFTERATETAEDDDGAiHSRVGRLCANDAGGQRVLVNKWSTFIKA 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  282 RLVCSAP---DWKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY 358
Cdd:cd11255 243 RLVCSVPgphGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPY 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  359 TDPVPSPRPGSCINNWHRDNG--YTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNT--NFTHVVADRVPGLDGa 434
Cdd:cd11255 323 EGKVPYPRPGVCPSKITAQPGraFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLpyRLTQIVVDRVEAEDG- 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8134699  435 TYTVLFIGTGDGWLLKAVSLG------PWIHMVEELQVFD-QEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 500
Cdd:cd11255 402 YYDVMFIGTDSGSVLKVIVLQkgnsaaGEEVTLEELQVFKvPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
52-500 3.25e-112

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: 350.66  E-value: 3.25e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   52 DFLTLTLTEHSGLLYVGAREALFAFSVEALELQG-AISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYVCGT 130
Cdd:cd11254   9 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPlIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNRTHLYVCGT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  131 YAFQPKCTYINM------LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKTE 204
Cdd:cd11254  89 GAYNPVCAYINRgrraedYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMGKQPAMRTD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  205 -YLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDcYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARL 283
Cdd:cd11254 169 qYNSRWLNDPAFVHAHLIPDSSEK---NDDKLYFFFREKSLEAP-QSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  284 VCSAPDW---KVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTD 360
Cdd:cd11254 245 VCSVPGAdgiETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTG 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  361 PVPSPRPGSCINNWHRDNgYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTN--FTHVVADRVPGLDGaTYTV 438
Cdd:cd11254 325 KIPYPRPGTCPGGTFTPS-MKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNyrFTTIAVDQVDAADG-RYEV 402
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  439 LFIGTGDGWLLKAVSLGPWIH-----MVEELQVFDQ-EPVESLVLSQSKKVLFAGSRSQLVQLSLADC 500
Cdd:cd11254 403 LFLGTDRGTVQKVIVLPKDDLeteelTLEEVEVFKVpAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
53-500 1.48e-109

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: 342.77  E-value: 1.48e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   53 FLTLTLTEHSglLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSnQTECFNFIRFLQPYNSSHLYVCGTYA 132
Cdd:cd11237   7 FKLLDQDGNS--LLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKS-EDDCQNYIRVLAKKSAGRLLVCGTNA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  133 FQPKCTYINMLTFT-LDRAEFeDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRymgthHSIKTE-YLAFWL 210
Cdd:cd11237  84 YKPLCREYTVKDGGyRVEREF-DGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYR-----EPLRTErYDLKQL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  211 NEPHFVGSafvpesvgsFTgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKARLVCSAP-D 289
Cdd:cd11237 158 NAPNFVSS---------FA-YGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPgE 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  290 WKVYFNQLKAVHTL---RGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY-TDPVPSP 365
Cdd:cd11237 228 YPFYFNEIQSTSDIvegGYGGKSAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVpSNKVPEP 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  366 RPGSCINNwhrdngytsSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTN--FTHVVAD-RVPGLDGATYTVLFIG 442
Cdd:cd11237 308 RPGQCVND---------SRTLPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQyrFTQIAVDpQVKALDGKYYDVLFIG 378
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8134699  443 TGDGWLLKAV--------SLGPWIHmVEELQVFDQ-EPVESLVLSQSKKV--LFAGSRSQLVQLSLADC 500
Cdd:cd11237 379 TDDGKVLKAVniasadtvDKVSPVV-IEETQVFPRgVPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
46-500 3.72e-101

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: 321.80  E-value: 3.72e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   46 SQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEAL-ELQGAISWEAPAEKKIECTQKGKsNQTECFNFIRFLQPYNSSH 124
Cdd:cd11253   3 SPFGFLDLHTMLLDEYQERLFVGGRDLLYSLSLERIsANYKEIHWPSTQLQVEDCIMKGR-DKPECANYIRVLHHYNRTH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  125 LYVCGTYAFQPKCTYINM------LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTH 198
Cdd:cd11253  82 LLACGTGAFDPVCAFIRVgrgsedHLFQLESDKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMNHL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  199 HSIKTEYLA-FWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTT 277
Cdd:cd11253 162 AHIRTEHDDeRLLKEPKFVGSYMIPDNEDP---DDNKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRMLVNKWST 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  278 FLKARLVCSAPDWK---VYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQK 354
Cdd:cd11253 239 FLKTRLICSVPGPNgidTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYH 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  355 WARYTDPVPSPRPGSC---INNWHrdngYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKN--TNFTHVVADRVP 429
Cdd:cd11253 319 WSVYEGKVPYPRPGSCaskVNGGH----YGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDgkYNLKQIAVDRVE 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  430 GLDGaTYTVLFIGTGDGWLLKAVSlgpwIH----------MVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11253 395 AEDG-QYDVLFIGTDNGIVLKVIT----IYnqetetmeevILEELQVFkVPVPIISMEISSKRQQLYIGSESGVAQIRFH 469

                ..
gi 8134699  499 DC 500
Cdd:cd11253 470 QC 471
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
52-500 1.81e-97

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: 312.21  E-value: 1.81e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   52 DFLTLTLTEHSGLLYVGAREALFAFSVEALElQGAIS--WEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSSHLYVCG 129
Cdd:cd11251   9 DYRILFMDEDQDRIYVGSKDHILSLNINNIS-QDALSifWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNRTHLYVCG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  130 TYAFQPKCTYINM------LTFTLDrAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKT 203
Cdd:cd11251  88 SGAFSPVCVYVNRgrrseeQVFHID-SKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  204 -EYLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKAR 282
Cdd:cd11251 167 dQHNSKWLSEPIFVDAHLIPDGTDP---NDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKAR 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  283 LVCSAPD---WKVYFNQLKAVHTLRGASWHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYT 359
Cdd:cd11251 244 LVCSVMDedgTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQ 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  360 DPVPSPRPGSCINNWHRDNgYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTN--FTHVVADRVPGLDGaTYT 437
Cdd:cd11251 324 GRIPYPRPGTCPGGAFTPN-MQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDykYTKIAVDRVNAADG-RYH 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8134699  438 VLFIGTGDGWLLKAVSL-------GPWIhmVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLADC 500
Cdd:cd11251 402 VLFLGTDKGTVQKVVVLptngslsGELI--LEELEVFkNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
50-470 5.47e-96

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: 307.91  E-value: 5.47e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   50 IQDFLTLTLTehsglLYVGAREALFAFSVEALELQG-----AISWEAPAEKKIECTQKGKsNQTECFNFIRFLQPYNSSH 124
Cdd:cd11242  11 FQRMLRINRT-----LYIAARDHVYTVDLDASHTEEivpskKLTWRSRQADVENCRMKGK-HKDECHNFIKVLVPRNDET 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  125 LYVCGTYAFQPKCTYINMLTFTLDRAEFEdGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKT- 203
Cdd:cd11242  85 LFVCGTNAFNPVCRNYRIDTLEQDGEEIS-GMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSLGDSPTLRTv 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  204 EYLAFWLNEPHFVGSAfvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKAR 282
Cdd:cd11242 164 KYDSKWLKEPHFVHAV----EYGDY------VYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGSpRVLEKQWTSFLKAR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  283 LVCSAP-DWKVYFNQLKAVHTLRGASwHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYT-D 360
Cdd:cd11242 234 LNCSVPgDSHFYFDVLQAVTDVIRIN-GRPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPeD 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  361 PVPSPRPGSCINNWHRDnGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNF--THVVADRVPGLDGaTYTV 438
Cdd:cd11242 313 RVPKPRPGCCAGSGSAE-KYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYrlTQIAVDNAAGPYQ-NYTV 390
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 8134699  439 LFIGTGDGWLLKAV-----SLGPWIHMVEELQVFDQE 470
Cdd:cd11242 391 VFLGSEAGTVLKFLarigpSGSNGSVFLEEIDVYNPA 427
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
45-498 1.19e-83

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: 274.17  E-value: 1.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   45 FSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSnQTECFNFIRFLQpYNSSH 124
Cdd:cd11264   1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKT-EEECQNYVRVLI-VYGKK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  125 LYVCGTYAFQPKCT--YINMLTFTLDRAefeDGKGKCPYDPAKGHTGLLVD-GELYSATLNNFLGTEPVILRYMGTHHSI 201
Cdd:cd11264  79 VFTCGTNAFSPVCTsrQVGNLSKVIERI---NGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGSVPPL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  202 KT-EYLAFWLNEPHFVgSAFvpeSVGSFTgdddkiYFFFSERAVEYDCySEQVVARVARVCKGDMGGARTLQKKWTTFLK 280
Cdd:cd11264 156 RTaQYNSKWLNEPNFI-AAY---DIGLFT------YFFFRENAVEHDC-GKTVYSRVARVCKNDIGGRFLLEDTWTTFMK 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  281 ARLVCSAP-DWKVYFNQLKAVHTLRgaswHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYT 359
Cdd:cd11264 225 ARLNCSRPgEIPFYYNELQSTFYLP----EQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTA 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  360 DPVPSPRPGSCINNWHRDNgytssleLPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDgATYTVL 439
Cdd:cd11264 301 NPIPNFQCGTLSDDSPNEN-------LTERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKD-TLYHVM 372
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8134699  440 FIGTGDGWLLKAVSL-GPWIH--MVEELQVF---DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11264 373 YIGTEYGTILKALSTtNRSLRscYLEEMQILppgQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
45-497 2.02e-83

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: 273.66  E-value: 2.02e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   45 FSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSNQtECFNFIRFLQPYNSSh 124
Cdd:cd11241   1 FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSVE-ECQNYVRVLLVVGKN- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  125 LYVCGTYAFQPKCTY--INMLTFTLDRAefeDGKGKCPYDPAKGHTGLLV-DGELYSATLNNFLGTEPVILRYMGTHHSI 201
Cdd:cd11241  79 LFTCGTYAFSPVCTIrkLSNLTQILDTI---SGVARCPYSPAHNSTALISaSGELYAGTVYDFSGRDPAIYRSLGGKPPL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  202 KT-EYLAFWLNEPHFVGSafvpESVGSFTgdddkiYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLK 280
Cdd:cd11241 156 RTaQYNSKWLNEPNFVGS----YEIGNHT------YFFFRENAVEHQDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  281 ARLVCSAP-DWKVYFNQLKavhtlrGASWH--NTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKeYSEQAQKWAR 357
Cdd:cd11241 226 ARLNCSLPgEFPFYYNEIQ------GTFYLpeTDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFK-YQENNGSAWL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  358 ytdPVPSPRPGSCINNWHRDNGYTSSLE--LPDNtlnfiKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGAT 435
Cdd:cd11241 299 ---PTPNPHPNFQCTTSIDRGQPANTTErdLQDA-----QKYQLMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRGTQL 370
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8134699  436 YTVLFIGTGDGWLLKAVSLGPWIH--MVEELQVF---DQEPVESLVLSQSKKVLFAGSRSQLVQLSL 497
Cdd:cd11241 371 VHIFYVGTDYGTILKMYQPHRSQKscTLEEIKILpamKGEPITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
53-498 6.64e-82

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: 270.06  E-value: 6.64e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   53 FLTLTLTEHSGLLYVGAREALFAFSVEALELQGAI----SWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNS-SHLYV 127
Cdd:cd11238   3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINDTGNNcardELTLSPSDVSECVSKGKDEEYECRNHVRVIQPMGDgQTLYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  128 CGTYAFQPKCTYINMLTFTLD--RAEFEDGKGKCPYDPAKGHTGLLVDG-------ELYSATLNNFLGTEPVILR---YM 195
Cdd:cd11238  83 CSTNAMNPKDRVLDANLLHLPeyVPGPGNGIGKCPYDPDDNSTAVWVEWgnpgdlpALYSGTRTEFTKANTVIYRpplYN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  196 GT----HHSIKT-EYLAFWLNEPHFVGSAfvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGART 270
Cdd:cd11238 163 NTkgrhESFMRTlKYDSKWLDEPNFVGSF----DIGDY------VYFFFRETAVEYINCGKVVYSRVARVCKKDTGGKNV 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  271 LQKKWTTFLKARLVCSAP-DWKVYFNQLKAVHTLRGASwhNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVF-EGPYKEY 348
Cdd:cd11238 233 LRQNWTTFLKARLNCSISgEFPFYFNEIQSVYKVPGRD--DTLFYATFTTSENGFTGSAVCVFTLSDINAAFdTGKFKEQ 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  349 SEQAQKW-ARYTDPVPSPRPGSCINNwhrdngytsSLELPDNTLNFIKKHPLMEDQVKPrlGRPLLVKKNTNFTHVVADR 427
Cdd:cd11238 311 ASSSSAWlPVLSSEVPEPRPGTCVND---------SATLSDTVLHFARTHPLMDDAVSH--GPPLLYLRDVVFTHLVVDK 379
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8134699  428 VPGlDGATYTVLFIGTGDGWLLKAVSlgpWIH-------MVEELQVFDQEPVESLVLSQSKKvLFAGSRSQLVQLSLA 498
Cdd:cd11238 380 LRI-DDQEYVVFYAGSNDGKVYKIVH---WKDagesksnLLDVFELTPGEPIRAMELLPGEF-LYVASDHRVSQIDLA 452
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
65-498 9.88e-82

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: 269.98  E-value: 9.88e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   65 LYVGAREALFAFSVEAL---ELQGA--ISWEAPAEKKIECTQKGKsNQTECFNFIRFLQPYNSSHLYVCGTYAFQPKCTY 139
Cdd:cd11269  21 LYIAGRDQVYTVNLNEVpktEVTPSrkLTWRSRQQDRENCAMKGK-HKDECHNFIKVFVPRNDEMVFVCGTNAFNPMCRY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  140 INMLTFTLDRAEFEdGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKT-EYLAFWLNEPHFVGS 218
Cdd:cd11269 100 YRLSTLEYDGEEIS-GLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTiKYDSKWIKEPHFLHA 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  219 AfvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQ 296
Cdd:cd11269 179 I----EYGNY------VYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSqRVLEKHWTSFLKARLNCSVPgDSFFYFDV 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  297 LKAVH---TLRGASwhntTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY-TDPVPSPRPGSCIN 372
Cdd:cd11269 249 LQSITdiiEINGIP----TVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVpEDKVPKPRPGCCAK 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  373 NWHRDnGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNF--THVVADRVPGlDGATYTVLFIGTGDGWLLK 450
Cdd:cd11269 325 HGLAE-AYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYrlTAIAVDHAAG-PHQNYTVIFVGSEAGVVLK 402
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8134699  451 AV------SLGPWIhMVEELQVF----------DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11269 403 ILaktspfSLNDSV-LLEEIEAYnhakcsaeneEDRRVISLQLDRDHHALFVAFSSCVVRIPLS 465
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
45-497 1.66e-81

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: 268.44  E-value: 1.66e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   45 FSQTGIQDFLTLTLTEHSGLLYVGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSNQtECFNFIRFLQpYNSSH 124
Cdd:cd11263   1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VGGDR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  125 LYVCGTYAFQPKCT--YINMLTFTLDRAEfedGKGKCPYDPAKGHTGLLV-DGELYSATLNNFLGTEPVILRYMGTHHSI 201
Cdd:cd11263  79 LFTCGTNAFTPICTnrTLNNLTEIHDQIS---GMARCPYSPQHNSTALLTsSGELYAATAMDFPGRDPAIYRSLGILPPL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  202 KT-EYLAFWLNEPHFVGSAfvpeSVGSFTgdddkiYFFFSERAVEYDCySEQVVARVARVCKGDMGGARTLQKKWTTFLK 280
Cdd:cd11263 156 RTaQYNSKWLNEPNFVSSY----DIGNFT------YFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMK 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  281 ARLVCSAP-DWKVYFNQLKAVHTLRGASwhntTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYT 359
Cdd:cd11263 225 ARLNCSRPgEIPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYP 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  360 DPVPSPRPGSCinnwhrDNGytSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDgATYTVL 439
Cdd:cd11263 301 NPNPNFQCGTM------DQG--LYVNLTERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKD-MLFHII 371
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8134699  440 FIGTGDGWLLKAvsLGPWIH-----MVEELQVF---DQEPVESLVLSQSKKVLFAGSRSQLVQLSL 497
Cdd:cd11263 372 YLATDYGTIKKV--LAPLNQsssscLLEEIELFpkrQREPIRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
65-450 1.65e-80

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: 266.90  E-value: 1.65e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   65 LYVGAREALFAFSV-----EALELQGAISWEAPAEKKIECTQKGKsNQTECFNFIRFLQPYNSSHLYVCGTYAFQPKCTY 139
Cdd:cd11266  21 LYIAARDHIYTVDIdtshtEEIYFSKKLTWKSRQADVDTCRMKGK-HKDECHNFIKVLLKRNDDTLFVCGTNAFNPSCRN 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  140 INMLTFTLDRAEFEdGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKT-EYLAFWLNEPHFVGS 218
Cdd:cd11266 100 YKMDTLEFFGDEFS-GMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTvKHDSKWLKEPYFVQA 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  219 AfvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQ 296
Cdd:cd11266 179 V----DYGDY------IYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGSqRVLEKQWTSFLKARLNCSVPgDSHFYFNI 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  297 LKAVHTLRGASWHNTTfFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDP-VPSPRPGSCINNWH 375
Cdd:cd11266 249 LQAVTDVIHINGRDVV-LATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDErVPKPRPGCCAGSSS 327
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8134699  376 RDNgYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNF--THVVADRVPGlDGATYTVLFIGTGDGWLLK 450
Cdd:cd11266 328 LEK-YATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYrlTKIAVDNAAG-PYQNHTVVFLGSEKGIILK 402
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
50-450 1.31e-79

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: 264.39  E-value: 1.31e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   50 IQDFLTLTLTehsglLYVGAREALFAFSVEA-----LELQGAISWEAPAEKKIECTQKGKsNQTECFNFIRFLQPYNSSH 124
Cdd:cd11267  11 IQRVLRVNRT-----LYIGDRDNLYRVELDPtagteMRYHKKLTWRSNKNDINVCRMKGK-HEGECRNFIKVLLLRDYGT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  125 LYVCGTYAFQPKCTYINMLTFTLdRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIKT- 203
Cdd:cd11267  85 LFVCGTNAFNPVCANYSIDTLEP-VGDNISGMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRTv 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  204 EYLAFWLNEPHFVGSAfvpeSVGSftgdddKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKAR 282
Cdd:cd11267 164 KHDSKWFKEPYFVHAV----EWGS------HVYFFFREIAMEFNYLEKVVVSRVARVCKNDMGGSqRVLEKQWTSFLKAR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  283 LVCSAP-DWKVYFNQLKAVH---TLRGaswhNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY 358
Cdd:cd11267 234 LNCSVPgDSHFYFNVLQAVSdilNLGG----RPVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPV 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  359 TDP-VPSPRPGSCINNWHRdngYTSSLELPDNTLNFIKKHPLMEDQVkPRLG-RPLLVKKNTNF--THVVADRVPGLDGa 434
Cdd:cd11267 310 PEElVPRPRPGCCAAPGMR---YNSSSTLPDEVLNFVKTHPLMDEAV-PSLGhAPWIVRTMTRYqlTHMVVDTEAGPHG- 384
                       410
                ....*....|....*.
gi 8134699  435 TYTVLFIGTGDGWLLK 450
Cdd:cd11267 385 NHTVVFLGSTRGTVLK 400
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
65-484 6.31e-74

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: 249.26  E-value: 6.31e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   65 LYVGAREALFAFSV----EALELQGAISWEApaEKKIECTQKGKSnQTECFNFIRFLQPYNSSHLYVCGTYAFQPKCTYI 140
Cdd:cd11270  21 VYIAARDHVFAINLsaslERIVPQQKLTWKT--KDVEKCTVRGKN-SDECYNYIKVLVPRNDETLFACGTNAFNPTCRNY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  141 NMLTFTLDRAEFeDGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSI--KTEYLAFWLNEPHFVGS 218
Cdd:cd11270  98 KMSSLEQDGEEV-IGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLGESSPVlrTVKYDSKWLREPHFLHA 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  219 AfvpeSVGSFtgdddkIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLKARLVCSAP-DWKVYFNQ 296
Cdd:cd11270 177 I----EYGNY------VYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPgDSFFYFDV 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  297 LKAVHTLRGASwHNTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARY-TDPVPSPRPGSCInNWH 375
Cdd:cd11270 247 LQSLTNVMQIN-HRPAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVpDEAVPKPRPGSCA-GDG 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  376 RDNGYTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNF--THVVADRVPGLDGaTYTVLFIGTGDGWLLKAVS 453
Cdd:cd11270 325 PAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFklTQIAVDTAAGPYK-NYTVVFLGSENGHVLKVLA 403
                       410       420       430
                ....*....|....*....|....*....|....
gi 8134699  454 LGPWIHMVEELQVFD---QEPVESLVLSQSKKVL 484
Cdd:cd11270 404 SMHPNSSYSTQVLEDidvYNPNKCNVRGEDRRIL 437
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
67-495 3.46e-73

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: 246.23  E-value: 3.46e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   67 VGAREALFAFSVEALELQGAISWEAPAEKKIECTQKGKSNQtECFNFIRFLQPYNSShLYVCGTYAFQPKCTYINMLTFT 146
Cdd:cd11265  23 VGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEE-DCHNYVKVLLSYGKQ-LFACGTNAFSPRCSWREMENLT 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  147 lDRAEFEDGKGKCPYDPAKGHTGLL-VDGELYSATLNNFLGTEPVILRYMGT--HHSIKT-EYLAFWLNEPHFVGSAfvp 222
Cdd:cd11265 101 -SVTEWDSGVAKCPYSPHANITALLsSSGQLFVGSPTDFSGSDSAIYRTLGTsnKSFLRTkQYNSKWLNEPQFVGSF--- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  223 ESvgsftgdDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQK-KWTTFLKARLVCSAP-DWKVYFNQLKav 300
Cdd:cd11265 177 ET-------GNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLLKdNWTTFLKARLNCSLPgEYPFYFDEIQ-- 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  301 htlrGASWH--NTTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYtdpvpsprpgsciNNWHRDN 378
Cdd:cd11265 248 ----GMTYLpdEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERV-------------NVNHRDH 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  379 ----GYTSSLELPDNTlnfikKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGATYTVLFIGTGDGwLLKAVSL 454
Cdd:cd11265 311 fnqcSSSSSSHLLESS-----RYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKIHQSVHVLYVATTGG-LIKKISV 384
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 8134699  455 GPWIH---MVEELQVFDQ--EPVESLVLSQSKKVLFAGSRSQLVQL 495
Cdd:cd11265 385 LPRTQetcLVEIWQPLPTpdSPIKTMQYLKVTDSLYVGTELALMRI 430
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
62-498 6.65e-73

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: 244.75  E-value: 6.65e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   62 SGLLYVGAREALFAFSVEAlelqGAISWEAPAEKKIECTQKGKSNQTECFNFIRFLQPYNSShLYVCGTYAFQPKCTYIN 141
Cdd:cd11243  13 SSSVYVGGQGALYLLDFTG----SAVIVKKIPDEKTEKDCKKRATLDDCENYITLIKKLDYR-LLVCGTNAGSPKCWFLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  142 MLTFTldraEFEDGKGKCPYDPAKGHTGLLVDGELYSaTLNNFLGTEPVILRYmGTHHSIKTEylAFWLNEPHFVGSAFV 221
Cdd:cd11243  88 NQTLV----TLSADRGVAPFLPDENSLVLIEGNNVYS-TISGKKGNIPRFRRY-GGKKELYTS--DTVMQKPQFVKATLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  222 PESvgsfTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQ-KKWTTFLKARLVCSAPDWKVYFNQLKAV 300
Cdd:cd11243 160 PED----EQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLStSKWSTFLKARLVCGDPATPMNFNRLQDV 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  301 HTLRGASWHNTTFFGVFQARWGDmdlSAVCEYQLEQIQQVFegpykeyseQAQKWARYTDPVPSPRPGSCInnwhrdngy 380
Cdd:cd11243 236 FLLPKEEWREAVVYGVFSNTWGS---SAVCSYSLGDIDKVF---------RTSSLKGYSGSLPNPRPGTCV--------- 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  381 TSSLELPDNTLNFIKKHPLMEDQVKPRLGRPL-LVKKNTNFTHVVADRVPGLDGATYTVLFIGTGDGWLLKAVSLGPWIH 459
Cdd:cd11243 295 PPEQTHPSETFSFADEHPELDDRIEPDEPRKLpVFQNKDHYQKVVVDEVRASDGVSYDVLYLATDKGKIHKVVESKGQTH 374
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 8134699  460 MVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd11243 375 NIMEIQPFkEQEPIQSMILDAERSHLYVGTKAEVTRLPLD 414
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
297-479 1.65e-70

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: 229.85  E-value: 1.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699    297 LKAVHTLR--GASWHNTTFFGVFQARWGD-MDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWARYTDPVPSPRPGSCINN 373
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQWSNsIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699    374 WHRdngytssLELPDNTLNFIKKHPLMEDQVKPRLGRPLLVKKNTNFTHVVADRVPGLDGaTYTVLFIGTGDGWLLKAVS 453
Cdd:pfam01403  81 PLR-------LDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDG-NYTVLFLGTDDGRLHKVVL 152
                         170       180
                  ....*....|....*....|....*...
gi 8134699    454 LGP-WIHMVEELQVFDQ-EPVESLVLSQ 479
Cdd:pfam01403 153 VGSeESHIIEEIQVFPEpQPVLNLLLSS 180
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
51-467 4.95e-70

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: 238.83  E-value: 4.95e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   51 QDFLTLTLTehsglLYVGAREALFAFSVEALElQGA-------ISWEApaeKKIE-CTQKGKSNQtECFNFIRFLQPYNS 122
Cdd:cd11268  12 QRFLTLNRT-----LLVAARDHVFSFDLQAEE-EGEglvpnkyLTWRS---QDVEnCAVRGKLTD-ECYNYIRVLVPWDS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  123 SHLYVCGTYAFQPKCTYINMLTFTLDRAEFEdGKGKCPYDPAKGHTGLLVDGELYSATLNNFLGTEPVILRYMGTHHSIK 202
Cdd:cd11268  82 QTLLACGTNSFSPVCRSYGITSLQQEGEELS-GQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  203 T-EYLAFWLNEPHFVGSafvpesvgsfTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGA-RTLQKKWTTFLK 280
Cdd:cd11268 161 SaKYDSKWLREPHFVQA----------LEHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  281 ARLVCSAP-DWKVYFNQLKAVH---TLRGASwhntTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEGPYKEYSEQAQKWA 356
Cdd:cd11268 231 LRLNCSVPgDSTFYFDVLQALTgpvNLHGRS----ALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWT 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  357 RYT-DPVPSPRPGSCINnwhrDNG---YTSSLELPDNTLNFIKKHPLMEDQVKPRLGRPLL-VKKNTNFTHVVADRVPGl 431
Cdd:cd11268 307 PVSeDRVPSPRPGSCAG----VGGaalFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLtLTSRALLTQVAVDGMAG- 381
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 8134699  432 DGATYTVLFIGTGDGWLLKAV-----SLGPWIHMVEELQVF 467
Cdd:cd11268 382 PHSNITVMFLGSNDGTVLKVLppggrSGGPEPILLEEIDAY 422
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
52-498 6.46e-70

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: 235.95  E-value: 6.46e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   52 DFLTLTLTEHSGLLYVGAREALFAF-----SVEALELQGAISWEaPAEKKIECTQKGKSNQTECFNFIRFLQPYNSS-HL 125
Cdd:cd09295   1 DDDKILVSFRKDTIYVGAIARIYKVdgggtRLLLSCISPELNFG-FNEDQKAFCPLRRGKWTECINYIKVLQQKGDLdIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  126 YVCGTYAFQPKCTYINM-LTFTLDRAEFEDGKGKCPYDPAKGHTGLLVDGELYSATLNNFL-GTEPVILRYMGTHHSIKT 203
Cdd:cd09295  80 AVCGSNAAQPSCGSYRLdVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNVHYLRI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  204 EYL-AFWLNEPHFVgSAFVpesvgsFTGDDDKIYFFFSERAVEYDCYSEQVVARVARVCKGDMGGARTLQKKWTTFLKAR 282
Cdd:cd09295 160 VVDsSTGLDEITFV-YAFV------SGDDDDEVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKAD 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  283 LVCSAPDWKVYFNQLKAVHTLRGASWHNtTFFGVFQARWGDMDLSAVCEYQLEQIQQVFEgpykeyseqaqkwarytDPV 362
Cdd:cd09295 233 LNCSRPQSGFAFNLLQDATGDTKNLIQD-VKFAIFSSCLNKSVESAVCAYLFTDINNVFD-----------------DPV 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  363 PsprpgscinnwhrdngytsslelpdntlnfikkhplmedqvkPRLGRPLLVKKNT--NFTHVVADRVPGlDGATYTVLF 440
Cdd:cd09295 295 E------------------------------------------AINNRPLYAHQNQrsRLTSIAVDATKQ-KSVGYQVVF 331
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8134699  441 IGTGDGWLLKAVSLGPWI--HMVEELQVF-DQEPVESLVLSQSKKVLFAGSRSQLVQLSLA 498
Cdd:cd09295 332 LGLKLGSLGKALAFFFLYkgHIIEEWKVFkDSSRITNLDLSRPPLYLYVGSESGVLGVPVQ 392
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
231-519 1.43e-19

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: 91.88  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  231 DDDKIYFFFSERAVeydcyseqVVARVARVCKGDMGGARTLqkkwttflkarLVCSAPDWKVYFNQL-KAVHTLRGASWH 309
Cdd:cd09295   1 DDDKILVSFRKDTI--------YVGAIARIYKVDGGGTRLL-----------LSCISPELNFGFNEDqKAFCPLRRGKWT 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  310 NTTFFGVFQARWGDMDLSAVCEYQLEQ-IQQVFEGPYKEYSEQAQKwarytdpvPSPRPGSCINNWHRDNGYTSslelpD 388
Cdd:cd09295  62 ECINYIKVLQQKGDLDILAVCGSNAAQpSCGSYRLDVLVELGKVRW--------PSGRPRCPIDNKHSNMGVNV-----D 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  389 NTLNFIKKHPLMEDQvkprlgRPLLVKK--NTNFTHVVADRVPGLDGATYTVLFIGTGDgwllkavslgpwihmVEELQV 466
Cdd:cd09295 129 SKLYSATDHDFKDGD------RPALSRRssNVHYLRIVVDSSTGLDEITFVYAFVSGDD---------------DDEVYF 187
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 8134699  467 F-DQEPVESLvlsqSKKVLFAGSRSQLVQLSLADCTKYRFCVDCVLARDPYCAW 519
Cdd:cd09295 188 FfRQEPVEYL----KKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSR 237
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
564-648 2.27e-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: 83.26  E-value: 2.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  564 KNITVVSGTDLVLPCHLSSNLAHAHWTFGSQDLPAEQPGsflYDTGLQALVVMAAQSRHSGPYRCYSEEQGTRLAAESYL 643
Cdd:cd05872   4 KFRTVVAGADVVLPCQLRSNLASPVWLFNGTPLNAQFSY---LRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYS 80

                ....*
gi 8134699  644 VAVVA 648
Cdd:cd05872  81 LNVVE 85
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
563-646 1.01e-10

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: 58.62  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  563 PKNITVVSGTDLVLPCHLSSNLAHAHWTFGSQDLPAEQPGSfLYDTGLQALVVMAAQSRHSGPYRCYSEEQGTRLAAESY 642
Cdd:cd04979   3 FKQISVKEGDTVILSCSVKSNNAPVTWIHNGKKVPRYRSPR-LVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSV 81

                ....
gi 8134699  643 LVAV 646
Cdd:cd04979  82 TLHV 85
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
499-528 2.02e-08

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 51.01  E-value: 2.02e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 8134699     499 DCTKYRFCVDCVLARDPYCAWNVNTSRCVA 528
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRCTS 30
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
56-496 8.69e-08

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: 55.55  E-value: 8.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   56 LTLTEHSGLLYVGAREALFAFSVEALELQGAISweAPAEKKIECTQKGKSNQ------TECFNFIRFLQPYNSShLYVCG 129
Cdd:cd11276  11 LVVDPQTGRVYLGAVNALYQLDADLQLESRVET--GPKKDNKKCTPPIEENQcteakmTDNYNKLLLLDSANKT-LVVCG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  130 TYaFQPKCTYINmLTFTLDRAEFEDGKGKCPYdPAKGHTGLLVDGELYSatlnnflgTEPVILRYM------GTHHS--- 200
Cdd:cd11276  88 SL-FKGICSLRN-LSNISEVIYYSDTSGEKSF-VASNDEGVSTVGLISS--------LKPGNDRVFfvgkgnGSNDNgki 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  201 IKTEYLAFWLNEPHF--------VGSAFVPESVGSFT---GDDDKIYFFFSERaveyDCYSEQVVARVARVCKGDMGgar 269
Cdd:cd11276 157 ISTRLLQNYDDREVFenyidaatVKSAYVSRYTQQFRyafEDNNYVYFLFNQQ----LGHPDKNRTLIARLCENDHH--- 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  270 tlqkkWTTFLKARLVCSAPDWKvyFNQLKAVH-----------TLRGASWhNTTFFGVFQARWGDMDLSAVCEYQLEQIQ 338
Cdd:cd11276 230 -----YYSYTEMDLNCRDGANA--YNKCQAAYvstpgkelaqnYGNSILS-DKVLFAVFSRDEKDSGESALCMFPLKSIN 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  339 QVFEGPYKE-YSEQAQKWARYTDPVPSPRPGSCINnwHRDNGYTS----SLELPdntlnfikkHPLMEDQvKPRLGRPLL 413
Cdd:cd11276 302 AKMEANREAcYTGTIDDRDVFYKPFHSQKDIICGS--HQQKNSKSfpcgSEHLP---------YPLGSRD-ELALTAPVL 369
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  414 VKKNTNFTHVVADRVPGldgatYTVLFIGTGDGWLLKavslgpwIHMVEELQVFDQEPVE-------SLVLSQSKKVLFA 486
Cdd:cd11276 370 QRGGLNLTAVTVAVENG-----HTVAFLGTSDGRILK-------VHLSPDPEEYNSILIEknkpvnkDLVLDKTLEHLYI 437
                       490
                ....*....|
gi 8134699  487 GSRSQLVQLS 496
Cdd:cd11276 438 MTEDKVFRLP 447
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
62-456 1.72e-07

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


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 54.55  E-value: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699   62 SGLLYVGAREALFAFSVEaLELQGAISwEAPAEKKIECT------QKGKSNQTECFNFIRFLQPYNSShLYVCGTyAFQP 135
Cdd:cd11245  11 TGRLYLGAVNGLFQLSPN-LQLESRAD-TGPKKDSPQCLppitaaECPQAKETDNFNKLLLVNSANGT-LVVCGS-LFQG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  136 KCTYINM--LTFTLDRAEfedGKGKCPY----DPAKGHTGL----------LVDGELYSATLNNflGTEPVILR------ 193
Cdd:cd11245  87 VCELRNLnsVNKPLYRPE---TPGDKQYvaanEPSVSTVGLisyfkdglslLFVGRGYTSSLSG--GIPPITTRllqehg 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  194 ------YMGTHHSIKTEYLAFwlnEPHFVGsAFvpesvgsftGDDDKIYFFFSERAVEYDcysEQVVARVARVCKGDmgg 267
Cdd:cd11245 162 emdafsNEVEAKLVVGSASRY---HHDFVY-AF---------ADNGYIYFLFSRRPGTAD---STKRTYISRLCEND--- 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  268 artlqKKWTTFLKARLVCSAPDWKVYfNQLKAVHTLR-GASWHNTTFFGVFQARWGDMDL----SAVCEYQLEQIQQVFE 342
Cdd:cd11245 223 -----HHYYSYVELPLNCTVNQENTY-NLVQAAYLAKpGKVLNGKVLFGVFSADEASTAApdgrSALCMYPLSSVDARFE 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  343 ---------------GPYKEYSEQAQKWARYTDPVPSPRPGSCinnwhrdngytSSLELPDntlnfikkhPLMEDqvKPR 407
Cdd:cd11245 297 rtrescytgegleddKPETAYIEYNVKSICKTLPDKNVKAYPC-----------GAEHTPS---------PLASR--YPL 354
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 8134699  408 LGRPLLvKKNTNFTHVVADRVPGldgatYTVLFIGTGDGWLLKaVSLGP 456
Cdd:cd11245 355 AAKPIL-TRNDMLTAVAVAVENG-----HTIAFLGDSGGQLHK-VYLDP 396
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
499-527 5.93e-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: 46.93  E-value: 5.93e-07
                          10        20
                  ....*....|....*....|....*....
gi 8134699    499 DCTKYRFCVDCVLARDPYCAWNVNTSRCV 527
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCV 29
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
563-633 9.72e-07

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: 47.50  E-value: 9.72e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8134699  563 PKNITVVSGTDLVLPCHLSSNLAHAHWTFGSQDLPAEQPGSFLYDtglQALVVMAAQSRHSGPYRCYSEEQ 633
Cdd:cd05873   3 PRQRTFKLGGNAELKCSPKSNLARVVWKFQGKVLKAESPKYGLYG---DGLLIFNASEADAGRYQCLSVEK 70
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
436-526 3.06e-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: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  436 YTVLFIGTGDGWLLKAVSLGPWIHMV--EELQVF-DQEPV-ESLVLSQSKKVLFAGSRSQLVQLSLADCTKYRFCVDCVL 511
Cdd:cd11272 406 YSVVFVGTKSGKLKKIRADGPPHGGVqyEMVSVFkDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLS 485
                        90
                ....*....|....*
gi 8134699  512 ARDPYCAWNVNTSRC 526
Cdd:cd11272 486 SGDPHCGWCALHNMC 500
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
563-637 1.39e-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: 44.03  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699     563 PKNITVVSGTDLVLPCHLSSN-LAHAHWTFGSQDLPAEQPG-SFLYDTGLQALVVMAAQSRHSGPYRC------YSEEQG 634
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSpPPEVTWYKQGGKLLAESGRfSVSRSGSTSTLTISNVTPEDSGTYTCaatnssGSASSG 80

                   ...
gi 8134699     635 TRL 637
Cdd:smart00410  81 TTL 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
558-628 6.08e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 6.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8134699    558 KVRSIPKNITVVSGTDLVLPCHLSSN-LAHAHWTFGSQDLPAEQPGSFLYDTGLQALVVMAAQSRHSGPYRC 628
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEATGSpPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTC 74
Ig6_Contactin-4 cd05853
Sixth immunoglobulin (Ig) domain of contactin-4; The members here are composed of the sixth ...
563-644 1.82e-03

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: 38.45  E-value: 1.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8134699  563 PKNITVVSGTDLVLPCHLSsnlaHAH-------WTFGSQDLPAEQPGSFLYDTGLQA----LVVMAAQSRHSGPYRCYSE 631
Cdd:cd05853   9 PSSMDVTVGESIVLPCQVS----HDHsldivftWSFNGHLIDFQKDGDHFERVGGQDsagdLMIRSIQLKHAGKYVCMVQ 84
                        90
                ....*....|...
gi 8134699  632 EQGTRLAAESYLV 644
Cdd:cd05853  85 TSVDKLSAAADLI 97
I-set pfam07679
Immunoglobulin I-set domain;
558-628 5.95e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.85  E-value: 5.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8134699    558 KVRSIPKNITVVSGTDLVLPCHLSSN-LAHAHWTFGSQDLPAEQPGSFLYDTGLQALVVMAAQSRHSGPYRC 628
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTC 73
 
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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