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Conserved domains on  [gi|1984005256|ref|XP_039315008|]
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semaphorin-5B isoform X2 [Solenopsis invicta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
 38-467 0e+00

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: 824.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGKSLF 117
Cdd:cd11265      1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSRgpSGGLFAGAPTDFSGADPAIYRTLASPN---LR 194
Cdd:cd11265     81 ACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSS--SGQLFVGSPTDFSGSDSAIYRTLGTSNksfLR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  195 TRQYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMM-KDVWTTFSKARLNCSLPGE 273
Cdd:cd11265    159 TKQYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLlKDNWTTFLKARLNCSLPGE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  274 FPFYYDEIQGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQrcGSPSS 353
Cdd:cd11265    239 YPFYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVNVNHRDHF--NQCSS 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  354 TAPHQIMDNQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTVLYVSTATGLIKKISVLPRTQETCIVEI 433
Cdd:cd11265    317 SSSSHLLESSRYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKIHQSVHVLYVATTGGLIKKISVLPRTQETCLVEI 396

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1984005256  434 WGSLP---SPPMTLQFLKDTQSLYVGMEIGLLRIPAV 467
Cdd:cd11265    397 WQPLPtpdSPIKTMQYLKVTDSLYVGTELALMRIPAQ 433
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 666-717 1.56e-13

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: 66.07  E-value: 1.56e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256   666 WSTWGPWHACSKPCNGGIRVRKRTCDSPSSKKGGAECPGCDQQIEECNAHEC 717
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 854-900 1.86e-12

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: 62.99  E-value: 1.86e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1984005256   854 WSCWTDWSECSASCGIGVRTRTRECLGP------ESCSGPRSIRETCEMPSCE 900
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPppqnggGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 599-645 4.34e-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: 59.14  E-value: 4.34e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1984005256   599 WTAWSAWSACSQTCGFAMKTRRRTCTNPAPAFGGRVCVGHDHDDIMC 645
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 796-841 4.62e-10

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: 56.06  E-value: 4.62e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256   796 WGEWSSWGICDRPCGRGSQHRVRQCESPPCEN------GLTKQSRVCNPHPC 841
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNgggpctGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 526-596 9.17e-05

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: 41.03  E-value: 9.17e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1984005256   526 WSAWSPWSTCQHGTGEqssghghphshshsehaekidTCQCQTRECNNPPPQHGGESCTGTRVRVTNCTVH 596
Cdd:smart00209    1 WSEWSEWSPCSVTCGG---------------------GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 905-944 6.08e-03

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: 36.03  E-value: 6.08e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1984005256   905 WDTWSLWTPCD---GDHQQHRKRICL----EHGSGMCQGKDREIRDC 944
Cdd:smart00209    1 WSEWSEWSPCSvtcGGGVQTRTRSCCspppQNGGGPCTGEDVETRAC 47
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 469-516 6.32e-03

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: 35.76  E-value: 6.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  469 CYRHRSRQACLNAQEPYCGWNEHLMKCAQAPKQNYLANH---WHQEVTKCP 516
Cdd:pfam01437    2 CSQYTSCSSCLAARDPYCGWCSSEGRCVRRSACGAPEGNceeWEQASSKCP 52
 
Name Accession Description Interval E-value
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
 38-467 0e+00

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: 824.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGKSLF 117
Cdd:cd11265      1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSRgpSGGLFAGAPTDFSGADPAIYRTLASPN---LR 194
Cdd:cd11265     81 ACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSS--SGQLFVGSPTDFSGSDSAIYRTLGTSNksfLR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  195 TRQYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMM-KDVWTTFSKARLNCSLPGE 273
Cdd:cd11265    159 TKQYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLlKDNWTTFLKARLNCSLPGE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  274 FPFYYDEIQGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQrcGSPSS 353
Cdd:cd11265    239 YPFYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVNVNHRDHF--NQCSS 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  354 TAPHQIMDNQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTVLYVSTATGLIKKISVLPRTQETCIVEI 433
Cdd:cd11265    317 SSSSHLLESSRYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKIHQSVHVLYVATTGGLIKKISVLPRTQETCLVEI 396

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1984005256  434 WGSLP---SPPMTLQFLKDTQSLYVGMEIGLLRIPAV 467
Cdd:cd11265    397 WQPLPtpdSPIKTMQYLKVTDSLYVGTELALMRIPAQ 433
Sema smart00630
semaphorin domain;
46-440 1.18e-104

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 333.57  E-value: 1.18e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256    46 YSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHA-SWSAPEDKVNTCQNKGQSV-EDCRNYVKVLLS-NGKSLFTCGTY 122
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKtGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLDyNEDRLLVCGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   123 AFSPWCAWREIENitsvtsemsgvamcpysphanvtallsrgpsggLFAGAPTDFSGADPAIYRTLASPN--------LR 194
Cdd:smart00630   81 AFQPVCRLRNLGE---------------------------------LYVGTVADFSGSDPAIPRSLSVRRlkgtsgvsLR 127

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   195 TRQYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSLPGEF 274
Cdd:smart00630  128 TVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGED 207

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   275 PFYYDEIQgAAYHPEEG-----IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQRCG 349
Cdd:smart00630  208 PFYFNELQ-AAFLLPPGsesddVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRGKVPYPRPG 286

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   350 S----PSSTA--PHQIMDN-QRYQLMDEAVQSTMLEPLHTATLE--RFIHIAVDVTPTklHRSVTVLYVSTATGLIKKIS 420
Cdd:smart00630  287 TcpnkPPSSKdlPDETLNFiKSHPLMDEVVQPLTGRPLFVKTDSnyLLTSIAVDRVAT--DGNYTVLFLGTSDGRILKVV 364

                           410       420
                    ....*....|....*....|....
gi 1984005256   421 VLP---RTQETCIVEIW-GSLPSP 440
Cdd:smart00630  365 LSEsssSSESVVLEEISvFPDGSP 388
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
 292-440 3.16e-31

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: 120.84  E-value: 3.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  292 IIYATFTTPI-NGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNrQRCGS-PSSTAPHQIMDN-----QR 364
Cdd:pfam01403   18 VLYGVFTTQWsNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPY-PRPGTcINDPLRLDLPDSvlnfvKD 96

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1984005256  365 YQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTkLHRSVTVLYVSTATGLIKKIsVLPRTQETCIVEIWGSLPSP 440
Cdd:pfam01403   97 HPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQA-LDGNYTVLFLGTDDGRLHKV-VLVGSEESHIIEEIQVFPEP 170
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 666-717 1.56e-13

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: 66.07  E-value: 1.56e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256   666 WSTWGPWHACSKPCNGGIRVRKRTCDSPSSKKGGAECPGCDQQIEECNAHEC 717
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 854-900 1.86e-12

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: 62.99  E-value: 1.86e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1984005256   854 WSCWTDWSECSASCGIGVRTRTRECLGP------ESCSGPRSIRETCEMPSCE 900
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPppqnggGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
667-717 3.56e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 58.97  E-value: 3.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  667 STWGPWHACSKPCNGGIRVRKRTCDSPssKKGGAECPGCDQQIEECNAHEC 717
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSP--FPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 599-645 4.34e-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: 59.14  E-value: 4.34e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1984005256   599 WTAWSAWSACSQTCGFAMKTRRRTCTNPAPAFGGRVCVGHDHDDIMC 645
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 796-841 4.62e-10

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: 56.06  E-value: 4.62e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256   796 WGEWSSWGICDRPCGRGSQHRVRQCESPPCEN------GLTKQSRVCNPHPC 841
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNgggpctGEDVETRACNEQPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 797-841 1.29e-08

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: 51.90  E-value: 1.29e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1984005256  797 GEWSSWGICDRPCGRGSQHRVRQCESPPCENG----LTKQSRVCNPHPC 841
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGrpcpELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
855-899 5.99e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 5.99e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1984005256  855 SCWTDWSECSASCGIGVRTRTREC----LGPESCSGPRSIRETCEMPSC 899
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 600-635 2.33e-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: 45.35  E-value: 2.33e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1984005256  600 TAWSAWSACSQTCGFAMKTRRRTCTNPaPAFGGRVC 635
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC 38
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 526-596 9.17e-05

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: 41.03  E-value: 9.17e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1984005256   526 WSAWSPWSTCQHGTGEqssghghphshshsehaekidTCQCQTRECNNPPPQHGGESCTGTRVRVTNCTVH 596
Cdd:smart00209    1 WSEWSEWSPCSVTCGG---------------------GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 855-899 1.88e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1984005256  855 SC--WTDWSECSASCGIGVRTRTRECLGpESCSgpRSIRETCEMPSC 899
Cdd:PTZ00441   239 SCgpWDEWTPCSVTCGKGTHSRSRPILH-EGCT--THMVEECEEEEC 282
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 905-944 6.08e-03

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: 36.03  E-value: 6.08e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1984005256   905 WDTWSLWTPCD---GDHQQHRKRICL----EHGSGMCQGKDREIRDC 944
Cdd:smart00209    1 WSEWSEWSPCSvtcGGGVQTRTRSCCspppQNGGGPCTGEDVETRAC 47
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 469-516 6.32e-03

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: 35.76  E-value: 6.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  469 CYRHRSRQACLNAQEPYCGWNEHLMKCAQAPKQNYLANH---WHQEVTKCP 516
Cdd:pfam01437    2 CSQYTSCSSCLAARDPYCGWCSSEGRCVRRSACGAPEGNceeWEQASSKCP 52
 
Name Accession Description Interval E-value
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
 38-467 0e+00

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: 824.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGKSLF 117
Cdd:cd11265      1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSRgpSGGLFAGAPTDFSGADPAIYRTLASPN---LR 194
Cdd:cd11265     81 ACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSS--SGQLFVGSPTDFSGSDSAIYRTLGTSNksfLR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  195 TRQYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMM-KDVWTTFSKARLNCSLPGE 273
Cdd:cd11265    159 TKQYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLlKDNWTTFLKARLNCSLPGE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  274 FPFYYDEIQGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQrcGSPSS 353
Cdd:cd11265    239 YPFYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVNVNHRDHF--NQCSS 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  354 TAPHQIMDNQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTVLYVSTATGLIKKISVLPRTQETCIVEI 433
Cdd:cd11265    317 SSSSHLLESSRYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKIHQSVHVLYVATTGGLIKKISVLPRTQETCLVEI 396

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1984005256  434 WGSLP---SPPMTLQFLKDTQSLYVGMEIGLLRIPAV 467
Cdd:cd11265    397 WQPLPtpdSPIKTMQYLKVTDSLYVGTELALMRIPAQ 433
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
 38-467 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: 765.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGKSLF 117
Cdd:cd11241      1 FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSVEECQNYVRVLLVVGKNLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSRgpSGGLFAGAPTDFSGADPAIYRTLAS-PNLRTR 196
Cdd:cd11241     81 TCGTYAFSPVCTIRKLSNLTQILDTISGVARCPYSPAHNSTALISA--SGELYAGTVYDFSGRDPAIYRSLGGkPPLRTA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  197 QYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSLPGEFPF 276
Cdd:cd11241    159 QYNSKWLNEPNFVGSYEIGNHTYFFFRENAVEHQDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGEFPF 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  277 YYDEIQGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQ-----RCGSP 351
Cdd:cd11241    239 YYNEIQGTFYLPETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPTPNPHPNFQcttsiDRGQP 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  352 SSTAPHQIMDNQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTVLYVSTATGLIKKISVLPRTQETCIV 431
Cdd:cd11241    319 ANTTERDLQDAQKYQLMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRGTQLVHIFYVGTDYGTILKMYQPHRSQKSCTL 398

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1984005256  432 EIWGSLP----SPPMTLQFLKDTQSLYVGMEIGLLRIPAV 467
Cdd:cd11241    399 EEIKILPamkgEPITSLQFLKSEKSLFVGLETGVLRIPLN 438
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
 44-467 0e+00

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


Pssm-ID: 200496 [Multi-domain]  Cd Length: 437  Bit Score: 614.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   44 TTYSQLLFDVARQQVVVGARDNLYRLTLTSL-TDLEHASWSAPeDKVNTCQNKGQSVEDCRNYVKVLLSNG-KSLFTCGT 121
Cdd:cd11235      1 LKYHTKLLHEDRSTLYVGARDRVYLVDLDSLyTEQKVAWPSSP-DDVDTCYLKGKSKDDCRNFIKVLEKNSdDSLLVCGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  122 YAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSRGpsgGLFAGAPTDFSGADPAIYRTL-ASPNLRTRQYDS 200
Cdd:cd11235     80 NAFNPSCRNYNVETFELVGKEESGRGKCPYDPDHNSTALFADG---ELYSGTSADFLGTDPVIYRTLgHNPPLRTEYHDS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  201 KWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSLPGEFPFYYDE 280
Cdd:cd11235    157 KWLNEPQFVGAFDIGDYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFPFYFNE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  281 IQGAAYHPE----EGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVA----HHNRQRCGSPS 352
Cdd:cd11235    237 LQDVFDLPSpsnkEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDErvpePRPGTCVDDSS 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  353 STAPHQIMDNQRYQLMDEAVQSTMLEPLHTATL--ERFIHIAVDVTPTKLHRSVTVLYVSTATGLIKKISVLPRT--QET 428
Cdd:cd11235    317 PLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDvnYRFTKIAVDRVQAKLGQTYDVLFVGTDRGIILKVVSLPEQglQAS 396

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1984005256  429 CIVEIWGSLP--SPPMTLQFLKDTQSLYVGMEIGLLRIPAV 467
Cdd:cd11235    397 NILEEMPVGPppEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
 38-465 1.87e-146

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: 445.58  E-value: 1.87e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGKSLF 117
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSRgpSGGLFAGAPTDFSGADPAIYRTLAS-PNLRTR 196
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITS--RGELYAATVIDFSGRDPAIYRSLGSvPPLRTA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  197 QYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYiNCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSLPGEFPF 276
Cdd:cd11264    159 QYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPF 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  277 YYDEIQGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQrCGSPSSTAP 356
Cdd:cd11264    238 YYNELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQ-CGTLSDDSP 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  357 HQ------IMDNQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTK--LHRsvtVLYVSTATGLI-KKISVLPRTQE 427
Cdd:cd11264    317 NEnltersLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKdtLYH---VMYIGTEYGTIlKALSTTNRSLR 393

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1984005256  428 TCIVEIWGSLPS----PPMTLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd11264    394 SCYLEEMQILPPgqrePIRSLQILHSDRSLFVGLNNGVLKIP 435
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
 38-465 7.90e-141

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: 430.61  E-value: 7.90e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGKSLF 117
Cdd:cd11263      1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSrgPSGGLFAGAPTDFSGADPAIYRTLAS-PNLRTR 196
Cdd:cd11263     81 TCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLT--SSGELYAATAMDFPGRDPAIYRSLGIlPPLRTA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  197 QYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYiNCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSLPGEFPF 276
Cdd:cd11263    159 QYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPF 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  277 YYDEIQGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQrCGSPSS--- 353
Cdd:cd11263    238 YYNELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQ-CGTMDQgly 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  354 --TAPHQIMDNQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKlHRSVTVLYVSTATGLIKKI-SVLPRTQETCI 430
Cdd:cd11263    317 vnLTERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGK-DMLFHIIYLATDYGTIKKVlAPLNQSSSSCL 395

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1984005256  431 VEIWGSLP----SPPMTLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd11263    396 LEEIELFPkrqrEPIRSLQILHSQSVLFVGLQEHVIKIP 434
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
 50-422 1.79e-118

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: 372.43  E-value: 1.79e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   50 LFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVL-LSNGKSLFTCGTYAFSPWC 128
Cdd:cd11237      9 LLDQDGNSLLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLaKKSAGRLLVCGTNAYKPLC 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  129 AWREIENITS-VTSEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTlaspNLRTRQYDSKWLNDPQ 207
Cdd:cd11237     89 REYTVKDGGYrVEREFDGQGLCPYDPKHNSTAVYA---DGQLYSATVADFSGADPLIYRE----PLRTERYDLKQLNAPN 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  208 FVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSLPGEFPFYYDEIQ----- 282
Cdd:cd11237    162 FVSSFAYGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGEYPFYFNEIQstsdi 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  283 --GAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAW---ERRPVAHHNRQRCGSPSSTAPh 357
Cdd:cd11237    242 veGGYGGKSAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWlpvPSNKVPEPRPGQCVNDSRTLP- 320

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  358 QIMDN--QRYQLMDEAVQSTMLEPL--HTATLERFIHIAVDVTPTKLH-RSVTVLYVSTATG-LIKKISVL 422
Cdd:cd11237    321 DVTVNfiKSHPLMDEAVPSFFGRPIlvRTSLQYRFTQIAVDPQVKALDgKYYDVLFIGTDDGkVLKAVNIA 391
Sema smart00630
semaphorin domain;
46-440 1.18e-104

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 333.57  E-value: 1.18e-104
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256    46 YSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHA-SWSAPEDKVNTCQNKGQSV-EDCRNYVKVLLS-NGKSLFTCGTY 122
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKtGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLDyNEDRLLVCGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   123 AFSPWCAWREIENitsvtsemsgvamcpysphanvtallsrgpsggLFAGAPTDFSGADPAIYRTLASPN--------LR 194
Cdd:smart00630   81 AFQPVCRLRNLGE---------------------------------LYVGTVADFSGSDPAIPRSLSVRRlkgtsgvsLR 127

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   195 TRQYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSLPGEF 274
Cdd:smart00630  128 TVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGED 207

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   275 PFYYDEIQgAAYHPEEG-----IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQRCG 349
Cdd:smart00630  208 PFYFNELQ-AAFLLPPGsesddVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRGKVPYPRPG 286

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   350 S----PSSTA--PHQIMDN-QRYQLMDEAVQSTMLEPLHTATLE--RFIHIAVDVTPTklHRSVTVLYVSTATGLIKKIS 420
Cdd:smart00630  287 TcpnkPPSSKdlPDETLNFiKSHPLMDEVVQPLTGRPLFVKTDSnyLLTSIAVDRVAT--DGNYTVLFLGTSDGRILKVV 364

                           410       420
                    ....*....|....*....|....
gi 1984005256   421 VLP---RTQETCIVEIW-GSLPSP 440
Cdd:smart00630  365 LSEsssSSESVVLEEISvFPDGSP 388
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
 46-464 3.36e-99

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: 321.30  E-value: 3.36e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   46 YSQLLFDVARQQVVVGARDNLYRLTLTSLTD----LEHASWSAPEDKVNTCQNKGQSVE-DCRNYVKVL--LSNGKSLFT 118
Cdd:cd11238      3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINDtgnnCARDELTLSPSDVSECVSKGKDEEyECRNHVRVIqpMGDGQTLYV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  119 CGTYAFSPwcAWREIENITSVTSEM-----SGVAMCPYSPHANVTA-LLSRGPSG---GLFAGAPTDFSGADPAIYRT-- 187
Cdd:cd11238     83 CSTNAMNP--KDRVLDANLLHLPEYvpgpgNGIGKCPYDPDDNSTAvWVEWGNPGdlpALYSGTRTEFTKANTVIYRPpl 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  188 ------LASPNLRTRQYDSKWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTF 261
Cdd:cd11238    161 ynntkgRHESFMRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETAVEYINCGKVVYSRVARVCKKDTGGKNVLRQNWTTF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  262 SKARLNCSLPGEFPFYYDEIQGAAYHP--EEGIIYATFTTPINGIAGSAICAFNMSAVFASFN-GPFKYQENAGAAWERR 338
Cdd:cd11238    241 LKARLNCSISGEFPFYFNEIQSVYKVPgrDDTLFYATFTTSENGFTGSAVCVFTLSDINAAFDtGKFKEQASSSSAWLPV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  339 P---VAHHNRQRCGSPSSTAPHQIMDNQR-YQLMDEAVQSTmlEPLHTATLERFIHIAVDVTPTKlHRSVTVLYVSTATG 414
Cdd:cd11238    321 LsseVPEPRPGTCVNDSATLSDTVLHFARtHPLMDDAVSHG--PPLLYLRDVVFTHLVVDKLRID-DQEYVVFYAGSNDG 397

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256  415 LIKKISVLPRTQE--TCIVEIWGSLPSPPMTLQFLKDTQSLYVGMEIGLLRI 464
Cdd:cd11238    398 KVYKIVHWKDAGEskSNLLDVFELTPGEPIRAMELLPGEFLYVASDHRVSQI 449
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
 55-425 4.95e-91

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: 299.82  E-value: 4.95e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   55 RQQVVVGARDNLYRLTL-----TSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLS-NGKSLFTCGTYAFSPWC 128
Cdd:cd11242     18 NRTLYIAARDHVYTVDLdashtEEIVPSKKLTWRSRQADVENCRMKGKHKDECHNFIKVLVPrNDETLFVCGTNAFNPVC 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  129 AWREIENITSVTSEMSGVAMCPYSP-HANVtALLSrgpSGGLFAGAPTDFSGADPAIYRTLA-SPNLRTRQYDSKWLNDP 206
Cdd:cd11242     98 RNYRIDTLEQDGEEISGMARCPFDAkQANV-ALFA---DGKLYSATVTDFLASDAVIYRSLGdSPTLRTVKYDSKWLKEP 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  207 QFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGG-QIMMKDVWTTFSKARLNCSLPGEFPFYYDEIQGAA 285
Cdd:cd11242    174 HFVHAVEYGDYVYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPGDSHFYFDVLQAVT 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  286 YHPEEG---IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQRCGS-----------P 351
Cdd:cd11242    254 DVIRINgrpVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPEDRVPKPRPGCcagsgsaekykT 333

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1984005256  352 SSTAPHQIMDN-QRYQLMDEAVQSTMLEPLHTATLERF--IHIAVDVTPTKlHRSVTVLYVSTATGLIKKisVLPRT 425
Cdd:cd11242    334 SNDFPDDTLNFiKTHPLMDEAVPSIINRPWFTRTMVRYrlTQIAVDNAAGP-YQNYTVVFLGSEAGTVLK--FLARI 407
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
 60-423 6.85e-89

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: 294.05  E-value: 6.85e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   60 VGARDNLYRLTLTSLTDLE-----HASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGKS-LFTCGTYAFSPWCAWREI 133
Cdd:cd11267     23 IGDRDNLYRVELDPTAGTEmryhkKLTWRSNKNDINVCRMKGKHEGECRNFIKVLLLRDYGtLFVCGTNAFNPVCANYSI 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  134 ENITSVTSEMSGVAMCPYSP-HANVtALLSrgpSGGLFAGAPTDFSGADPAIYRTLA-SPNLRTRQYDSKWLNDPQFVGS 211
Cdd:cd11267    103 DTLEPVGDNISGMARCPYDPkHANV-ALFA---DGMLFTATVTDFLAIDAVIYRSLGdSPALRTVKHDSKWFKEPYFVHA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  212 FETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGG-QIMMKDVWTTFSKARLNCSLPGEFPFYYDEIQGAAYHPEE 290
Cdd:cd11267    179 VEWGSHVYFFFREIAMEFNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVSDILNL 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  291 G---IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNRQRCG---------SPSSTAPHQ 358
Cdd:cd11267    259 GgrpVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEELVPRPRPGccaapgmryNSSSTLPDE 338

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1984005256  359 IMD-NQRYQLMDEAVQSTMLEPLHTATLERF--IHIAVDvTPTKLHRSVTVLYVSTATGLIKKISVLP 423
Cdd:cd11267    339 VLNfVKTHPLMDEAVPSLGHAPWIVRTMTRYqlTHMVVD-TEAGPHGNHTVVFLGSTRGTVLKFLIIP 405
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
 38-465 3.60e-84

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: 280.84  E-value: 3.60e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHA--SWSAPEDKVNTCQNKGQSVE-DCRNYVKVLLS-NG 113
Cdd:cd11240      1 FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDISTELKDkiKWEASEDKKKECANKGKDNQtDCFNFIRILQFyNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  114 KSLFTCGTYAFSPWCAWREIENITSVTSEM-SGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPN 192
Cdd:cd11240     81 THLYVCGTFAFSPRCTYINLSDFSLSSIKFeDGKGRCPFDPAQRYTAIMV---DGELYSATVNNFLGSEPVISRNHSEGN 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  193 LRTRQYDSKWLNDPQFVGS----------FETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFS 262
Cdd:cd11240    158 VLKTENTLRWLNEPAFVGSahiresidspDGDDDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGGQRTLQKKWTTFL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  263 KARLNCSLPGEfPFYYDEIQGA----AYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWER- 337
Cdd:cd11240    238 KAQLVCSQPDS-GLPFNVLRDVfvlsPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRy 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  338 -------RP---VAHHNRQRCGSPSSTAPhqimDN-----QRYQLMDEAVQStMLEPLHTATLERFIHIAVDVTPTKLHR 402
Cdd:cd11240    317 tgpvpdpRPgacITNSARSQGITSSLNLP----DNvltfvKDHPLMDEQVHP-INRPLLVKSGVNYTRIAVHRVQALDGQ 391

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1984005256  403 SVTVLYVSTATG-LIKKISVLPRTQetcIVEIWGSLPSPPM--TLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd11240    392 TYTVLFLGTEDGfLHKAVSLDGGMH---IIEEIQLFDQPQPvkNLLLSSSKGVLYVGSSSGVVQVP 454
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
 53-465 7.41e-80

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


Pssm-ID: 200527 [Multi-domain]  Cd Length: 466  Bit Score: 269.21  E-value: 7.41e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   53 VARQQVVVGARDNLYRLTL-TSLTDLEHAS----WSAPEDKVNTCQNKGQSVEDCRNYVKVLLS-NGKSLFTCGTYAFSP 126
Cdd:cd11266     16 IMNRTLYIAARDHIYTVDIdTSHTEEIYFSkkltWKSRQADVDTCRMKGKHKDECHNFIKVLLKrNDDTLFVCGTNAFNP 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  127 WCAWREIENITSVTSEMSGVAMCPY-SPHANVtALLSrgpSGGLFAGAPTDFSGADPAIYRTLA-SPNLRTRQYDSKWLN 204
Cdd:cd11266     96 SCRNYKMDTLEFFGDEFSGMARCPYdAKHANV-ALFA---DGKLYSATVTDFLAIDAVIYRSLGdSPTLRTVKHDSKWLK 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  205 DPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGG-QIMMKDVWTTFSKARLNCSLPGEFPFYYDEIQG 283
Cdd:cd11266    172 EPYFVQAVDYGDYIYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQA 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  284 AA---YHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAW-----ERRPvahHNRQRCGSPSSTA 355
Cdd:cd11266    252 VTdviHINGRDVVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWtpvpdERVP---KPRPGCCAGSSSL 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  356 PHQIMDNQ----------RYQLMDEAVQSTMLEPLHTATLERF--IHIAVDVT--PTKLHrsvTVLYVSTATGLIKKIsv 421
Cdd:cd11266    329 EKYATSNEfpddtlnfikTHPLMDEAVPSIINRPWFLRTMVRYrlTKIAVDNAagPYQNH---TVVFLGSEKGIILKF-- 403

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1984005256  422 LPRT-------------------QETCIVEiwGSLPSPPMTLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd11266    404 LARTgnsgflndslfleemnvynSEKCSYD--GVEDKRIMGMQLDKASSALYVAFSTCVIKVP 464
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
 46-469 7.76e-78

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: 263.84  E-value: 7.76e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   46 YSQLLFDVARQQVVVGARDNLYRLTLTSLT-DLEHASWSAPEDKVNTCQNKGQSVE-DCRNYVKVLLS-NGKSLFTCGTY 122
Cdd:cd11239     10 YRSLLLDEDRDRLYVGGKDHILSLSLDNINqDPKKIYWPASPERIEECKMAGKDPNtECANFVRVLQPyNRTHLYACGTG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  123 AFSPWCAWREI-----ENITSVTSEM--SGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPN-LR 194
Cdd:cd11239     90 AFHPICAFINVgrrleDPIFKLDDSSleSGRGKCPFDPNQPFASVLI---DGELYSGTAIDFMGRDAAIFRSLGHRHyIR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  195 TRQYDSKWLNDPQFVGSF---ETEDH----VYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLN 267
Cdd:cd11239    167 TEQYDSRWLNEPKFVGAYlipDSDNPdddkVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLKARLV 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  268 CSLPGE--FPFYYDEIQGA----AYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWerrpVA 341
Cdd:cd11239    247 CSVPGPdgIDTYFDELEDVfllpTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQW----VE 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  342 HHNR---QRCGS-PSSTAPHQIMDNQRY-----------QLMDEAVQstmlePLH-------TATLERFIHIAVD-VTPT 398
Cdd:cd11239    323 YQGKvpyPRPGTcPSKTYGPLYKSTKDFpddvisfarshPLMYNPVY-----PLHgrpllirTNVPYRLTQIAVDrVEAE 397

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1984005256  399 KLHrsVTVLYVSTATGLIKKISVLPR----TQETCIVEIWGS-LPSPPMTLQFLKDTQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11239    398 DGQ--YDVLFIGTDSGTVLKVVSLPKenweMEEVILEELQVFkHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
 48-465 1.20e-76

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: 260.35  E-value: 1.20e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   48 QLLFDVaRQQVVVGARDNLYRLTL-----TSLTDLEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLL-SNGKSLFTCGT 121
Cdd:cd11269     12 QLMLKI-RDTLYIAGRDQVYTVNLnevpkTEVTPSRKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVpRNDEMVFVCGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  122 YAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPN-LRTRQYDS 200
Cdd:cd11269     91 NAFNPMCRYYRLSTLEYDGEEISGLARCPFDARQTNVALFA---DGKLYSATVADFLASDAVIYRSMGDGSaLRTIKYDS 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  201 KWLNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGG-QIMMKDVWTTFSKARLNCSLPGEFPFYYD 279
Cdd:cd11269    168 KWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFFYFD 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  280 EIQGAAYHPE-EGI--IYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAW-----ERRP------VAHHNR 345
Cdd:cd11269    248 VLQSITDIIEiNGIptVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWtavpeDKVPkprpgcCAKHGL 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  346 QRCGSPSSTAPHQIMDN-QRYQLMDEAVQSTMLEPLHTATLERF--IHIAVDVTPTKlHRSVTVLYVSTATGLIKKI--- 419
Cdd:cd11269    328 AEAYKTSIDFPDETLSFiKSHPLMDSAVPSIIEEPWFTKTRVRYrlTAIAVDHAAGP-HQNYTVIFVGSEAGVVLKIlak 406

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1984005256  420 --------SVLPR-----TQETCIVEiwGSLPSPPMTLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd11269    407 tspfslndSVLLEeieayNHAKCSAE--NEEDRRVISLQLDRDHHALFVAFSSCVVRIP 463
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
 38-465 9.17e-69

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: 238.22  E-value: 9.17e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHAS---WSAPEDKVNTCQNKGQSVE-DCRNYVKVLLS-N 112
Cdd:cd11257      2 FEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISPTGEQQeltWSADEEKKQECSFKGKDPQrDCQNYIKILLRlN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  113 GKSLFTCGTYAFSPWCAWREIENITSVTSEMSGVAM------CPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYR 186
Cdd:cd11257     82 STHLFTCGTYAFSPICTYIVMTNFSLERDEKGEPLLedgkgrCPFDPEYKSTAIMV---DGELYTGTVSNFQGNDPIIYR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  187 TLASPNLRTRQYDSKWLNDPQFVGS----------FETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKD 256
Cdd:cd11257    159 SLGSGTPLKTENSLNWLQDPAFVGSayiqeslpklVGDDDKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGGERVLQK 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  257 VWTTFSKARLNCSLPGE-FPFYYDE----IQGAAYHPEEGIIYATFTTPIN-GIAG-SAICAFNMSAVFASFNGPFKYQE 329
Cdd:cd11257    239 RWTTFLKAQLLCSLPDDgFPFNVLQdvfvLTPSPEDWKDTLFYGVFTSQWHkGTAGsSAVCVFTMDQVQRAFNGLYKEVN 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  330 NAGAAW--------ERRP---VAHHNRQRCGSPSSTAPHQIMDNQR-YQLMDEAVQSTMLEPLHTAtleRFIHIAVDVTP 397
Cdd:cd11257    319 RETQQWytythpvpEPRPgacITNSARERKINSSLHMPDRVLNFVKdHFLMDGQVRSQPLLLQPQV---RYTQIAVHRVK 395

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  398 TkLHRSVTVLYVSTATGLIKK-ISVLPRTQetcIVEIWGSLPSPPMTLQFLKDTQS--LYVGMEIGLLRIP 465
Cdd:cd11257    396 G-LHKTYDVLFLGTDDGRLHKaVSVGPMVH---IIEELQIFSEGQPVQNLLLDTHKglLYASSHSGVVQVP 462
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
 38-488 2.19e-68

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: 236.73  E-value: 2.19e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLT---SLTDLEHASWSAPEDKVNTCQNKGQSVE-DCRNYVKVLLS-N 112
Cdd:cd11256      2 FRQENVHNYDQLLLSPDETTLYVGARDNILALGIRtpgPIRLKHQIPWPANDSKISECAFKKKSNEtECFNFIRVLVPvN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  113 GKSLFTCGTYAFSPWCAWREIENITSVTSE-----MSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRT 187
Cdd:cd11256     82 GTHLYTCGTYAFSPACTYIELDHFSLPPPNgtiitMDGKGQSPFDPQHNYTAILV---DGELYTGTMNNFRGNEPIIFRN 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  188 LAS-PNLRTRQYdSKWLN-DPQFVGSF--ETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSK 263
Cdd:cd11256    159 LGTkVSLKTDGF-LRWLNaDAVFVASFnpQGDSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKWTTFLK 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  264 ARLNCSLPGEFPF--YYDEIQGAAYHPEEGIIYATFTT--PINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERR- 338
Cdd:cd11256    238 AQLTCSQQGHFPFnvIHHVALLNQPDPNNSVFYAVFTSqwQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYm 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  339 -PVAHHNRQRC-GSPSSTAPHQIMdnQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTVLYVSTATGLI 416
Cdd:cd11256    318 gPVSDPRPGSCsGGKSSDKALNFM--KDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSGHNYTVMFLGTDKGFL 395

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1984005256  417 KKiSVLPrtqetciveiwgslpsppmtlqflkDTQSLYVGMEIGLLRIPAVQCYRHRS-RQACLNAQEPYCGW 488
Cdd:cd11256    396 HK-AVLM-------------------------GGSESHIIEEIELLTPPEPVENLLLAaNEGVVYIGYSAGVW 442
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
 44-469 1.40e-67

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: 235.10  E-value: 1.40e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   44 TTYSQLLFDVARQQVVVGARDNLYRLTLTSLTD---LEHasWSAPEDKVNTC--QNKGQSVEdCRNYVKVLLS-NGKSLF 117
Cdd:cd11254      8 SDYRILLKDEDHDRMYVGSKDYVLSLDLHDINReplIIH--WPASPQRIEECilSGKGSNGE-CGNFIRLIQPwNRTHLY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCA-----WREIENITSVT--SEMSGVAMCPYSPHA-NVTALLSrgpsGGLFAGAPTDFSGADPAIYRTLA 189
Cdd:cd11254     85 VCGTGAYNPVCAyinrgRRAEDYMFRLEpdKLESGKGKCPYDPKQdSVSALIN----GELYAGVYIDFMGTDAAIFRTMG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  190 -SPNLRTRQYDSKWLNDPQFVG-------SFETEDHVYFLFRESAVEYINcGKKIYSRIARVCKNDRGGQIMMKDVWTTF 261
Cdd:cd11254    161 kQPAMRTDQYNSRWLNDPAFVHahlipdsSEKNDDKLYFFFREKSLEAPQ-SPAVLSRIGRVCLNDDGGHCCLVNKWSTF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  262 SKARLNCSLPGE--FPFYYDEIQGAAYHPEEG----IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAW 335
Cdd:cd11254    240 LKARLVCSVPGAdgIETHFDELRDVFIQPTQDtknpVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQW 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  336 ER--------RPVAHHNRQRCGSPSSTA--PHQIMDNQR-YQLMDEAVQSTMLEPL--HTATLERFIHIAVDVTPTKLHR 402
Cdd:cd11254    320 MPytgkipypRPGTCPGGTFTPSMKSTKdyPDEVINFMRtHPLMYNAVYPVHRRPLvvRTNVNYRFTTIAVDQVDAADGR 399

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1984005256  403 sVTVLYVSTATGLIKKISVLPR----TQETCI--VEIWgSLPSPPMTLQFLKDTQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11254    400 -YEVLFLGTDRGTVQKVIVLPKddleTEELTLeeVEVF-KVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
 56-465 3.85e-66

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: 230.77  E-value: 3.85e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   56 QQVVVGARDNLYRLTLTSLTDL----EHASWSAPEdkVNTCQNKGQSVEDCRNYVKVLL-SNGKSLFTCGTYAFSPWCAW 130
Cdd:cd11270     19 HMVYIAARDHVFAINLSASLERivpqQKLTWKTKD--VEKCTVRGKNSDECYNYIKVLVpRNDETLFACGTNAFNPTCRN 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  131 REIENITSVTSEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLA--SPNLRTRQYDSKWLNDPQF 208
Cdd:cd11270     97 YKMSSLEQDGEEVIGQARCPFESRQSNVGLFA---GGDFYSATMTDFLASDAVIYRSLGesSPVLRTVKYDSKWLREPHF 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  209 VGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQI-MMKDVWTTFSKARLNCSLPGEFPFYYDEIQGAA-- 285
Cdd:cd11270    174 LHAIEYGNYVYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSPrVLERYWTSFLKARLNCSVPGDSFFYFDVLQSLTnv 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  286 --YHPEEGIIyATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRP-----------VAHHNRQRCGSPS 352
Cdd:cd11270    254 mqINHRPAVL-GVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVPdeavpkprpgsCAGDGPAAGYKSS 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  353 STAPHQIMDN-QRYQLMDEAVQSTMLEPLHTATLERF--IHIAVDvTPTKLHRSVTVLYVSTATGliKKISVLPRTQETC 429
Cdd:cd11270    333 TNFPDETLTFiKSYPLMDEAVPSVNNRPCFTRTTSRFklTQIAVD-TAAGPYKNYTVVFLGSENG--HVLKVLASMHPNS 409

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  430 IVEIWG----SLPSPP-----------MTLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd11270    410 SYSTQVlediDVYNPNkcnvrgedrriLGLELDKDHHALFVAFTGCVIRVP 460
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
 27-469 7.04e-65

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: 227.96  E-value: 7.04e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   27 ISYEDLAETS-MFRQEGV---TTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSV-ED 101
Cdd:cd11249      9 LSYKEMLESNnLITFNGLansSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKWAGKDIlKE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  102 CRNYVKVLLS-NGKSLFTCGTYAFSPWCAWREI-----ENITSVTSEM--SGVAMCPYSPHANVTALLSrgpSGGLFAGA 173
Cdd:cd11249     89 CANFIKVLKAyNQTHLYACGTGAFHPVCTYIEVghhpeDNIFRLEDSHfeNGRGKSPYDPKLLTASLLI---DGELYSGT 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  174 PTDFSGADPAIYRTLASPN-LRTRQYDSKWLNDPQFVGSF-------ETEDHVYFLFRESAVEYINCGKKIYSRIARVCK 245
Cdd:cd11249    166 AADFMGRDFAIFRTLGHHHpIRTEQHDSRWLNDPRFISAHlipesdnPEDDKIYFFFRENAIDGEHTGKATHARIGQLCK 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  246 NDRGGQIMMKDVWTTFSKARLNCSLPGE--FPFYYDEIQGA----AYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFA 319
Cdd:cd11249    246 NDFGGHRSLVNKWTTFLKARLICSVPGPngIDTHFDELQDVflmnSKDPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIRR 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  320 SFNGPFKYQENAGAAWerrpVAHHNRQRCGSPsSTAPHQIMD--NQRYQLMDEAV-----QSTMLEP----------LHT 382
Cdd:cd11249    326 VFLGPYAHRDGPNYQW----VPFQGRVPYPRP-GTCPSKTFGgfDSTKDLPDDVItfarsHPAMYNPvfpinnrpiiIKT 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  383 ATLERFIHIAVDVTPTKlHRSVTVLYVSTATGLIKKISVLPRtqetcivEIWGSL-------------PSPPMTLQFLKD 449
Cdd:cd11249    401 DVDYQFTQIVVDRVEAE-DGQYDVMFIGTDMGTVLKVVSIPK-------ETWHDLeevlleemtvfrePTAISAMELSTK 472

                          490       500
                   ....*....|....*....|
gi 1984005256  450 TQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11249    473 QQQLYIGSAIGVSQLPLHRC 492
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
 38-469 3.18e-64

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: 225.56  E-value: 3.18e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHA-SWSAPEDKVNTCQNKGQSVE-DCRNYVKVL-LSNGK 114
Cdd:cd11250      2 FDLERSCCYDALLLDEERGRLFVGAKNYLASLSLDNISKQEKKiYWPAPVEWREECNWAGKDINtDCMNYVKILhHYNRT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  115 SLFTCGTYAFSPWCAWREIENITSVT-------SEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRT 187
Cdd:cd11250     82 HLYACGTGAFHPTCAFVEVGQRMEDHvfrldpsRVEDGKGKSPYDPRHTAASVLV---GDELYSGVATDLMGRDFTIFRS 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  188 LAS-PNLRTRQYDSKWLNDPQFVGSF---ETE----DHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWT 259
Cdd:cd11250    159 LGQrPSLRTEQHDSRWLNEPKFVKVFwipESEnpddDKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGGQRSLVNKWT 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  260 TFSKARLNCSLPGE--FPFYYDEIQGAAYHPEEG----IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGA 333
Cdd:cd11250    239 TFLKARLVCSVPGNegGDTHFDELRDVFLLQTRDkrnpLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNY 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  334 AWerrpVAHHNR-----------QRCGSPSSTA--PHQIMDNQR-YQLMDEAVQSTMLEP--LHTATLERFIHIAVD-VT 396
Cdd:cd11250    319 QW----VSYQGKvpyprpgmcpsKTFGSFESTKdfPDDVIQFARnHPLMFNPVLPLGGRPlfLRTGIPYTFTQIAVDrVA 394

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1984005256  397 PTKLHRSvtVLYVSTATGLIKKISVLPR----TQETCIVEIWGSL--PSPPMTLQFLKDTQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11250    395 AADGHYD--VMFIGTDVGSVLKVISVPKgswpSNEELLLEELHVFkdSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
 49-469 1.80e-61

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: 217.80  E-value: 1.80e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   49 LLFDVARQQVVVGARDNLYRLTLTSLTD-LEHASWSAPEDKVNTCQNKGQSVEDCRNYVKVLLS-NGKSLFTCGTYAFSP 126
Cdd:cd11253     13 MLLDEYQERLFVGGRDLLYSLSLERISAnYKEIHWPSTQLQVEDCIMKGRDKPECANYIRVLHHyNRTHLLACGTGAFDP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  127 WCAW----REIEN----ITSVTSEmSGVAMCPYSPHANVTALLSRGPsggLFAGAPTDFSGADPAIYRTLAS-PNLRTRQ 197
Cdd:cd11253     93 VCAFirvgRGSEDhlfqLESDKFE-RGRGRCPFDPNSSFISTLIGGE---LFVGLYSDYWGRDAAIFRTMNHlAHIRTEH 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  198 YDSKWLNDPQFVGSF---ETEDH----VYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSL 270
Cdd:cd11253    169 DDERLLKEPKFVGSYmipDNEDPddnkVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLICSV 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  271 PGE--FPFYYDEIQGAAYHPEEG----IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWE-------- 336
Cdd:cd11253    249 PGPngIDTHFDELEDVFLLRTRDnknpEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSvyegkvpy 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  337 RRPVAHHNRQRCGSPSSTA--PHQIMDNQR-YQLMDEAVQSTMLEP--LHTATLERFIHIAVDVTPTKlHRSVTVLYVST 411
Cdd:cd11253    329 PRPGSCASKVNGGHYGTTKdyPDEALRFARsHPLMYQAVKPVHKRPilVKTDGKYNLKQIAVDRVEAE-DGQYDVLFIGT 407

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1984005256  412 ATGLIKKISVLpRTQETCIVE--IWGSL-----PSPPMTLQFLKDTQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11253    408 DNGIVLKVITI-YNQETETMEevILEELqvfkvPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
 51-423 3.25e-61

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: 216.88  E-value: 3.25e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   51 FDVARQQVVVGARDNLYRLTLTSLTDLE------HASWSAPEdkVNTCQNKGQSVEDCRNYVKVLLS-NGKSLFTCGTYA 123
Cdd:cd11268     14 FLTLNRTLLVAARDHVFSFDLQAEEEGEglvpnkYLTWRSQD--VENCAVRGKLTDECYNYIRVLVPwDSQTLLACGTNS 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  124 FSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSRGpsgGLFAGAPTDFSGADPAIYRTLA-SPNLRTRQYDSKW 202
Cdd:cd11268     92 FSPVCRSYGITSLQQEGEELSGQARCPFDATQSNVAIFAEG---SLYSATAADFQASDAVVYRSLGpQPPLRSAKYDSKW 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  203 LNDPQFVGSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDV-WTTFSKARLNCSLPGEFPFYYDEI 281
Cdd:cd11268    169 LREPHFVQALEHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSPRALDRhWTSFLKLRLNCSVPGDSTFYFDVL 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  282 Q---GAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWErrPVAHHN--RQRCGSPSSTAP 356
Cdd:cd11268    249 QaltGPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWT--PVSEDRvpSPRPGSCAGVGG 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  357 HQIMDNQR------------YQLMDEAVQSTMLEPLHTATLERFI-HIAVDVTPTKlHRSVTVLYVSTATGLIKKisVLP 423
Cdd:cd11268    327 AALFSSSRdlpddvltfikaHPLLDPAVPPVTHQPLLTLTSRALLtQVAVDGMAGP-HSNITVMFLGSNDGTVLK--VLP 403
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
 46-465 4.74e-61

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: 216.17  E-value: 4.74e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   46 YSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHAS--WSAPEDKVNTCQNKGQSVE-DCRNYVKVLLS-NGKSLFTCGT 121
Cdd:cd11262     10 YSTLLLEDESGRLYVGARGAIFSLNASDISDSSALTidWEASPEQKHQCLKKGKNNQtECFNHVRFLQRfNSTHLYTCGT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  122 YAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGAdPAIYRTLASPNLRTRQYDSK 201
Cdd:cd11262     90 HAFRPLCAYIDAERFTLSSQFEEGKEKCPYDPAKGYTGLIV---DGQLYTASQYEFRSF-PDIRRNSPQPTLRTEEAPTR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  202 WLNDPQFVGSF---ET-------EDHVYFLFRESAVE---YINCGKkiYSRIARVCKNDRGGQIMMKDVWTTFSKARLNC 268
Cdd:cd11262    166 WLNDADFVGSVlvrESmnssvgdDDKIYFFFTERSQEetaYFSQSR--VARVARVCKGDRGGKKTLQRKWTSFLKARLVC 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  269 SLPgefpfYYDEIQGA--------AYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPF--------KYQENAG 332
Cdd:cd11262    244 YIP-----EYEFLFNVlrsvfvlwGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYmeyqdsssKWSRYTG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  333 AAWERRP---VAHHNRQRCGSPSSTAPHQIMD-NQRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTVLY 408
Cdd:cd11262    319 KVPEPRPgscITDEHRSQGINSSQDLPDNVLDfVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDGRVYDVLF 398

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  409 VSTATGLIKK----ISVLPRTQETCIVEiwgsLPSPPMTLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd11262    399 LGTDEGWLHKavviGSAVHIIEELQVFR----EPQPVENLVISKKQNSLYVGARSGVVQVP 455
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
 46-469 4.77e-58

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: 207.82  E-value: 4.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   46 YSQLLFDVARQQVVVGARDNLYRLTLTSLT-DLEHASWSAPEDKVNTCQNKGQS-VEDCRNYVKVLLS-NGKSLFTCGTY 122
Cdd:cd11251     10 YRILFMDEDQDRIYVGSKDHILSLNINNISqDALSIFWPASASKVEECKMAGKDpTHGCGNFVRVIQPyNRTHLYVCGSG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  123 AFSPWCAW-----REIENITSVTSEM-SGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPN-LRT 195
Cdd:cd11251     90 AFSPVCVYvnrgrRSEEQVFHIDSKAeSGKGRCSFNPNVNTVSVMI---NEELFSGMYIDFMGTDAAIFRSLTKRNaVRT 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  196 RQYDSKWLNDPQFV-------GSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNC 268
Cdd:cd11251    167 DQHNSKWLSEPIFVdahlipdGTDPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKARLVC 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  269 SLPGE--FPFYYDEIQGA----AYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWerrpVAH 342
Cdd:cd11251    247 SVMDEdgTETHFDELEDVflleTDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQL----IAY 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  343 HNR---QRCG-------SPSSTAPHQIMDN-----QRYQLMDEAVQSTMLEPL--HTATLERFIHIAVDVTPTKlHRSVT 405
Cdd:cd11251    323 QGRipyPRPGtcpggafTPNMQSTKEFPDDvvtfiRNHPLMFNPIYPIGRRPLlvRTGTDYKYTKIAVDRVNAA-DGRYH 401

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  406 VLYVSTATGLIKKISVLPR----TQETCI--VEIWGSlPSPPMTLQFLKDTQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11251    402 VLFLGTDKGTVQKVVVLPTngslSGELILeeLEVFKN-HAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
 46-469 2.80e-57

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: 205.91  E-value: 2.80e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   46 YSQLLFDVARQQVVVGARDNLYRLTLTSLT-DLEHASWSAPEDKVNTCQNKGQSVE-DCRNYVKVLLSNGKS-LFTCGTY 122
Cdd:cd11252     10 FQTLLLDEERGRLLLGAKDHIYLLDLVDLNkNPKKIYWPAAKERVELCKLAGKDANtECANFIRVLHPYNRThVYVCGTG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  123 AFSPWCAWREI-----ENITSVTSEM--SGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPN--- 192
Cdd:cd11252     90 AFHPTCGYIELgthkeDRIFLLDTQNleSGRLKCPFDPQQPFASVMT---DEYLYAGTASDFLGKDTTFTRSLGPTPdhh 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  193 -LRTRQYDSKWLNDPQFVGSFET-------EDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKA 264
Cdd:cd11252    167 yIRTDISEHYWLNGAKFIGTFPIpdtynpdDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKWTTFLKA 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  265 RLNCSLPGE--FPFYYDEIQGAAYHPEEG----IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWerr 338
Cdd:cd11252    247 RLVCSIPGPdgADTHFDELQDIFLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRW--- 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  339 pVAHHNR---QRCGS-PSSTA----------PHQIMD-NQRYQLMDEAVQSTMLEPLHTA--TLERFIHIAVDVTPTKlH 401
Cdd:cd11252    324 -VQYEGRipyPRPGTcPSKTYdplikstkdfPDEVISfIKRHPLMYKSVYPLTGGPVFTRinVDYRLTQIVVDHVAAE-D 401

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1984005256  402 RSVTVLYVSTATGLIKKISVLPR---TQETCIVE---IWGSlPSPPMTLQFLKDTQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11252    402 GQYDVMFLGTDIGTVLKVVSITKekwTMEEVVLEelqIFKH-PSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
 38-465 2.89e-56

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: 202.78  E-value: 2.89e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEH-ASWSAPEDKVNTCQNKGQSVE-DCRNYVKVLLS-NGK 114
Cdd:cd11259     12 FHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNALNISEKQHeLYWKVSEDKRTKCAVKGKSKQtECRNYIRVLQPlNDT 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  115 SLFTCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPNLR 194
Cdd:cd11259     92 FLYVCGTNAFQPTCDYLNLTSFRLLGKNEDGKGRCPFDPAQSYTSVMV---DGELYSGTSYNFLGSEPIISRNSSQSPLR 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  195 TrQYDSKWLNDPQFV---------GSFETED-HVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKA 264
Cdd:cd11259    169 T-EYAIPWLNEPSFVfadviradpDSPDGEDdKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKA 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  265 RLNCSLPGE---FPFYYDEIQGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPfKYQ-----ENAGAAWE 336
Cdd:cd11259    248 RLICSIPDKnlvFNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSKG-KYMqsatvEQSHTKWV 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  337 R--------RPVA---HHNRQRCGSPSSTAPHQIMDNQR-YQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSV 404
Cdd:cd11259    327 RyngevpkpRPGAcinNEARAANYTSSLNLPDKTLQFVKdHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDGTIY 406

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1984005256  405 TVLYVSTATGLIKKISVLprTQETCIVEIWGSLP-SPPMTLQFLKDTQS---LYVGMEIGLLRIP 465
Cdd:cd11259    407 DVMFISTDRGALHKAISL--ENEVHIIEETQLFPdFEPVQTLLLSSKKGrrfLYAGSNSGVVQSP 469
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
 38-465 7.73e-56

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: 201.18  E-value: 7.73e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHASWSAPEDKVNTCQNKGQSVE-DCRNYVKVLLS-NGKS 115
Cdd:cd11258      4 FSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQtECFNYIRFLQPyNQSH 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  116 LFTCGTYAFSPWCAWREIENITSVTSEMS-GVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPNLR 194
Cdd:cd11258     84 LYTCGTYAFQPKCAYINMLTFTLDRAEFEdGKGKCPYDPAKGHTGLIV---DGELYSATLNNFLGTEPVILRNLGQHYSM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  195 TRQYDSKWLNDPQFVGS-FETE---------DHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKA 264
Cdd:cd11258    161 KTEYLAFWLNEPHFVGSaFVPEsvgsftgddDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKA 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  265 RLNCSLPgEFPFYYDEIQGA----AYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWER--- 337
Cdd:cd11258    241 RLLCSIP-EWQLYFNQLKAVftleGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRytd 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  338 -----RPVAH-HNRQRCGSPSSTapHQIMDN-----QRYQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTV 406
Cdd:cd11258    320 pvpspRPGSCiNNWHRDHGYTSS--LELPDNtlnfvKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDGETYSV 397

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  407 LYVSTATGLIKKISVLPRTQETCiVEIWGSLPSPPMTLQFLKDTQ-SLYVGMEIGLLRIP 465
Cdd:cd11258    398 LFIGTLDGWLIKAVSLGSWVHMI-EELQVFDQEPPESLVVSQSSKkLLFAGSRSELLQLP 456
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
 38-465 8.83e-52

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: 189.35  E-value: 8.83e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTdLEHAS--WSAPEDKVNTCQNKGQSVE-DCRNYVKVLLSNGK 114
Cdd:cd11260      1 FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDIS-VKRAKvlWEVTEEKQKDCTNKGKHADiDCHNYIRILHKMND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  115 S-LFTCGTYAFSPWCAWREIEN--ITSVTSEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTlASP 191
Cdd:cd11260     80 SrMYVCGTNAFSPTCDYISYDDgqLTLEGKQEDGKGKCPFDPFQRYSSVMV---DQDLYSATSMNFLGSEPVIMRS-SPI 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  192 NLRTrQYDSKWLNDPQFVG------SFETE----DHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTF 261
Cdd:cd11260    156 TIRT-EFKSSWLNEPNFIYmaavpeSEDSPegddDKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQKKWTSF 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  262 SKARLNCSLP-GEFPFYYDEiqgaAYHPEEG-----IIYATFTTPINGIAGSAICAFN---MSAVFA--SFNGPF----- 325
Cdd:cd11260    235 LKARLDCSVPePSLPYVIQD----VFHVCHQdwrkcVFYAVFTSQSDSSQSSAVCAYNvtdISNVFSrgKFKTPVavets 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  326 --KYQENAGAAWERRP---VAHHNRQRCGSPSSTAPHQIMDNQRYQ-LMDEAVQSTMLEPLHTATLERFIHIAVDVTPTK 399
Cdd:cd11260    311 fvKWVMYSGELPVPRPgacINNAARTSGIKKSLNLPDKTLQFVKDKpLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAA 390

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1984005256  400 LHRSVTVLYVSTATGLIKKiSVLPRTQETCIVEIwgSLPSPPMTLQFLKDTQ-SLYVGMEIGLLRIP 465
Cdd:cd11260    391 DGQSYPVMFIGTANGYVLK-AVNYDGEMHIIEEV--QLFEPEEPIDILRLSQnQLYAGSASGVVQMP 454
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
 38-418 2.84e-51

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: 187.78  E-value: 2.84e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   38 FRQEGVTTYSQLLFDVARQQVVVGARDNLYRLTLTSLTDL-EHASWSAPEDKVNTCQNKGQSVEDCRNYVKVL-LSNGKS 115
Cdd:cd11261      6 FSAPHTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERpRRIDWMVPEAHRQNCRKKGKKEAECHNFIRILaIANASH 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  116 LFTCGTYAFSPWCAWREIENITSVTSEMSGVAMCPYSPHANVTALLSrgpSGGLFAGAPTDFSGADPAIYRTLASPNLRT 195
Cdd:cd11261     86 LLTCGTFAFDPKCGVIDVSSFQQVERLESGRGKCPFEPAQRSAAIMA---GGVLYAATVKNFLGTEPIISRAVGRAEEWI 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  196 R-QYDSKWLNDPQFV----------GSFETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKA 264
Cdd:cd11261    163 RtETLPSWLNAPAFVaavflspaewGDEDGDDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLKA 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  265 RLNCSLPGEFPFYYDEIQGAAYHPEEG----IIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWER--- 337
Cdd:cd11261    243 DLLCPGPEHGRASSILQDVTTLRPLPGagtpIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGLPvmd 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  338 ------RP---VAHHNRQRCGSPSSTAPHQIMDNQR-YQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTKLHRSVTVL 407
Cdd:cd11261    323 sdvpqpRPgecITNNMKLLGFGSSLSLPDRVLTFVRdHPLMDRPVFPADGHPLLVTTDTAYLRVAAHRVTSLSGKEYDVL 402

                          410
                   ....*....|.
gi 1984005256  408 YVSTATGLIKK 418
Cdd:cd11261    403 YLGTEDGHLHR 413
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
 45-465 1.00e-49

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: 181.25  E-value: 1.00e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   45 TYSQLLFDVARQQVVVGARDNLYRLTLTSLTDLEHAS-----WSAPEDKVNTCQNKGQSVEDCRNYVKVLLSNGK--SLF 117
Cdd:cd09295      1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLSCIspelnFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGDldILA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWC-AWR-EIENITSVTSEMSGVAMCPYSPHANVTALLSRGPsggLFAGAPTDF-SGADPAIYRTLA-SPNL 193
Cdd:cd09295     81 VCGSNAAQPSCgSYRlDVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSK---LYSATDHDFkDGDRPALSRRSSnVHYL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  194 RTRQYDSKWLNDPQFVGSF---ETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQIMMKDVWTTFSKARLNCSL 270
Cdd:cd09295    158 RIVVDSSTGLDEITFVYAFvsgDDDDEVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSR 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  271 PG---EFPFYYDEIqGAAYHPEEGIIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENagaawerRPVAHHNRQR 347
Cdd:cd09295    238 PQsgfAFNLLQDAT-GDTKNLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVFDDPVEAINN-------RPLYAHQNQR 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  348 cgspsstaphqimdnqryqlmdeavqstmleplhtatlERFIHIAVDVTPTKLHRSvTVLYVSTATG-LIKKISVLPRTQ 426
Cdd:cd09295    310 --------------------------------------SRLTSIAVDATKQKSVGY-QVVFLGLKLGsLGKALAFFFLYK 350

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1984005256  427 ETCIVEIWGSLP-SPPMTLQFLKDTQSLYVGMEIGLLRIP 465
Cdd:cd09295    351 GHIIEEWKVFKDsSRITNLDLSRPPLYLYVGSESGVLGVP 390
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
 41-469 5.83e-49

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: 181.65  E-value: 5.83e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   41 EGVTTYSQLLFDVARQQVVVGARDNLYRLTL-TSLTDLEHASWSAPEDKVNTCQNKGQS-VEDCRNYVKVLLS-NGKSLF 117
Cdd:cd11255      5 HGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLdQTHPDAKEIHWPPLPGQREECIRKGKDpETECANFVRVLQPfNRTHLL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  118 TCGTYAFSPWCAWREI----ENITSV--TSEMSGVAMCPYSPHanvTALLSRGPSGGLFAGAPTDFSGADPAIYRTLAS- 190
Cdd:cd11255     85 ACGTGAFQPVCALINVghrgEHVFSLdpTTVESGRGRCPHEPK---RPFASTFTGGELYTGLTADFLGRDSVIFRGFGTr 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  191 PNLRTrQYDSKWLNDPQFVGSF-------ETEDHVYFLFRESAVEY-INCGKKIYSRIARVCKNDRGGQIMMKDVWTTFS 262
Cdd:cd11255    162 SPLRT-ETDQRLLHEPRFVAAHlipdnadRDNDKVYFFFTERATETaEDDDGAIHSRVGRLCANDAGGQRVLVNKWSTFI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  263 KARLNCSLPGE--FPFYYDEIQG-------AAYHPEegiIYATFTTPINGIAGSAICAFNMSAVFASFNGPFKYQENAGA 333
Cdd:cd11255    241 KARLVCSVPGPhgIQTHFDQLEDvfllrtkDGKSPE---IYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDH 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  334 AWER--------RP-------VAHHNRQRcgSPSSTAPHQIMDNQR-YQLMDEAVQSTMLEP--LHTATLERFIHIAVDV 395
Cdd:cd11255    318 QWGPyegkvpypRPgvcpskiTAQPGRAF--RSTKDYPDEVLQFARaHPLMWRPVYPSHRRPvlVKTGLPYRLTQIVVDR 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  396 TPTKlHRSVTVLYVSTATGLIKKISVLPR-----TQETCIVEIW-GSLPSPPMTLQFLKDTQSLYVGMEIGLLRIPAVQC 469
Cdd:cd11255    396 VEAE-DGYYDVMFIGTDSGSVLKVIVLQKgnsaaGEEVTLEELQvFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
 57-465 1.59e-32

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: 131.51  E-value: 1.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   57 QVVVGARDNLYRLTLTSltdlEHASWSAPEDKVN--TCQNKGqSVEDCRNYVKVLLSNGKSLFTCGTYAFSPWCaWREIE 134
Cdd:cd11243     15 SVYVGGQGALYLLDFTG----SAVIVKKIPDEKTekDCKKRA-TLDDCENYITLIKKLDYRLLVCGTNAGSPKC-WFLVN 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  135 NITSVTSEMSGVAmcPYSPHANVTALLSrgpsgglfagaptdfsgaDPAIYRTLASPN---LRTRQYDSK--------WL 203
Cdd:cd11243     89 QTLVTLSADRGVA--PFLPDENSLVLIE------------------GNNVYSTISGKKgniPRFRRYGGKkelytsdtVM 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  204 NDPQFVGSF------ETEDHVYFLFRESAVEYINCGKKIYSRIARVCKNDRGGQ-IMMKDVWTTFSKARLNCSLPGEfPF 276
Cdd:cd11243    149 QKPQFVKATllpedeQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTsSLSTSKWSTFLKARLVCGDPAT-PM 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  277 YYDEIQGAAYHP----EEGIIYATFTTPINgiaGSAICAFNMSAVFASFNGPfKYQENAGAAWERRPvahhnrQRCGSPS 352
Cdd:cd11243    228 NFNRLQDVFLLPkeewREAVVYGVFSNTWG---SSAVCSYSLGDIDKVFRTS-SLKGYSGSLPNPRP------GTCVPPE 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  353 STAPH---QIMDnqRYQLMDEAVQStmLEPLHTATLE---RFIHIAVDVTPTKLHRSVTVLYVSTATGLIKKIsVLPRTQ 426
Cdd:cd11243    298 QTHPSetfSFAD--EHPELDDRIEP--DEPRKLPVFQnkdHYQKVVVDEVRASDGVSYDVLYLATDKGKIHKV-VESKGQ 372

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1984005256  427 ETCIVEIWGSLPSPPMTLQFLKDTQS-LYVGMEIGLLRIP 465
Cdd:cd11243    373 THNIMEIQPFKEQEPIQSMILDAERShLYVGTKAEVTRLP 412
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
 292-440 3.16e-31

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: 120.84  E-value: 3.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  292 IIYATFTTPI-NGIAGSAICAFNMSAVFASFNGPFKYQENAGAAWERRPVAHHNrQRCGS-PSSTAPHQIMDN-----QR 364
Cdd:pfam01403   18 VLYGVFTTQWsNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPY-PRPGTcINDPLRLDLPDSvlnfvKD 96

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1984005256  365 YQLMDEAVQSTMLEPLHTATLERFIHIAVDVTPTkLHRSVTVLYVSTATGLIKKIsVLPRTQETCIVEIWGSLPSP 440
Cdd:pfam01403   97 HPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQA-LDGNYTVLFLGTDDGRLHKV-VLVGSEESHIIEEIQVFPEP 170
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 666-717 1.56e-13

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: 66.07  E-value: 1.56e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256   666 WSTWGPWHACSKPCNGGIRVRKRTCDSPSSKKGGAECPGCDQQIEECNAHEC 717
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 854-900 1.86e-12

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: 62.99  E-value: 1.86e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1984005256   854 WSCWTDWSECSASCGIGVRTRTRECLGP------ESCSGPRSIRETCEMPSCE 900
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPppqnggGPCTGEDVETRACNEQPCP 53
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
 49-455 3.22e-11

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: 66.59  E-value: 3.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   49 LLFDVARQQVVVGARDNLYRLTlTSLTDLEHASwSAPEDKVNTCQNKGQSVEDCR-----NYVKVLLSN--GKSLFTCGT 121
Cdd:cd11236      5 LAVDNSTGRVYVGAVNRLYQLD-SSLLLEAEVS-TGPVLDSPLCLPPGCCSCDHPrsptdNYNKILLIDysSGRLITCGS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  122 YaFSPWCAWREIENItSVTSEMSGVAMCPYSPHANVTALLSRGPSGG---LFAGAPTDFSGAD---PAI-------YRTL 188
Cdd:cd11236     83 L-YQGVCQLRNLSNI-SVVVERSSTPVAANDPNASTVGFVGPGPYNNenvLYVGATYTNNGYRdyrPAVssrslppDDDF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  189 ASPNLRTRQY-DSKWLNDPQF----VGSFETEDHVYFLFREsaVEYINCGKKIYSRIARVCKNDRGgqimmkdvWTTFSK 263
Cdd:cd11236    161 NAGSLTGGSAiSIDDEYRDRYsikyVYGFSSGGFSYFVTVQ--RKSVDDESPYISRLVRVCQSDSN--------YYSYTE 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  264 ARLNCSlpGEFPFYYDEIQgAAY--------------HPEEGIIYATFT---TPINGIAG-SAICAFNMSAVFASFngpf 325
Cdd:cd11236    231 VPLQCT--GGDGTNYNLLQ-AAYvgkagsdlarslgiSTDDDVLFGVFSkskGPSAEPSSkSALCVFSMKDIEAAF---- 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  326 kyqenagaaWERRPVahhnrqrcGSPSSTAPHQIMDNQRYqlmdeavqstmleplhTAtlerfihIAVDVTptklhRSVT 405
Cdd:cd11236    304 ---------NDNCPL--------GGGVPITTSAVLSDSLL----------------TS-------VAVTTT-----RNHT 338

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1984005256  406 VLYVSTATGLIKKISVLPRTQ----ETCIVEIwGSLPSPPMtlQFLKDTQSLYV 455
Cdd:cd11236    339 VAFLGTSDGQLKKVVLESSSSatqyETLLVDS-GSPILPDM--VFDPDGEHLYV 389
TSP_1 pfam00090
Thrombospondin type 1 domain;
667-717 3.56e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 58.97  E-value: 3.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  667 STWGPWHACSKPCNGGIRVRKRTCDSPssKKGGAECPGCDQQIEECNAHEC 717
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSP--FPGGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 599-645 4.34e-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: 59.14  E-value: 4.34e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1984005256   599 WTAWSAWSACSQTCGFAMKTRRRTCTNPAPAFGGRVCVGHDHDDIMC 645
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 796-841 4.62e-10

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: 56.06  E-value: 4.62e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256   796 WGEWSSWGICDRPCGRGSQHRVRQCESPPCEN------GLTKQSRVCNPHPC 841
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNgggpctGEDVETRACNEQPC 52
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
 44-468 1.13e-09

The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor of Sema4C and Sema4G. By signaling the effect of Sema4C and Sema4G, the plexin B2 receptor plays important roles in neural tube closure and cerebellar granule cell development. Mice lacking Plexin B2 demonstrated defects in closure of the neural tube and disorganization of the embryonic brain. In developing kidney, Sema4C-Plexin B2 signaling modulates ureteric branching. Plexin B2 is expressed both in the pretubular aggregates and the ureteric epithelium in the developing kidney. Deletion of Plexin B2 results in renal hypoplasia and occasional double ureters. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 62.10  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   44 TTYSQLLFDVARQQVVVGARDNLYRLTlTSLTDLEHASwSAPEDKVNTC-----QNKGQSVEDCRNYVKVLLSN--GKSL 116
Cdd:cd11276      6 TELNHLVVDPQTGRVYLGAVNALYQLD-ADLQLESRVE-TGPKKDNKKCtppieENQCTEAKMTDNYNKLLLLDsaNKTL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  117 FTCGTYaFSPWCAWREIENITSVT--SEMSGVAMCPYSPHANVT-----ALLSRGPSGGLFAG---APTD---------- 176
Cdd:cd11276     84 VVCGSL-FKGICSLRNLSNISEVIyySDTSGEKSFVASNDEGVStvgliSSLKPGNDRVFFVGkgnGSNDngkiistrll 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  177 FSGADPAIYRTLASPNLRTRQYDSKWLNdpQFVGSFETEDHVYFLFRESaveyINCGKKIYSRIARVCKNDRGgqimmkd 256
Cdd:cd11276    163 QNYDDREVFENYIDAATVKSAYVSRYTQ--QFRYAFEDNNYVYFLFNQQ----LGHPDKNRTLIARLCENDHH------- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  257 vWTTFSKARLNCSLPGEfpfYYDEIQgAAYHPEEG---------------IIYATFTTPINGIAGSAICAFNMSAVFAsf 321
Cdd:cd11276    230 -YYSYTEMDLNCRDGAN---AYNKCQ-AAYVSTPGkelaqnygnsilsdkVLFAVFSRDEKDSGESALCMFPLKSINA-- 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  322 ngpfKYQENAGAAW----ERRPVAhHNRQRCGSPSSTAPHQIMDNQRYQLMDEAVQSTM--------LEPLHTAtlERFI 389
Cdd:cd11276    303 ----KMEANREACYtgtiDDRDVF-YKPFHSQKDIICGSHQQKNSKSFPCGSEHLPYPLgsrdelalTAPVLQR--GGLN 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  390 HIAVDVTPTKLHrsvTVLYVSTATGLIKKISVLPRTQEtciveiWGSLP---SPPMT--LQFLKDTQSLYVGMEIGLLRI 464
Cdd:cd11276    376 LTAVTVAVENGH---TVAFLGTSDGRILKVHLSPDPEE------YNSILiekNKPVNkdLVLDKTLEHLYIMTEDKVFRL 446


                   ....
gi 1984005256  465 PaVQ 468
Cdd:cd11276    447 P-VQ 449
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 797-841 1.29e-08

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: 51.90  E-value: 1.29e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1984005256  797 GEWSSWGICDRPCGRGSQHRVRQCESPPCENG----LTKQSRVCNPHPC 841
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGrpcpELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
855-899 5.99e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 5.99e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1984005256  855 SCWTDWSECSASCGIGVRTRTREC----LGPESCSGPRSIRETCEMPSC 899
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 667-717 1.23e-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: 49.20  E-value: 1.23e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  667 STWGPWHACSKPCNGGIRVRKRTCDSPSSkKGGAECPGcDQQIEECNAHEC 717
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQ-NGGRPCPE-LLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 857-899 3.69e-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: 3.69e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1984005256  857 WTDWSECSASCGIGVRTRTRECLGPESCSG----PRSIRETCEMPSC 899
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVEPQNGGrpcpELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 600-635 2.33e-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: 45.35  E-value: 2.33e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1984005256  600 TAWSAWSACSQTCGFAMKTRRRTCTNPaPAFGGRVC 635
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC 38
TSP_1 pfam00090
Thrombospondin type 1 domain;
600-645 7.11e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 43.95  E-value: 7.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1984005256  600 TAWSAWSACSQTCGFAMKTRRRTCTNPAPafGGRVCVGHDHDDIMC 645
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQAC 44
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 526-596 9.17e-05

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: 41.03  E-value: 9.17e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1984005256   526 WSAWSPWSTCQHGTGEqssghghphshshsehaekidTCQCQTRECNNPPPQHGGESCTGTRVRVTNCTVH 596
Cdd:smart00209    1 WSEWSEWSPCSVTCGG---------------------GVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
Sema_plexin_B3 cd11277
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of ...
 44-320 1.09e-04

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


Pssm-ID: 200538 [Multi-domain]  Cd Length: 434  Bit Score: 45.96  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256   44 TTYSQLLFDVARQQVVVGARDNLYRLTltslTDLEHASW--SAPEDKVNTCQnKGQSVEDCR------NYVKVLLSNGKS 115
Cdd:cd11277      6 ATFNHLALDPGSGTLYVGAVNRLYQLS----PDLQLLGEavTGPVLDSPDCL-PFRDPADCPqarltdNANKLLLVSERA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  116 --LFTCGTyAFSPWCAWREIENITS-------------VTSEMSGVAMCPY-SPHANVTALL-SRGPSGGLFAGAPtdfs 178
Cdd:cd11277     81 geLVACGQ-VRQGVCEKRRLGNVAQvlyqaedpgdgqfVAANDPGVATVGLvVEAPGRDLLLvGRGLTGKLSAGIP---- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  179 gadPAIYRTLASPNLRTRQYDSKWL-------NDpQFVGSFETEDHVYFLFRESAVEyincGKKIY-SRIARVCKNDRGg 250
Cdd:cd11277    156 ---PLTIRQLAGAQAFSSEGLGKLVvgdfsdyNN-SYVGAFAHNGYVYFLFRRRGAR----AQAEYrTYVARVCLGDTN- 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1984005256  251 qimmkdvWTTFSKARLNCSLPgefpfyYDEIQGAAYHPEEGIIYATF-----TTPiNGIAGSAICAFNMSAVFAS 320
Cdd:cd11277    227 -------LYSYVEVPLVCQGG------YNLAQAAYLAPGQGTLFVVFaagqgSTP-TPTDQTALCAYPLVELDSA 287
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 855-899 1.88e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 1.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1984005256  855 SC--WTDWSECSASCGIGVRTRTRECLGpESCSgpRSIRETCEMPSC 899
Cdd:PTZ00441   239 SCgpWDEWTPCSVTCGKGTHSRSRPILH-EGCT--THMVEECEEEEC 282
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 858-899 3.31e-04

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: 39.74  E-value: 3.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1984005256  858 TDWSECSASCGIGVRTRTREC--------LGPESCSGPR--SIRETCEMPSC 899
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCvqkgggsiVPDSECSAQKkpPETQSCNLKPC 55
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
 374-488 3.95e-04

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: 44.15  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984005256  374 STMLE--PLHTATLERFIHIAvdvtpTKLHRSVTVLYVSTATGLIKKISVLPRTQETCIVEIWGSLP--SPPM-TLQFLK 448
Cdd:cd11272    379 STPVEgvTLYTSSRDRLTSVA-----SYVYNGYSVVFVGTKSGKLKKIRADGPPHGGVQYEMVSVFKdgSPILrDMAFSI 453

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1984005256  449 DTQSLYVGMEIGLLRIPAVQCYRHRSRQACLNAQEPYCGW 488
Cdd:cd11272    454 DHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDPHCGW 493
TSP_1 pfam00090
Thrombospondin type 1 domain;
797-841 1.40e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 37.78  E-value: 1.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1984005256  797 GEWSSWGICDRPCGRGSQHRVRQCESPPCENGL----TKQSRVCNPHPC 841
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPctgdDIETQACKMDKC 49
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 858-899 4.63e-03

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 36.16  E-value: 4.63e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1984005256  858 TDWSECSASCGIGVRTRTREclGPESCsgpRSIRET--CEMPSC 899
Cdd:pfam19035    6 TEWSPCSKTCGMGVSTRVSN--DNAEC---KLVTETrlCQLRPC 44
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 666-717 5.94e-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: 35.89  E-value: 5.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1984005256  666 WSTwGPWHACSKPCNGGIRVRKRTCDSPSSKK--GGAECPGCD--QQIEECNAHEC 717
Cdd:pfam19030    1 WVA-GPWGECSVTCGGGVQTRLVQCVQKGGGSivPDSECSAQKkpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 905-944 6.08e-03

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: 36.03  E-value: 6.08e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1984005256   905 WDTWSLWTPCD---GDHQQHRKRICL----EHGSGMCQGKDREIRDC 944
Cdd:smart00209    1 WSEWSEWSPCSvtcGGGVQTRTRSCCspppQNGGGPCTGEDVETRAC 47
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 469-516 6.32e-03

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: 35.76  E-value: 6.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1984005256  469 CYRHRSRQACLNAQEPYCGWNEHLMKCAQAPKQNYLANH---WHQEVTKCP 516
Cdd:pfam01437    2 CSQYTSCSSCLAARDPYCGWCSSEGRCVRRSACGAPEGNceeWEQASSKCP 52
 
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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