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Conserved domains on  [gi|767934735|ref|XP_011512461|]
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semaphorin-5A isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sema super family cl15693
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
 34-438 0e+00

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


The actual alignment was detected with superfamily member cd11263:

Pssm-ID: 472829 [Multi-domain]  Cd Length: 436  Bit Score: 892.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   34 VGGRPYSGR---------KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNRSLSNLTEI 104
Cdd:cd11263    23 VGARNYLFRlqledlsliQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPICTNRTLNNLTEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  105 HDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYF 184
Cdd:cd11263   103 HDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  185 FFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTTNV 264
Cdd:cd11263   183 FFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYNELQSTFFLPELDLIYGIFTTNV 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  265 NSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLYVNLTERNLQDAQKFILMHEVVQPVTT 344
Cdd:cd11263   263 NSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLTERNLQDAQKFILMHEVVQPVTP 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  345 VPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTSSSCLLEEIELFPERRREPIRSLQILHSQSVL 424
Cdd:cd11263   343 VPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEIELFPKRQREPIRSLQILHSQSVL 422

                         410
                  ....*....|....
gi 767934735  425 FVGLREHVVKIPLK 438
Cdd:cd11263   423 FVGLQEHVIKIPLK 436
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 797-849 4.11e-17

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 76.09  E-value: 4.11e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    797 WSCWSPWTKCSATCGGGHYMRTRSCSNPAPAYGGDICLGLHTEEALCNTQPCP 849
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 551-604 1.27e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.27e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767934735    551 WTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERYCNEHlLCP 604
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 740-792 2.97e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 2.97e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    740 WSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEYQECNILPCP 792
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 609-655 1.70e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 59.91  E-value: 1.70e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    609 WTGWGPWERCTAQCGGGIQARRRICENGP------DCAGCNVEYQSCNTNPCP 655
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 439-486 3.47e-08

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: 50.78  E-value: 3.47e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767934735   439 RCQFYRTRSTCIGAQDPYCGWDVVMKKCTS----LEESLSMTQWEQSISACP 486
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 497-548 9.54e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 9.54e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767934735    497 GVWSPWTPCTHTDGSAVgscLCRTRSCDSPAPQCGGWQCEGPGMEIANCSRN 548
Cdd:smart00209    2 SEWSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
853-896 1.09e-06

Thrombospondin type 1 domain;


:

Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 1.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767934735   853 SEWSDWSECEAS---GVQVRARQCILLFPMGSQCSGNTTESRPCVFD 896
Cdd:pfam00090    1 SPWSPWSPCSVTcgkGIQVRQRTCKSPFPGGEPCTGDDIETQACKMD 47
 
Name Accession Description Interval E-value
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
 34-438 0e+00

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: 892.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   34 VGGRPYSGR---------KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNRSLSNLTEI 104
Cdd:cd11263    23 VGARNYLFRlqledlsliQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPICTNRTLNNLTEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  105 HDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYF 184
Cdd:cd11263   103 HDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  185 FFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTTNV 264
Cdd:cd11263   183 FFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYNELQSTFFLPELDLIYGIFTTNV 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  265 NSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLYVNLTERNLQDAQKFILMHEVVQPVTT 344
Cdd:cd11263   263 NSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLTERNLQDAQKFILMHEVVQPVTP 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  345 VPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTSSSCLLEEIELFPERRREPIRSLQILHSQSVL 424
Cdd:cd11263   343 VPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEIELFPKRQREPIRSLQILHSQSVL 422

                         410
                  ....*....|....
gi 767934735  425 FVGLREHVVKIPLK 438
Cdd:cd11263   423 FVGLQEHVIKIPLK 436
Sema smart00630
semaphorin domain;
43-413 7.13e-119

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 370.16  E-value: 7.13e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735     43 KAVEWECDEATKKACYSKGKSK-EECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLsnlteihdqisgmarcpyspqh 120
Cdd:smart00630   34 LKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTNAFQPVCRLRNL---------------------- 91

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735    121 nstalltagGELYAATAMDFPGRDPAIYRSLGILP-------PLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH 193
Cdd:smart00630   92 ---------GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVED 162

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735    194 D-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPEL----DLIYGIFTTNVNSIA 268
Cdd:smart00630  163 DnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPFYFNELQAAFLLPPGsesdDVLYGVFSTSSNPIP 242

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735    269 ASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPN-PNPHFQCGTVDQGLY--VNLTERNLQDAQKFILMHEVVQPVTTV 345
Cdd:smart00630  243 GSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCPNKPPssKDLPDETLNFIKSHPLMDEVVQPLTGR 322

                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934735    346 PSFME--DNSRFSHVAVDVVQGREAlVHIIYLATDYGTIKKVRVPLNQTSS-SCLLEEIELFPErrREPIR 413
Cdd:smart00630  323 PLFVKtdSNYLLTSIAVDRVATDGN-YTVLFLGTSDGRILKVVLSESSSSSeSVVLEEISVFPD--GSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
 244-419 1.69e-51

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: 179.00  E-value: 1.69e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   244 LQSTFFLPEL------DLIYGIFTTN-VNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGT-VDQ 315
Cdd:pfam01403    1 LQDVFVLKPGagdaldTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTcIND 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   316 GLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTssS 395
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEE--S 158

                          170       180
                   ....*....|....*....|....
gi 767934735   396 CLLEEIELFPErrREPIRSLQILH 419
Cdd:pfam01403  159 HIIEEIQVFPE--PQPVLNLLLSS 180
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 797-849 4.11e-17

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 76.09  E-value: 4.11e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    797 WSCWSPWTKCSATCGGGHYMRTRSCSNPAPAYGGDICLGLHTEEALCNTQPCP 849
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 551-604 1.27e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.27e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767934735    551 WTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERYCNEHlLCP 604
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 740-792 2.97e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 2.97e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    740 WSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEYQECNILPCP 792
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 609-655 1.70e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 59.91  E-value: 1.70e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    609 WTGWGPWERCTAQCGGGIQARRRICENGP------DCAGCNVEYQSCNTNPCP 655
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggPCTGEDVETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 552-600 2.06e-09

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 54.21  E-value: 2.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767934735   552 TPWTSWSPCSTTCGIGFQVRQRSCSNPtPRHGGRVCvGQNREERYCNEH 600
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLP 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
798-848 3.47e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 3.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767934735   798 SCWSPWTKCSATCGGGHYMRTRSCSNPAPayGGDICLGLHTEEALCNTQPC 848
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
741-791 7.98e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.42  E-value: 7.98e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767934735   741 SAWTSWSQCSRDCSRGIRNRKRVCNNPEPkyGGMPCLGPSLEYQECNILPC 791
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 439-486 3.47e-08

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: 50.78  E-value: 3.47e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767934735   439 RCQFYRTRSTCIGAQDPYCGWDVVMKKCTS----LEESLSMTQWEQSISACP 486
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 497-548 9.54e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 9.54e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767934735    497 GVWSPWTPCTHTDGSAVgscLCRTRSCDSPAPQCGGWQCEGPGMEIANCSRN 548
Cdd:smart00209    2 SEWSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
853-896 1.09e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 1.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767934735   853 SEWSDWSECEAS---GVQVRARQCILLFPMGSQCSGNTTESRPCVFD 896
Cdd:pfam00090    1 SPWSPWSPCSVTcgkGIQVRQRTCKSPFPGGEPCTGDDIETQACKMD 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 852-893 1.16e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.43  E-value: 1.16e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 767934735    852 WSEWSDWSECEAS---GVQVRARQCIL--LFPMGSQCSGNTTESRPC 893
Cdd:smart00209    1 WSEWSEWSPCSVTcggGVQTRTRSCCSppPQNGGGPCTGEDVETRAC 47
TSP_1 pfam00090
Thrombospondin type 1 domain;
612-654 4.63e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 4.63e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767934735   612 WGPWERCTAQCGGGIQARRRIC----ENGPDCAGCNVEYQSCNTNPC 654
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
439-477 1.49e-05

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 42.92  E-value: 1.49e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 767934735    439 RCQFYRTRSTCIGAQDPYCGWDVVMKKCTSLEESLSMTQ 477
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRRQ 39
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 852-894 8.29e-04

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 43.01  E-value: 8.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767934735  852 WSEWSDWSEC-----EASGVQVRARQCIllFPMGSQCSGNTTESRPCV 894
Cdd:PTZ00087  233 YTEWGEWSNCsmecdHPDNVQIRERKCA--HPSGDCFKGDLKETRPCQ 278
TSP_1 pfam00090
Thrombospondin type 1 domain;
497-546 3.61e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.24  E-value: 3.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767934735   497 GVWSPWTPCTHTDGSAVGSclcRTRSCDSPAPqcGGWQCEGPGMEIANCS 546
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQV---RQRTCKSPFP--GGEPCTGDDIETQACK 45
 
Name Accession Description Interval E-value
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
 34-438 0e+00

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: 892.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   34 VGGRPYSGR---------KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNRSLSNLTEI 104
Cdd:cd11263    23 VGARNYLFRlqledlsliQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPICTNRTLNNLTEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  105 HDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYF 184
Cdd:cd11263   103 HDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  185 FFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTTNV 264
Cdd:cd11263   183 FFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYNELQSTFFLPELDLIYGIFTTNV 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  265 NSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLYVNLTERNLQDAQKFILMHEVVQPVTT 344
Cdd:cd11263   263 NSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLTERNLQDAQKFILMHEVVQPVTP 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  345 VPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTSSSCLLEEIELFPERRREPIRSLQILHSQSVL 424
Cdd:cd11263   343 VPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEIELFPKRQREPIRSLQILHSQSVL 422

                         410
                  ....*....|....
gi 767934735  425 FVGLREHVVKIPLK 438
Cdd:cd11263   423 FVGLQEHVIKIPLK 436
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
 33-438 0e+00

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: 720.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   33 AVGGRPYSGR---------KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNRSLSNLTE 103
Cdd:cd11241    22 IVGARNYLFRlrlqslsllQAVPWNSDEDTKRQCQSKGKSVEECQNYVRVLLVVGKNLFTCGTYAFSPVCTIRKLSNLTQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  104 IHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTY 183
Cdd:cd11241   102 ILDTISGVARCPYSPAHNSTALISASGELYAGTVYDFSGRDPAIYRSLGGKPPLRTAQYNSKWLNEPNFVGSYEIGNHTY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  184 FFFRENAVEH-DCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTT 262
Cdd:cd11241   182 FFFRENAVEHqDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGEFPFYYNEIQGTFYLPETDLIYAVFTT 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  263 NVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGT-VDQGLYVNLTERNLQDAQKFILMHEVVQP 341
Cdd:cd11241   262 NVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPTPNPHPNFQCTTsIDRGQPANTTERDLQDAQKYQLMAEVVQP 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  342 VTTVPSFMEDNSRFSHVAVDVVQGRE-ALVHIIYLATDYGTIKKVRVPLnQTSSSCLLEEIELFPERRREPIRSLQILHS 420
Cdd:cd11241   342 VTKIPLVTMDDVRFSKLAVDVVQGRGtQLVHIFYVGTDYGTILKMYQPH-RSQKSCTLEEIKILPAMKGEPITSLQFLKS 420

                         410
                  ....*....|....*...
gi 767934735  421 QSVLFVGLREHVVKIPLK 438
Cdd:cd11241   421 EKSLFVGLETGVLRIPLN 438
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
 34-438 0e+00

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: 684.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   34 VGGRPYSGR---------KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNRSLSNLTEI 104
Cdd:cd11264    23 VGARNYLFRlslhnvsliQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVFTCGTNAFSPVCTSRQVGNLSKV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  105 HDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYF 184
Cdd:cd11264   103 IERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQYNSKWLNEPNFIAAYDIGLFTYF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  185 FFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTTNV 264
Cdd:cd11264   183 FFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYNELQSTFYLPEQDLIYGVFTTNV 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  265 NSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTV-DQGLYVNLTERNLQDAQKFILMHEVVQPVT 343
Cdd:cd11264   263 NSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLsDDSPNENLTERSLQDAQRLFLMNDVVQPVT 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  344 TVPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTSSSCLLEEIELFPERRREPIRSLQILHSQSV 423
Cdd:cd11264   343 VDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEMQILPPGQREPIRSLQILHSDRS 422

                         410
                  ....*....|....*
gi 767934735  424 LFVGLREHVVKIPLK 438
Cdd:cd11264   423 LFVGLNNGVLKIPLE 437
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
 45-437 7.39e-151

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: 455.33  E-value: 7.39e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   45 VEWECDEATKKACYSKGKSKEECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNST 123
Cdd:cd11235    37 VAWPSSPDDVDTCYLKGKSKDDCRNFIKVLEkNSDDSLLVCGTNAFNPSCRNYNVETFELVGKEESGRGKCPYDPDHNST 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  124 ALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVFSR 202
Cdd:cd11235   117 ALF-ADGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWLNEPQFVGAFDIGDYVYFFFREIAVEYiNCGKAVYSR 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  203 AARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCVFNLS 278
Cdd:cd11235   196 VARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFPFYFNELQDVFDLPSPSnkekIFYAVFTTPYNSIPGSAVCAYSLS 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  279 AIAQAFSGPFKYQENSRSAWLPYPN---PNPH-FQCGTVDQglyvNLTERNLQDAQKFILMHEVVQPVTTVPSFM--EDN 352
Cdd:cd11235   276 DIEAVFNGPFKEQHSSNSAWLPVPDervPEPRpGTCVDDSS----PLPDDTLNFIKSHPLMDEAVTPILNRPLFIktDVN 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  353 SRFSHVAVDVVQGREA-LVHIIYLATDYGTIKKVRVPLNQTSS-SCLLEEIELFPErrREPIRSLQILHSQSVLFVGLRE 430
Cdd:cd11235   352 YRFTKIAVDRVQAKLGqTYDVLFVGTDRGIILKVVSLPEQGLQaSNILEEMPVGPP--PEPIQTMQLSRKRRSLYVGSET 429


                  ....*..
gi 767934735  431 HVVKIPL 437
Cdd:cd11235   430 GVLQVPL 436
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
 33-436 4.61e-149

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: 450.39  E-value: 4.61e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   33 AVGGRPYSGR---------KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNRSLSNLTE 103
Cdd:cd11265    22 IVGARDNLYRlsldglellERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLFACGTNAFSPRCSWREMENLTS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  104 IHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGI--LPPLRTAQYNSKWLNEPNFVSSYDIGNF 181
Cdd:cd11265   102 VTEWDSGVAKCPYSPHANITALLSSSGQLFVGSPTDFSGSDSAIYRTLGTsnKSFLRTKQYNSKWLNEPQFVGSFETGNF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  182 TYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGI 259
Cdd:cd11265   182 VYFLFRESAVEYmNCGKVIYSRIARVCKNDVGGGtMLLKDNWTTFLKARLNCSLPGEYPFYFDEIQGMTYLPDEGILYAT 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  260 FTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPN--PHFQCGTVDQGlyvnlterNLQDAQKFILMHE 337
Cdd:cd11265   262 FTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVNVNHrdHFNQCSSSSSS--------HLLESSRYQLMDE 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  338 VVQPVTTVPSFMEDNSRFSHVAVDVVQGR-EALVHIIYLATDYGTIKKVRVpLNQTSSSCLLEEIELFPERRRePIRSLQ 416
Cdd:cd11265   334 AVQPITLEPLHHAKLERFSHIAVDVIPTKiHQSVHVLYVATTGGLIKKISV-LPRTQETCLVEIWQPLPTPDS-PIKTMQ 411

                         410       420
                  ....*....|....*....|
gi 767934735  417 ILHSQSVLFVGLREHVVKIP 436
Cdd:cd11265   412 YLKVTDSLYVGTELALMRIP 431
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
 42-440 1.09e-121

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: 379.37  E-value: 1.09e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   42 RKAVEWECDEATKKACYSKGKSKEECQNYIRVL-LVGGDRLFTCGTNAFTPVCT--NRSLSNLTEIHDQiSGMARCPYSP 118
Cdd:cd11237    36 NQRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLaKKSAGRLLVCGTNAYKPLCReyTVKDGGYRVEREF-DGQGLCPYDP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  119 QHNSTALLtAGGELYAATAMDFPGRDPAIYRSlgilpPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGK 197
Cdd:cd11237   115 KHNSTAVY-ADGQLYSATVADFSGADPLIYRE-----PLRTERYDLKQLNAPNFVSSFAYGDYVYFFFRETAVEYiNCGK 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  198 TVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPE-------LDLIYGIFTTNVNSIAAS 270
Cdd:cd11237   189 AIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGEYPFYFNEIQSTSDIVEggyggksAKLIYGVFTTPVNSISGS 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  271 AVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPN-----PNPHfQCgtvdqglyVNlTERNLQD-AQKFI----LMHEVVQ 340
Cdd:cd11237   269 AVCAFSLQDILEVFDGSFKEQQDINSNWLPVPSnkvpePRPG-QC--------VN-DSRTLPDvTVNFIkshpLMDEAVP 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  341 PVTTVPSFME--DNSRFSHVAVD--VVQGREALVHIIYLATDYG-TIKKVRVPLNQTSS---SCLLEEIELFPerRREPI 412
Cdd:cd11237   339 SFFGRPILVRtsLQYRFTQIAVDpqVKALDGKYYDVLFIGTDDGkVLKAVNIASADTVDkvsPVVIEETQVFP--RGVPI 416

                         410       420       430
                  ....*....|....*....|....*....|
gi 767934735  413 RSLQILHS--QSVLFVGLREHVVKIPLKRC 440
Cdd:cd11237   417 RNLLIVRGkdDGRLVVVSDDEIVSIPLHRC 446
Sema smart00630
semaphorin domain;
43-413 7.13e-119

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 370.16  E-value: 7.13e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735     43 KAVEWECDEATKKACYSKGKSK-EECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLsnlteihdqisgmarcpyspqh 120
Cdd:smart00630   34 LKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTNAFQPVCRLRNL---------------------- 91

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735    121 nstalltagGELYAATAMDFPGRDPAIYRSLGILP-------PLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH 193
Cdd:smart00630   92 ---------GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVED 162

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735    194 D-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPEL----DLIYGIFTTNVNSIA 268
Cdd:smart00630  163 DnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPFYFNELQAAFLLPPGsesdDVLYGVFSTSSNPIP 242

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735    269 ASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPN-PNPHFQCGTVDQGLY--VNLTERNLQDAQKFILMHEVVQPVTTV 345
Cdd:smart00630  243 GSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCPNKPPssKDLPDETLNFIKSHPLMDEVVQPLTGR 322

                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767934735    346 PSFME--DNSRFSHVAVDVVQGREAlVHIIYLATDYGTIKKVRVPLNQTSS-SCLLEEIELFPErrREPIR 413
Cdd:smart00630  323 PLFVKtdSNYLLTSIAVDRVATDGN-YTVLFLGTSDGRILKVVLSESSSSSeSVVLEEISVFPD--GSPIS 390
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
 43-437 2.05e-113

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: 358.37  E-value: 2.05e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDR-LFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHN 121
Cdd:cd11242    46 KKLTWRSRQADVENCRMKGKHKDECHNFIKVLVPRNDEtLFVCGTNAFNPVCRNYRIDTLEQDGEEISGMARCPFDAKQA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  122 STALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHD-CGKTVF 200
Cdd:cd11242   126 NVALF-ADGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYDSKWLKEPHFVHAVEYGDYVYFFFREIAVEYNtLGKVVF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  201 SRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPEL---DLIYGIFTTNVNSIAASAVCVFN 276
Cdd:cd11242   205 SRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPGDSHFYFDVLQAVTDVIRIngrPVVLGVFTTQYNSIPGSAVCAFD 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  277 LSAIAQAFSGPFKYQENSRSAWLPYPN---PNPHFQCGTVDQGLYVNLTERNLQD-AQKFI----LMHEVVQPVTTVPSF 348
Cdd:cd11242   285 MDDIEKVFEGRFKEQKSPDSAWTPVPEdrvPKPRPGCCAGSGSAEKYKTSNDFPDdTLNFIkthpLMDEAVPSIINRPWF 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  349 MEDNSRF--SHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTSS--SCLLEEIELF-PER--------RRepIRSL 415
Cdd:cd11242   365 TRTMVRYrlTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARIGPSGSngSVFLEEIDVYnPAKcsydgeedRR--IIGL 442

                         410       420
                  ....*....|....*....|..
gi 767934735  416 QILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11242   443 ELDRASHALFVAFSGCVIRVPL 464
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
 41-437 7.89e-105

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: 335.15  E-value: 7.89e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   41 GRKAVEWECDEATKKACYSKGKSKE-ECQNYIRVLLVGGD-RLFTCGTNAFTPVCTNRSLSNLTEIH-DQISGMARCPYS 117
Cdd:cd11240    41 LKDKIKWEASEDKKKECANKGKDNQtDCFNFIRILQFYNStHLYVCGTFAFSPRCTYINLSDFSLSSiKFEDGKGRCPFD 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  118 PQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTaQYNSKWLNEPNFVSSY----DIGNFT------YFFFR 187
Cdd:cd11240   121 PAQRYTAIM-VDGELYSATVNNFLGSEPVISRNHSEGNVLKT-ENTLRWLNEPAFVGSAhireSIDSPDgdddkiYFFFT 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  188 ENAVEHDCG-KTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEvPFYYNELQSTFFLPELD----LIYGIFTT 262
Cdd:cd11240   199 ETAVEYDFYeKVTVSRVARVCKGDLGGQRTLQKKWTTFLKAQLVCSQPDS-GLPFNVLRDVFVLSPDSwdatIFYGVFTS 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  263 NVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQ---CGT-----VDQGLYVNLTERNLQDAQKFIL 334
Cdd:cd11240   278 QWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRYTGPVPDPRpgaCITnsarsQGITSSLNLPDNVLTFVKDHPL 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  335 MHEVVQPVTTvPSFMEDNSRFSHVAVDVVQGREALVH-IIYLATDYGTIKKVrVPLNqtSSSCLLEEIELFPErrREPIR 413
Cdd:cd11240   358 MDEQVHPINR-PLLVKSGVNYTRIAVHRVQALDGQTYtVLFLGTEDGFLHKA-VSLD--GGMHIIEEIQLFDQ--PQPVK 431

                         410       420
                  ....*....|....*....|....
gi 767934735  414 SLQILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11240   432 NLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
 43-437 4.34e-96

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: 312.54  E-value: 4.34e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDR-LFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHN 121
Cdd:cd11267    46 KKLTWRSNKNDINVCRMKGKHEGECRNFIKVLLLRDYGtLFVCGTNAFNPVCANYSIDTLEPVGDNISGMARCPYDPKHA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  122 STALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVE-HDCGKTVF 200
Cdd:cd11267   126 NVALF-ADGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEPYFVHAVEWGSHVYFFFREIAMEfNYLEKVVV 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  201 SRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPEL---DLIYGIFTTNVNSIAASAVCVFN 276
Cdd:cd11267   205 SRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVSDILNLggrPVVLAVFSTPTNSIPGSAVCAFD 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  277 LSAIAQAFSGPFKYQENSRSAWLPYPN---PNPHFQCGTVdQGLYVNLTERNLQDAQKFI----LMHEVVQPVTTVPSFM 349
Cdd:cd11267   285 MTQVAAVFEGRFREQKSPESIWTPVPEelvPRPRPGCCAA-PGMRYNSSSTLPDEVLNFVkthpLMDEAVPSLGHAPWIV 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  350 EDNSRF--SHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTSS-----SCLLEEIELF-PERRREPIRSLQILHSQ 421
Cdd:cd11267   364 RTMTRYqlTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLIIPNASSSeisnqSVFLEELETYnPERCGWDSPQAQKLLSL 443

                         410       420
                  ....*....|....*....|..
gi 767934735  422 SV------LFVGLREHVVKIPL 437
Cdd:cd11267   444 ELdkgsggLLLAFPSCVVRVPV 465
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
 43-440 4.74e-96

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: 312.37  E-value: 4.74e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKE-ECQNYIRVL-LVGGDRLFTCGTNAFTPVCT----NRSLSNLT---EIHDQISGMAR 113
Cdd:cd11239    43 KKIYWPASPERIEECKMAGKDPNtECANFVRVLqPYNRTHLYACGTGAFHPICAfinvGRRLEDPIfklDDSSLESGRGK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  114 CPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDI-------GNFTYFFF 186
Cdd:cd11239   123 CPFDPNQPFASVLI-DGELYSGTAIDFMGRDAAIFRSLGHRHYIRTEQYDSRWLNEPKFVGAYLIpdsdnpdDDKVYFFF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  187 RENAVEHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQSTFFLPELD----LIYGI 259
Cdd:cd11239   202 REKAVEAEgSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLKARLVCSVPGPdgIDTYFDELEDVFLLPTRDpknpLIYGV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  260 FTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPY----PNPNPhfqcGTVDQGLYVNL---TERNLQDAQKF 332
Cdd:cd11239   282 FTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVEYqgkvPYPRP----GTCPSKTYGPLyksTKDFPDDVISF 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  333 I----LMHEVVQPVTTVPSFMEDNS--RFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTSSS--CLLEEIELF 404
Cdd:cd11239   358 ArshpLMYNPVYPLHGRPLLIRTNVpyRLTQIAVDRVEAEDGQYDVLFIGTDSGTVLKVVSLPKENWEMeeVILEELQVF 437

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 767934735  405 peRRREPIRSLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11239   438 --KHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
 57-423 1.03e-95

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: 310.90  E-value: 1.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   57 CYSKGKSKE-ECQNYIRVLLV--GGDRLFTCGTNAFTPvcTNRSL--SNLTEIHDQIS---GMARCPYSPQHNSTALLTA 128
Cdd:cd11238    53 CVSKGKDEEyECRNHVRVIQPmgDGQTLYVCSTNAMNP--KDRVLdaNLLHLPEYVPGpgnGIGKCPYDPDDNSTAVWVE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  129 GGE------LYAATAMDFPGRDPAIYRslgilPPL------------RTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENA 190
Cdd:cd11238   131 WGNpgdlpaLYSGTRTEFTKANTVIYR-----PPLynntkgrhesfmRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETA 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  191 VEH-DCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELD--LIYGIFTTNVNSI 267
Cdd:cd11238   206 VEYiNCGKVVYSRVARVCKKDTGGKNVLRQNWTTFLKARLNCSISGEFPFYFNEIQSVYKVPGRDdtLFYATFTTSENGF 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  268 AASAVCVFNLSAIAQAF-SGPFKYQENSRSAWLPYPNPN--PHF--QCgTVDQGlyvNLTERNLQDAQKFILMHEVVQpv 342
Cdd:cd11238   286 TGSAVCVFTLSDINAAFdTGKFKEQASSSSAWLPVLSSEvpEPRpgTC-VNDSA---TLSDTVLHFARTHPLMDDAVS-- 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  343 TTVPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKK-VRVPLNQTSSSCLLEEIELFPErrrEPIRSLQILHSQ 421
Cdd:cd11238   360 HGPPLLYLRDVVFTHLVVDKLRIDDQEYVVFYAGSNDGKVYKiVHWKDAGESKSNLLDVFELTPG---EPIRAMELLPGE 436


                  ..
gi 767934735  422 SV 423
Cdd:cd11238   437 FL 438
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
 43-437 2.22e-95

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: 310.42  E-value: 2.22e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRL-FTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHN 121
Cdd:cd11269    46 RKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEMvFVCGTNAFNPMCRYYRLSTLEYDGEEISGLARCPFDARQT 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  122 STALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVF 200
Cdd:cd11269   126 NVALF-ADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHnNLGKAVY 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  201 SRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELD---LIYGIFTTNVNSIAASAVCVFN 276
Cdd:cd11269   205 SRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFFYFDVLQSITDIIEINgipTVVGVFTTQLNSIPGSAVCAFS 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  277 LSAIAQAFSGPFKYQENSRSAWLPYPN---PNPHFQCgTVDQGL------YVNLTERNLQDAQKFILMHEVVQPVTTVPS 347
Cdd:cd11269   285 MDDIEKVFKGRFKEQKTPDSVWTAVPEdkvPKPRPGC-CAKHGLaeayktSIDFPDETLSFIKSHPLMDSAVPSIIEEPW 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  348 FMEDNSRF--SHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTS--SSCLLEEIELF---------PERRRepIRS 414
Cdd:cd11269   364 FTKTRVRYrlTAIAVDHAAGPHQNYTVIFVGSEAGVVLKILAKTSPFSlnDSVLLEEIEAYnhakcsaenEEDRR--VIS 441

                         410       420
                  ....*....|....*....|...
gi 767934735  415 LQILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11269   442 LQLDRDHHALFVAFSSCVVRIPL 464
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
 43-437 1.71e-94

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: 308.11  E-value: 1.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKEECQNYIRVLLV-GGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHN 121
Cdd:cd11266    46 KKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKrNDDTLFVCGTNAFNPSCRNYKMDTLEFFGDEFSGMARCPYDAKHA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  122 STALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVE-HDCGKTVF 200
Cdd:cd11266   126 NVALF-ADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAVDYGDYIYFFFREIAVEyNSMGKVVF 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  201 SRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPEL---DLIYGIFTTNVNSIAASAVCVFN 276
Cdd:cd11266   205 PRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQAVTDVIHIngrDVVLATFSTPYNSIPGSAVCAYD 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  277 LSAIAQAFSGPFKYQENSRSAWLPYPN---PNPHFQCGTVDQGLYVNLTERNL-QDAQKFI----LMHEVVQPVTTVPSF 348
Cdd:cd11266   285 MLDIASVFTGRFKEQKSPDSTWTPVPDervPKPRPGCCAGSSSLEKYATSNEFpDDTLNFIkthpLMDEAVPSIINRPWF 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  349 MEDNSRF--SHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQT---SSSCLLEEIELF-PER------RREPIRSLQ 416
Cdd:cd11266   365 LRTMVRYrlTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARTGNSgflNDSLFLEEMNVYnSEKcsydgvEDKRIMGMQ 444

                         410       420
                  ....*....|....*....|.
gi 767934735  417 ILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11266   445 LDKASSALYVAFSTCVIKVPL 465
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
 45-440 1.53e-81

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: 273.24  E-value: 1.53e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   45 VEWECDEATKKACYSKGK-SKEECQNYIRVLL-VGGDRLFTCGTNAFTPVCT--NRSLSNLTEIHDQI-----SGMARCP 115
Cdd:cd11254    45 IHWPASPQRIEECILSGKgSNGECGNFIRLIQpWNRTHLYVCGTGAYNPVCAyiNRGRRAEDYMFRLEpdkleSGKGKCP 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  116 YSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRE 188
Cdd:cd11254   125 YDPKQDSVSALI-NGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSeknddklYFFFRE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  189 NAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQSTFFLPELD----LIYGIFTT 262
Cdd:cd11254   204 KSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGAdgIETHFDELRDVFIQPTQDtknpVIYAVFST 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  263 NVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLYV--NLTERNLQD-AQKFI----LM 335
Cdd:cd11254   284 SGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTpsMKSTKDYPDeVINFMrthpLM 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  336 HEVVQPVTTVPSFMEDNS--RFSHVAVDVVQGREALVHIIYLATDYGTIKKVRV-PLNQ-TSSSCLLEEIELFpeRRREP 411
Cdd:cd11254   364 YNAVYPVHRRPLVVRTNVnyRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVlPKDDlETEELTLEEVEVF--KVPAP 441

                         410       420
                  ....*....|....*....|....*....
gi 767934735  412 IRSLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11254   442 IKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
 43-437 3.06e-81

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: 271.98  E-value: 3.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEAtkKACYSKGKSKEECQNYIRVLLVGGDR-LFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHN 121
Cdd:cd11270    45 QKLTWKTKDV--EKCTVRGKNSDECYNYIKVLVPRNDEtLFACGTNAFNPTCRNYKMSSLEQDGEEVIGQARCPFESRQS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  122 STALLtAGGELYAATAMDFPGRDPAIYRSLGILPP-LRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDC-GKTV 199
Cdd:cd11270   123 NVGLF-AGGDFYSATMTDFLASDAVIYRSLGESSPvLRTVKYDSKWLREPHFLHAIEYGNYVYFFLSEIAVEYTTlGKVV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  200 FSRAARVCKNDIGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELD---LIYGIFTTNVNSIAASAVCVF 275
Cdd:cd11270   202 FSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPGDSFFYFDVLQSLTNVMQINhrpAVLGVFTTQANSITGSAVCAF 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  276 NLSAIAQAFSGPFKYQENSRSAWLPYPN---PNPHFQC--GTVDQGLYVNLTE---RNLQDAQKFILMHEVVQPVTTVPS 347
Cdd:cd11270   282 YMDDIEKVFNGKFKEQRNSESAWTPVPDeavPKPRPGScaGDGPAAGYKSSTNfpdETLTFIKSYPLMDEAVPSVNNRPC 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  348 FMEDNSRF--SHVAVDVVQGREALVHIIYLATDYGTIKKVR--VPLNQTSSSCLLEEIELF--------PERRRepIRSL 415
Cdd:cd11270   362 FTRTTSRFklTQIAVDTAAGPYKNYTVVFLGSENGHVLKVLasMHPNSSYSTQVLEDIDVYnpnkcnvrGEDRR--ILGL 439

                         410       420
                  ....*....|....*....|..
gi 767934735  416 QILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11270   440 ELDKDHHALFVAFTGCVIRVPL 461
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
 22-440 5.98e-79

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: 266.01  E-value: 5.98e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   22 ESRGRRVehhraVGGRPY----------SGRKAVEWECDEATKKACYSKGKS-KEECQNYIRVL-LVGGDRLFTCGTNAF 89
Cdd:cd11250    17 EERGRLF-----VGAKNYlaslsldnisKQEKKIYWPAPVEWREECNWAGKDiNTDCMNYVKILhHYNRTHLYACGTGAF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   90 TPVCTNRSLSNLTEIH----DQIS---GMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 162
Cdd:cd11250    92 HPTCAFVEVGQRMEDHvfrlDPSRvedGKGKSPYDPRHTAASVL-VGDELYSGVATDLMGRDFTIFRSLGQRPSLRTEQH 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  163 NSKWLNEPNFVSSYDI-------GNFTYFFFRENAVE-HDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRP 234
Cdd:cd11250   171 DSRWLNEPKFVKVFWIpesenpdDDKIYFFFRETAVEaAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCSVP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  235 GE--VPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPY----PNP 304
Cdd:cd11250   251 GNegGDTHFDELRDVFLLQTRDkrnpLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYqgkvPYP 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  305 NPHFqCGTVDQGLYV---NLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNS--RFSHVAVDVVQGREALVHIIYLATDY 379
Cdd:cd11250   331 RPGM-CPSKTFGSFEstkDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIpyTFTQIAVDRVAAADGHYDVMFIGTDV 409

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767934735  380 GTIKKV-RVPLN--QTSSSCLLEEIELFpeRRREPIRSLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11250   410 GSVLKViSVPKGswPSNEELLLEELHVF--KDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
 43-440 5.99e-77

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: 261.47  E-value: 5.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKS-KEECQNYIRVL-LVGGDRLFTCGTNAFTPVCT-----NRSLSNLTEIHDQI--SGMAR 113
Cdd:cd11249    64 QKIVWPVSPSRRDECKWAGKDiLKECANFIKVLkAYNQTHLYACGTGAFHPVCTyievgHHPEDNIFRLEDSHfeNGRGK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  114 CPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDI-------GNFTYFFF 186
Cdd:cd11249   144 SPYDPKLLTASLLI-DGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIpesdnpeDDKIYFFF 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  187 RENAV--EHdCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQSTFFL----PELDLIYG 258
Cdd:cd11249   223 RENAIdgEH-TGKATHARIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPngIDTHFDELQDVFLMnskdPKNPIVYA 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  259 IFTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLYVNL-TERNLQD-----AQKF 332
Cdd:cd11249   302 VFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGGFdSTKDLPDdvitfARSH 381

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  333 ILMHEVVQPVTTVPSFM--EDNSRFSHVAVDVVQGREALVHIIYLATDYGTI-KKVRVPLNQTS--SSCLLEEIELFper 407
Cdd:cd11249   382 PAMYNPVFPINNRPIIIktDVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVlKVVSIPKETWHdlEEVLLEEMTVF--- 458

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 767934735  408 rREP--IRSLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11249   459 -REPtaISAMELSTKQQQLYIGSAIGVSQLPLHRC 492
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
 43-437 1.37e-76

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: 259.63  E-value: 1.37e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEAtkKACYSKGKSKEECQNYIRVLLV-GGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHN 121
Cdd:cd11268    47 KYLTWRSQDV--ENCAVRGKLTDECYNYIRVLVPwDSQTLLACGTNSFSPVCRSYGITSLQQEGEELSGQARCPFDATQS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  122 STALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVF 200
Cdd:cd11268   125 NVAIF-AEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLREPHFVQALEHGDHVYFFFREVSVEDaRLGRVQF 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  201 SRAARVCKNDIGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQS---TFFLPELDLIYGIFTTNVNSIAASAVCVFN 276
Cdd:cd11268   204 SRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPGDSTFYFDVLQAltgPVNLHGRSALFGVFTTQTNSIPGSAVCAFY 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  277 LSAIAQAFSGPFKYQENSRSAWLP-----YPNPNPHFQCGTVDQGLYVnlTERNL-QDAQKFILMHEV----VQPVTTVP 346
Cdd:cd11268   284 LDEIERGFEGKFKEQRSLDGAWTPvsedrVPSPRPGSCAGVGGAALFS--SSRDLpDDVLTFIKAHPLldpaVPPVTHQP 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  347 SF-MEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTS--SSCLLEEIELFPERRREPIRS--------- 414
Cdd:cd11268   362 LLtLTSRALLTQVAVDGMAGPHSNITVMFLGSNDGTVLKVLPPGGRSGgpEPILLEEIDAYSPARCSGKRTaqtarriig 441

                         410       420
                  ....*....|....*....|...
gi 767934735  415 LQILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11268   442 LELDTEGHRLFVAFSGCIVYLPL 464
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
 34-440 7.83e-74

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


Pssm-ID: 200514 [Multi-domain]  Cd Length: 471  Bit Score: 252.08  E-value: 7.83e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   34 VGGRP--YS--------GRKAVEWECDEATKKACYSKGKSKEECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNLT 102
Cdd:cd11253    24 VGGRDllYSlslerisaNYKEIHWPSTQLQVEDCIMKGRDKPECANYIRVLHhYNRTHLLACGTGAFDPVCAFIRVGRGS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  103 EIH------DQI-SGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSS 175
Cdd:cd11253   104 EDHlfqlesDKFeRGRGRCPFDPNSSFISTLI-GGELFVGLYSDYWGRDAAIFRTMNHLAHIRTEHDDERLLKEPKFVGS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  176 YDI-------GNFTYFFFRENAVEHDCG-KTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQ 245
Cdd:cd11253   183 YMIpdnedpdDNKVYFFFTEKALEAEGGnHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLICSVPGPngIDTHFDELE 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  246 STFFLPELD----LIYGIFTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAW------LPYPNPNphfQCGT-VD 314
Cdd:cd11253   263 DVFLLRTRDnknpEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWsvyegkVPYPRPG---SCASkVN 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  315 QGLYVNLTE---RNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFS--HVAVDVVQGREALVHIIYLATDYGTIKKVRVPL 389
Cdd:cd11253   340 GGHYGTTKDypdEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNlkQIAVDRVEAEDGQYDVLFIGTDNGIVLKVITIY 419

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767934735  390 NQTSSS---CLLEEIELFpeRRREPIRSLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11253   420 NQETETmeeVILEELQVF--KVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
 43-440 1.46e-73

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: 251.37  E-value: 1.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNLTE-------IHDQISGMAR 113
Cdd:cd11252    43 KKIYWPAAKERVELCKLAGKDANtECANFIRVLHpYNRTHVYVCGTGAFHPTCGYIELGTHKEdriflldTQNLESGRLK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  114 CPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPP---LRTAQYNSKWLNEPNFVSSYDIGNF-------TY 183
Cdd:cd11252   123 CPFDPQQPFASVMT-DEYLYAGTASDFLGKDTTFTRSLGPTPDhhyIRTDISEHYWLNGAKFIGTFPIPDTynpdddkIY 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  184 FFFRENAVEHDCG-KTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQSTFFLPELD----LI 256
Cdd:cd11252   202 FFFREASQDGSTSdKSVLSRVGRVCKNDVGGQRSLINKWTTFLKARLVCSIPGPdgADTHFDELQDIFLLPTRDernpVV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  257 YGIFTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLY---VNLTERNLQDAQKFI 333
Cdd:cd11252   282 YGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWVQYEGRIPYPRPGTCPSKTYdplIKSTKDFPDEVISFI 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  334 ----LMHEVVQPVTTVPSFMEDNS--RFSHVAVDVVQGREALVHIIYLATDYGTIKKVrVPLNQ---TSSSCLLEEIELF 404
Cdd:cd11252   362 krhpLMYKSVYPLTGGPVFTRINVdyRLTQIVVDHVAAEDGQYDVMFLGTDIGTVLKV-VSITKekwTMEEVVLEELQIF 440

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 767934735  405 peRRREPIRSLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11252   441 --KHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
 47-437 1.51e-72

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: 247.52  E-value: 1.51e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   47 WECDEATKKACYSKGKSKE-ECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNLT---EIHDQI--SGMARCPYSPQ 119
Cdd:cd11256    49 WPANDSKISECAFKKKSNEtECFNFIRVLVpVNGTHLYTCGTYAFSPACTYIELDHFSlppPNGTIItmDGKGQSPFDPQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  120 HNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNsKWLN-EPNFVSSYDI--GNFTYFFFRENAVEHDC- 195
Cdd:cd11256   129 HNYTAILV-DGELYTGTMNNFRGNEPIIFRNLGTKVSLKTDGFL-RWLNaDAVFVASFNPqgDSKVYFFFEETAREFDFf 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  196 GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFyyNELQSTFFLPELD----LIYGIFTT--NVNSIAA 269
Cdd:cd11256   207 EKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQLTCSQQGHFPF--NVIHHVALLNQPDpnnsVFYAVFTSqwQLGGRRS 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  270 SAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLYvnlTERNLQDAQKFILMHEVVQPVTTVPSFM 349
Cdd:cd11256   285 SAVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPVSDPRPGSCSGGKS---SDKALNFMKDHFLMDEVVLPGAGRPLLV 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  350 EDNSRFSHVAVDVVQGREALVH-IIYLATDYGTIKKVRVPlnQTSSSCLLEEIELFPErrREPIRSLQILHSQSVLFVGL 428
Cdd:cd11256   362 KSNVQYTRIAVDSVQGVSGHNYtVMFLGTDKGFLHKAVLM--GGSESHIIEEIELLTP--PEPVENLLLAANEGVVYIGY 437


                  ....*....
gi 767934735  429 REHVVKIPL 437
Cdd:cd11256   438 SAGVWRVPL 446
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
 43-437 8.60e-71

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: 243.23  E-value: 8.60e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKS-KEECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQI------SGMARC 114
Cdd:cd11257    45 QELTWSADEEKKQECSFKGKDpQRDCQNYIKILLrLNSTHLFTCGTYAFSPICTYIVMTNFSLERDEKgeplleDGKGRC 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  115 PYSPQHNSTALlTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAqyNS-KWLNEPNFVSSYDI----------GNFTY 183
Cdd:cd11257   125 PFDPEYKSTAI-MVDGELYTGTVSNFQGNDPIIYRSLGSGTPLKTE--NSlNWLQDPAFVGSAYIqeslpklvgdDDKIY 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  184 FFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEvPFYYNELQSTFFLPELD------LI 256
Cdd:cd11257   202 FFFSETGKEFDFfENTIVSRIARVCKGDEGGERVLQKRWTTFLKAQLLCSLPDD-GFPFNVLQDVFVLTPSPedwkdtLF 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  257 YGIFTTNVNSIAA--SAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGT----------VDQGLyvNLTER 324
Cdd:cd11257   281 YGVFTSQWHKGTAgsSAVCVFTMDQVQRAFNGLYKEVNRETQQWYTYTHPVPEPRPGAcitnsarerkINSSL--HMPDR 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  325 NLQDAQKFILMHevvQPVTTVPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVrvpLNQTSSSCLLEEIELF 404
Cdd:cd11257   359 VLNFVKDHFLMD---GQVRSQPLLLQPQVRYTQIAVHRVKGLHKTYDVLFLGTDDGRLHKA---VSVGPMVHIIEELQIF 432

                         410       420       430
                  ....*....|....*....|....*....|...
gi 767934735  405 PErrREPIRSLQILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11257   433 SE--GQPVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
 42-437 1.53e-70

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: 242.50  E-value: 1.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   42 RKAVEWECDEATKKACYSKGKSKE-ECQNYIRVL-LVGGDRLFTCGTNAFTPVCTNRSLSN--LTEIHDQISGMARCPYS 117
Cdd:cd11260    41 RAKVLWEVTEEKQKDCTNKGKHADiDCHNYIRILhKMNDSRMYVCGTNAFSPTCDYISYDDgqLTLEGKQEDGKGKCPFD 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  118 PQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGIlpPLRTaQYNSKWLNEPNFVSSYDI----------GNFTYFFFR 187
Cdd:cd11260   121 PFQRYSSVMV-DQDLYSATSMNFLGSEPVIMRSSPI--TIRT-EFKSSWLNEPNFIYMAAVpesedspegdDDKIYLFFS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  188 ENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRP-GEVPFYyneLQSTFFLPELD----LIYGIFT 261
Cdd:cd11260   197 ETAVEYDFyNKLVVSRVARVCKGDLGGQRTLQKKWTSFLKARLDCSVPePSLPYV---IQDVFHVCHQDwrkcVFYAVFT 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  262 TNVNSIAASAVCVFNLSAIAQAFS-GPFKYQ---ENSRSAW------LPYPNP----NPHFQCGTVDQGLyvNLTERNLQ 327
Cdd:cd11260   274 SQSDSSQSSAVCAYNVTDISNVFSrGKFKTPvavETSFVKWvmysgeLPVPRPgaciNNAARTSGIKKSL--NLPDKTLQ 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  328 DAQKFILMHEVVQPVTTVPSFMEDNSRFSHVAVDVVQGREALVH-IIYLATDYGTIKKVrvpLNQTSSSCLLEEIELF-P 405
Cdd:cd11260   352 FVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADGQSYpVMFIGTANGYVLKA---VNYDGEMHIIEEVQLFeP 428

                         410       420       430
                  ....*....|....*....|....*....|..
gi 767934735  406 ErrrEPIRSLQIlhSQSVLFVGLREHVVKIPL 437
Cdd:cd11260   429 E---EPIDILRL--SQNQLYAGSASGVVQMPV 455
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
 47-440 6.21e-70

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: 240.95  E-value: 6.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   47 WECDEATKKACYSKGKSKEE-CQNYIRVLL-VGGDRLFTCGTNAFTPVCT-----NRSLSNLTEIHDQI-SGMARCPYSP 118
Cdd:cd11251    47 WPASASKVEECKMAGKDPTHgCGNFVRVIQpYNRTHLYVCGSGAFSPVCVyvnrgRRSEEQVFHIDSKAeSGKGRCSFNP 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  119 QHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRENAV 191
Cdd:cd11251   127 NVNTVSVMI-NEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEPIFVDAHLIPDGTdpndaklYFFLKERLT 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  192 EHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQSTFFL----PELDLIYGIFTTNV 264
Cdd:cd11251   206 DNSgSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKARLVCSVMDEdgTETHFDELEDVFLLetdnPRTTLVYGIFTTSS 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  265 NSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTVDQGLY---VNLTERNLQDAQKFI----LMHE 337
Cdd:cd11251   286 SVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQGRIPYPRPGTCPGGAFtpnMQSTKEFPDDVVTFIrnhpLMFN 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  338 VVQPVTTVPSFMEDNS--RFSHVAVDVVQGREALVHIIYLATDYGTIKKVRV-PLNQTSSSCL-LEEIELFpeRRREPIR 413
Cdd:cd11251   366 PIYPIGRRPLLVRTGTdyKYTKIAVDRVNAADGRYHVLFLGTDKGTVQKVVVlPTNGSLSGELiLEELEVF--KNHAPIT 443

                         410       420
                  ....*....|....*....|....*..
gi 767934735  414 SLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11251   444 NMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
 40-437 3.78e-68

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: 235.81  E-value: 3.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   40 SGRKAVEWECDEATKKACYSKGK-SKEECQNYIRVLL-VGGDRLFTCGTNAFTPVCT-----NRSLSNLTEihdqiSGMA 112
Cdd:cd11262    41 SSALTIDWEASPEQKHQCLKKGKnNQTECFNHVRFLQrFNSTHLYTCGTHAFRPLCAyidaeRFTLSSQFE-----EGKE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  113 RCPYSPQHNSTALLTaGGELYAATAMDFpgRD-PAIYRSLGiLPPLRTAQYNSKWLNEPNFVSSY----DIGNFT----- 182
Cdd:cd11262   116 KCPYDPAKGYTGLIV-DGQLYTASQYEF--RSfPDIRRNSP-QPTLRTEEAPTRWLNDADFVGSVlvreSMNSSVgdddk 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  183 -YFFFRENAVEHDC--GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPgEVPFYYNELQSTFFL----PELDL 255
Cdd:cd11262   192 iYFFFTERSQEETAyfSQSRVARVARVCKGDRGGKKTLQRKWTSFLKARLVCYIP-EYEFLFNVLRSVFVLwgstPQDTV 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  256 IYGIFTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPY----PNPNPHfQCGTVD---QGLYvnlTERNLQD 328
Cdd:cd11262   271 FYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYtgkvPEPRPG-SCITDEhrsQGIN---SSQDLPD 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  329 -----AQKFILMHEVVQPVTTVPSFMEDNSRFSHVAVDVVQGREALV-HIIYLATDYGTIKKvrvPLNQTSSSCLLEEIE 402
Cdd:cd11262   347 nvldfVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDGRVyDVLFLGTDEGWLHK---AVVIGSAVHIIEELQ 423

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 767934735  403 LFpeRRREPIRSLQILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11262   424 VF--REPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
 42-437 4.84e-68

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: 235.47  E-value: 4.84e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   42 RKAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQIS-GMARCPYSP 118
Cdd:cd11258    43 QPPISWEAPAEKKTECAQKGKSNQtECFNYIRFLQpYNQSHLYTCGTYAFQPKCAYINMLTFTLDRAEFEdGKGKCPYDP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  119 QHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTaQYNSKWLNEPNFVSSY----DIGNFT------YFFFRE 188
Cdd:cd11258   123 AKGHTGLIV-DGELYSATLNNFLGTEPVILRNLGQHYSMKT-EYLAFWLNEPHFVGSAfvpeSVGSFTgdddkiYFFFSE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  189 NAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPgEVPFYYNELQSTFFLPELDL----IYGIFTTN 263
Cdd:cd11258   201 RAVEYDCdSEQVVARVARVCKGDLGGARTLQKKWTTFLKARLLCSIP-EWQLYFNQLKAVFTLEGASWrnttFFAVFQAR 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  264 VNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGTV------DQGLY--VNLTERNLQDAQKFILM 335
Cdd:cd11258   280 WGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDPVPSPRPGSCinnwhrDHGYTssLELPDNTLNFVKKHPLM 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  336 HEVVQPVTTVPSFMEDNSRFSHVAVDVVQG-REALVHIIYLATDYGTIKKVrVPLNqtSSSCLLEEIELFpeRRREPIRS 414
Cdd:cd11258   360 EDRVKPRLGRPLLVPCNSNFTHVVWTRVLGlDGETYSVLFIGTLDGWLIKA-VSLG--SWVHMIEELQVF--DQEPPESL 434

                         410       420
                  ....*....|....*....|...
gi 767934735  415 LQILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11258   435 VVSQSSKKLLFAGSRSELLQLPW 457
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
 45-437 8.02e-68

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: 235.14  E-value: 8.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   45 VEWECDEATKKACYSKGKSKE-ECQNYIRVLLVGGDR-LFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNS 122
Cdd:cd11259    55 LYWKVSEDKRTKCAVKGKSKQtECRNYIRVLQPLNDTfLYVCGTNAFQPTCDYLNLTSFRLLGKNEDGKGRCPFDPAQSY 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  123 TALLTaGGELYAATAMDFPGRDPAIYRSLGiLPPLRTaQYNSKWLNEPNFVSSYDI----------GNFTYFFFRENAVE 192
Cdd:cd11259   135 TSVMV-DGELYSGTSYNFLGSEPIISRNSS-QSPLRT-EYAIPWLNEPSFVFADVIradpdspdgeDDKIYFFFTEVSVE 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  193 HD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPgEVPFYYNELQSTFFLPELDL----IYGIFTTNVNSI 267
Cdd:cd11259   212 YEfVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSIP-DKNLVFNVVNDVFILKSPTLkepvIYGVFTPQLNNV 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  268 AASAVCVFNLSAIAQAFSGPfKYQ-----ENSRSAWLPY----PNPNP----HFQCGTVDQGLYVNLTERNLQDAQKFIL 334
Cdd:cd11259   291 GLSAVCAYNLSTVEEVFSKG-KYMqsatvEQSHTKWVRYngevPKPRPgaciNNEARAANYTSSLNLPDKTLQFVKDHPL 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  335 MHEVVQPVTTVPSFMEDNSRFSHVAVDVVQGREALVH-IIYLATDYGTIKKVrvpLNQTSSSCLLEEIELFPErrREPIR 413
Cdd:cd11259   370 MDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDGTIYdVMFISTDRGALHKA---ISLENEVHIIEETQLFPD--FEPVQ 444

                         410       420
                  ....*....|....*....|....*.
gi 767934735  414 SLQILHSQS--VLFVGLREHVVKIPL 437
Cdd:cd11259   445 TLLLSSKKGrrFLYAGSNSGVVQSPL 470
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
 43-440 2.50e-65

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: 228.26  E-value: 2.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNLTEiH----DQI---SGMAR 113
Cdd:cd11255    43 KEIHWPPLPGQREECIRKGKDPEtECANFVRVLQpFNRTHLLACGTGAFQPVCALINVGHRGE-HvfslDPTtveSGRGR 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  114 CPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRTaQYNSKWLNEPNFVSSYDI-------GNFTYFFF 186
Cdd:cd11255   122 CPHEPKRPFASTFT-GGELYTGLTADFLGRDSVIFRGFGTRSPLRT-ETDQRLLHEPRFVAAHLIpdnadrdNDKVYFFF 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  187 RENAVEHDCGK--TVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQSTFFL-------PEldl 255
Cdd:cd11255   200 TERATETAEDDdgAIHSRVGRLCANDAGGQRVLVNKWSTFIKARLVCSVPGPhgIQTHFDQLEDVFLLrtkdgksPE--- 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  256 IYGIFTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPY----PNPNPHFqC--GTVDQ-----GLYVNLTER 324
Cdd:cd11255   277 IYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPYegkvPYPRPGV-CpsKITAQpgrafRSTKDYPDE 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  325 NLQDAQKFILMHEVVQPVTTVPSFMEDNS--RFSHVAVDVVQGREALVHIIYLATDYGTIKKVrVPLNQTSSS----CLL 398
Cdd:cd11255   356 VLQFARAHPLMWRPVYPSHRRPVLVKTGLpyRLTQIVVDRVEAEDGYYDVMFIGTDSGSVLKV-IVLQKGNSAageeVTL 434

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 767934735  399 EEIELFpeRRREPIRSLQILHSQSVLFVGLREHVVKIPLKRC 440
Cdd:cd11255   435 EELQVF--KVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
 34-436 6.14e-61

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: 215.52  E-value: 6.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   34 VGGRPysgrKAVEWECDEATKKACYSKGKSKEECQNYIRVL-LVGGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQISGMA 112
Cdd:cd11261    42 SGERP----RRIDWMVPEAHRQNCRKKGKKEAECHNFIRILaIANASHLLTCGTFAFDPKCGVIDVSSFQQVERLESGRG 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  113 RCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSY----------DIGNFT 182
Cdd:cd11261   118 KCPFEPAQRSAAIM-AGGVLYAATVKNFLGTEPIISRAVGRAEEWIRTETLPSWLNAPAFVAAVflspaewgdeDGDDEI 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  183 YFFFRENAVEHDCGKTV-FSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRP--GEVpfyYNELQSTFFLPELD----- 254
Cdd:cd11261   197 YFFFTETAREYDSYERIkVPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGPehGRA---SSILQDVTTLRPLPgagtp 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  255 LIYGIFTTNVNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPY-----PNPNPHfQCGTVDQ-----GLYVNLTER 324
Cdd:cd11261   274 IFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGLPVmdsdvPQPRPG-ECITNNMkllgfGSSLSLPDR 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  325 NLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVA---VDVVQGREalVHIIYLATDYGTI-KKVRVplnqTSSSCLLEE 400
Cdd:cd11261   353 VLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAahrVTSLSGKE--YDVLYLGTEDGHLhRAVRI----GAQLSVLED 426

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 767934735  401 IELFPErrREPIRSLQILHSQsvLFVGLREHVVKIP 436
Cdd:cd11261   427 LALFPE--PQPVENLQLHHNW--LLVGSDTEVTQIN 458
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
 43-437 1.02e-55

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: 198.58  E-value: 1.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   43 KAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGG--DRLFTCGTNAFTPVCTNRSLsNLTEIHDQI---SGMARCPYS 117
Cdd:cd09295    39 PELNFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGdlDILAVCGSNAAQPSCGSYRL-DVLVELGKVrwpSGRPRCPID 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  118 PQHNSTALLTAGgELYAATAMDF-PGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIG---NFTYFFFRENAVEH 193
Cdd:cd09295   118 NKHSNMGVNVDS-KLYSATDHDFkDGDRPALSRRSSNVHYLRIVVDSSTGLDEITFVYAFVSGdddDEVYFFFRQEPVEY 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  194 DC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEvPFYYNELQSTFFL---PELDLIYGIFTTNVNSIAA 269
Cdd:cd09295   197 LKkGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSRPQS-GFAFNLLQDATGDtknLIQDVKFAIFSSCLNKSVE 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  270 SAVCVFNLSAIAQAFSGPFKYQENsrsawlpYPnpnphfqcgtvdqgLYVNLTERnlqdaqkfilmhevvqpvttvpsfm 349
Cdd:cd09295   276 SAVCAYLFTDINNVFDDPVEAINN-------RP--------------LYAHQNQR------------------------- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  350 ednSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVpLNQTSSSCLLEEIELFpeRRREPIRSLQILHSQSVLFVGLR 429
Cdd:cd09295   310 ---SRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKALA-FFFLYKGHIIEEWKVF--KDSSRITNLDLSRPPLYLYVGSE 383


                  ....*...
gi 767934735  430 EHVVKIPL 437
Cdd:cd09295   384 SGVLGVPV 391
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
 244-419 1.69e-51

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: 179.00  E-value: 1.69e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   244 LQSTFFLPEL------DLIYGIFTTN-VNSIAASAVCVFNLSAIAQAFSGPFKYQENSRSAWLPYPNPNPHFQCGT-VDQ 315
Cdd:pfam01403    1 LQDVFVLKPGagdaldTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTcIND 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   316 GLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVAVDVVQGREALVHIIYLATDYGTIKKVRVPLNQTssS 395
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEE--S 158

                          170       180
                   ....*....|....*....|....
gi 767934735   396 CLLEEIELFPErrREPIRSLQILH 419
Cdd:pfam01403  159 HIIEEIQVFPE--PQPVLNLLLSS 180
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
 34-437 8.34e-50

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: 182.35  E-value: 8.34e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   34 VGGR------PYSGRKA-VEWECDEATKKACYSKGkSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNrsLSNLTEIHD 106
Cdd:cd11243    18 VGGQgalyllDFTGSAViVKKIPDEKTEKDCKKRA-TLDDCENYITLIKKLDYRLLVCGTNAGSPKCWF--LVNQTLVTL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  107 QiSGMARCPYSPQHNStALLTAGGELYAATAmdfpGRDPAI--YRSLGILPPLRTAqynSKWLNEPNFVSS--------Y 176
Cdd:cd11243    95 S-ADRGVAPFLPDENS-LVLIEGNNVYSTIS----GKKGNIprFRRYGGKKELYTS---DTVMQKPQFVKAtllpedeqY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  177 DigNFTYFFFREN--AVEHDCGKTVfSRAARVCKNDIGGRFLLE-DTWTTFMKARLNCSRPGEvPFYYNELQSTFFLP-- 251
Cdd:cd11243   166 Q--DKIYYFFREDneDKGPEAEPNI-SRVARLCKEDQGGTSSLStSKWSTFLKARLVCGDPAT-PMNFNRLQDVFLLPke 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  252 --ELDLIYGIFTTNVNSiaaSAVCVFNLSAIAQAFSgpfkyqenSRSAW-LPYPNPNPH-FQCGTVDQglyvNLTERNLQ 327
Cdd:cd11243   242 ewREAVVYGVFSNTWGS---SAVCSYSLGDIDKVFR--------TSSLKgYSGSLPNPRpGTCVPPEQ----THPSETFS 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  328 DAQKFILMHEVVQPVTTVPSFM-EDNSRFSHVAVDVVQGREAL-VHIIYLATDYGTIKKVRVPLNQTSSsclLEEIELFp 405
Cdd:cd11243   307 FADEHPELDDRIEPDEPRKLPVfQNKDHYQKVVVDEVRASDGVsYDVLYLATDKGKIHKVVESKGQTHN---IMEIQPF- 382

                         410       420       430
                  ....*....|....*....|....*....|..
gi 767934735  406 eRRREPIRSLQILHSQSVLFVGLREHVVKIPL 437
Cdd:cd11243   383 -KEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 797-849 4.11e-17

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 76.09  E-value: 4.11e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    797 WSCWSPWTKCSATCGGGHYMRTRSCSNPAPAYGGDICLGLHTEEALCNTQPCP 849
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 551-604 1.27e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.27e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767934735    551 WTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERYCNEHlLCP 604
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 740-792 2.97e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 2.97e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    740 WSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEYQECNILPCP 792
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 609-655 1.70e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 59.91  E-value: 1.70e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767934735    609 WTGWGPWERCTAQCGGGIQARRRICENGP------DCAGCNVEYQSCNTNPCP 655
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggPCTGEDVETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 552-600 2.06e-09

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 54.21  E-value: 2.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767934735   552 TPWTSWSPCSTTCGIGFQVRQRSCSNPtPRHGGRVCvGQNREERYCNEH 600
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLP 50
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
 55-284 3.22e-09

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


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 60.04  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735   55 KACYSKGKSKEECQNYIRVLLV--GGDRLFTCGTnAFTPVCTNRSLSNLTEIHdQISGMARCPYSPQHNSTALLTAGGE- 131
Cdd:cd11236    49 PGCCSCDHPRSPTDNYNKILLIdySSGRLITCGS-LYQGVCQLRNLSNISVVV-ERSSTPVAANDPNASTVGFVGPGPYn 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  132 ----LYAATAMD---FPGRDPAI-YRSLGILPPLRTAQYN--SKWLNEPNFVSSYDI--------GNFTYFFFRENAVeH 193
Cdd:cd11236   127 nenvLYVGATYTnngYRDYRPAVsSRSLPPDDDFNAGSLTggSAISIDDEYRDRYSIkyvygfssGGFSYFVTVQRKS-V 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  194 DCGKTVFSRAARVCKNDIGgrflledtWTTFMKARLNC-SRPGEVpfyYNELQSTF-------------FLPELDLIYGI 259
Cdd:cd11236   206 DDESPYISRLVRVCQSDSN--------YYSYTEVPLQCtGGDGTN---YNLLQAAYvgkagsdlarslgISTDDDVLFGV 274

                         250       260
                  ....*....|....*....|....*....
gi 767934735  260 FTTNVNSIAA----SAVCVFNLSAIAQAF 284
Cdd:cd11236   275 FSKSKGPSAEpsskSALCVFSMKDIEAAF 303
TSP_1 pfam00090
Thrombospondin type 1 domain;
798-848 3.47e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 3.47e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767934735   798 SCWSPWTKCSATCGGGHYMRTRSCSNPAPayGGDICLGLHTEEALCNTQPC 848
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-598 7.24e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.42  E-value: 7.24e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767934735   552 TPWTSWSPCSTTCGIGFQVRQRSCSNPTPrhGGRVCVGQNREERYCN 598
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACK 45
TSP_1 pfam00090
Thrombospondin type 1 domain;
741-791 7.98e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.42  E-value: 7.98e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767934735   741 SAWTSWSQCSRDCSRGIRNRKRVCNNPEPkyGGMPCLGPSLEYQECNILPC 791
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 439-486 3.47e-08

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: 50.78  E-value: 3.47e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767934735   439 RCQFYRTRSTCIGAQDPYCGWDVVMKKCTS----LEESLSMTQWEQSISACP 486
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 497-548 9.54e-08

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 9.54e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767934735    497 GVWSPWTPCTHTDGSAVgscLCRTRSCDSPAPQCGGWQCEGPGMEIANCSRN 548
Cdd:smart00209    2 SEWSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
 130-467 1.54e-07

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: 55.32  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  130 GELYAATAMD-----FPG-------RDPaiyRSLGILPPLRTAQYNSKWLNEPN----FVSSYDI--------GNFTYFF 185
Cdd:cd11272   143 GKLFIGTAVDgkqdyFPTlssrklpRDP---ESSAMLDYELHSDFVSSLIKIPSdtlaLVSHFDIfyiygfasGNFVYFL 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  186 F-----RENAVEHDCGKTVF-SRAARVCKNDiggrflleDTWTTFMKARLNCSRPGEvpfYYNELQSTFF---------- 249
Cdd:cd11272   220 TvqpetPEGVSINSAGDLFYtSRIVRLCKDD--------PKFHSYVSLPFGCVRGGV---EYRLLQAAYLskpgevlars 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  250 ---LPELDLIYGIFTTNVNSIAA----SAVCVFNLSA----IAQAFSGPFKYQENSRSAWL----------PYPnPNPHF 308
Cdd:cd11272   289 lniTAQEDVLFAIFSKGQKQYHHppddSALCAFPIRAinaqIKERLQSCYQGEGNLELNWLlgkdvqctkaPVP-IDDNF 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  309 qCG-TVDQGLYVNlternlqdaqkfilmhevvQPVTTVPSFMEDNSRFSHVAVDVVQGREalvhIIYLATDYGTIKKVRV 387
Cdd:cd11272   368 -CGlDINQPLGGS-------------------TPVEGVTLYTSSRDRLTSVASYVYNGYS----VVFVGTKSGKLKKIRA 423

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934735  388 --PLNqtsSSCLLEEIELFpeRRREPI-RSLQILHSQSVLFVGLREHVVKIPLKRCQFYRTRSTCIGAQDPYCGWDVVMK 464
Cdd:cd11272   424 dgPPH---GGVQYEMVSVF--KDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDPHCGWCALHN 498


                  ...
gi 767934735  465 KCT 467
Cdd:cd11272   499 MCS 501
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 800-848 3.81e-07

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 47.66  E-value: 3.81e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767934735   800 WSPWTKCSATCGGGHYMRTRSCSNPaPAYGGDIClGLHTEEALCNTQPC 848
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
853-896 1.09e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 1.09e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767934735   853 SEWSDWSECEAS---GVQVRARQCILLFPMGSQCSGNTTESRPCVFD 896
Cdd:pfam00090    1 SPWSPWSPCSVTcgkGIQVRQRTCKSPFPGGEPCTGDDIETQACKMD 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 852-893 1.16e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.43  E-value: 1.16e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 767934735    852 WSEWSDWSECEAS---GVQVRARQCIL--LFPMGSQCSGNTTESRPC 893
Cdd:smart00209    1 WSEWSEWSPCSVTcggGVQTRTRSCCSppPQNGGGPCTGEDVETRAC 47
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 741-791 1.67e-06

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 45.73  E-value: 1.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767934735   741 SAWTSWSQCSRDCSRGIRNRKR---VcnnpEPKYGGMPClGPSLEYQECNILPC 791
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRtviV----EPQNGGRPC-PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
612-654 4.63e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 4.63e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767934735   612 WGPWERCTAQCGGGIQARRRIC----ENGPDCAGCNVEYQSCNTNPC 654
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
439-477 1.49e-05

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 42.92  E-value: 1.49e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 767934735    439 RCQFYRTRSTCIGAQDPYCGWDVVMKKCTSLEESLSMTQ 477
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRRQ 39
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 555-600 2.22e-05

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 42.83  E-value: 2.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767934735   555 TSWSPCSTTCGIGFQVRQRSCSNPTPR--HGGRVCVGQNR--EERYCNEH 600
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLK 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 853-893 1.43e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 40.34  E-value: 1.43e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767934735   853 SEWSDWSECEAS---GVQVRARQcILLFPM--GSQCsGNTTESRPC 893
Cdd:pfam19028    4 SEWSEWSECSVTcggGVQTRTRT-VIVEPQngGRPC-PELLERRPC 47
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 852-894 8.29e-04

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 43.01  E-value: 8.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767934735  852 WSEWSDWSEC-----EASGVQVRARQCIllFPMGSQCSGNTTESRPCV 894
Cdd:PTZ00087  233 YTEWGEWSNCsmecdHPDNVQIRERKCA--HPSGDCFKGDLKETRPCQ 278
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 610-654 2.80e-03

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 36.87  E-value: 2.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767934735   610 TGWGPWERCTAQCGGGIQARRRIC-----ENGPDCAGcNVEYQSCNTNPC 654
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVivepqNGGRPCPE-LLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
497-546 3.61e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.24  E-value: 3.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767934735   497 GVWSPWTPCTHTDGSAVGSclcRTRSCDSPAPqcGGWQCEGPGMEIANCS 546
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQV---RQRTCKSPFP--GGEPCTGDDIETQACK 45
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 802-848 3.74e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 36.66  E-value: 3.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767934735   802 PWTKCSATCGGGhyMRTRS--CSNPAP--AYGGDICLGLH--TEEALCNTQPC 848
Cdd:pfam19030    5 PWGECSVTCGGG--VQTRLvqCVQKGGgsIVPDSECSAQKkpPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 613-654 7.92e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 35.51  E-value: 7.92e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767934735   613 GPWERCTAQCGGGIQARRRIC--------ENGPDCAGCN--VEYQSCNTNPC 654
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCvqkgggsiVPDSECSAQKkpPETQSCNLKPC 55
 
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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