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Conserved domains on  [gi|91982767|ref|NP_001026872|]
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semaphorin-5B isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
118-554 0e+00

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


:

Pssm-ID: 200525 [Multi-domain]  Cd Length: 437  Bit Score: 967.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 197
Cdd:cd11264    1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 277
Cdd:cd11264   81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  278 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 357
Cdd:cd11264  161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  358 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNENL 437
Cdd:cd11264  241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  438 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 517
Cdd:cd11264  321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 91982767  518 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 554
Cdd:cd11264  401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
856-908 1.93e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.93e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     856 WAAWGPWSSCSRDCELGFRVRKRTCTNPEPRNGGLPCVGDAAEYQDCNPQACP 908
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
913-965 1.07e-14

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: 69.15  E-value: 1.07e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     913 WSCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDICLGLHTEEALCATQACP 965
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
667-720 3.37e-14

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: 68.00  E-value: 3.37e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 91982767     667 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRHGGRICVGKSREERFCNENtPCP 720
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
725-771 2.47e-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: 56.83  E-value: 2.47e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     725 WASWGSWSKCSSNCGGGMQSRRRACEN------GNSCLGCGVEFKTCNPEGCP 771
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
555-602 1.56e-08

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


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 51.94  E-value: 1.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91982767    555 RCAAYRSQGACLGARDPYCGWDGKQQRCST----LEDSSNMSLWTQNITACP 602
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
969-1010 4.25e-05

Thrombospondin type 1 domain;


:

Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 4.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 91982767    969 SPWSEWSKCT---DDGAQSRSRHCEELLPGSSACAGNSSQSRPCP 1010
Cdd:pfam00090    1 SPWSPWSPCSvtcGKGIQVRQRTCKSPFPGGEPCTGDDIETQACK 45
 
Name Accession Description Interval E-value
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
118-554 0e+00

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


Pssm-ID: 200525 [Multi-domain]  Cd Length: 437  Bit Score: 967.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 197
Cdd:cd11264    1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 277
Cdd:cd11264   81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  278 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 357
Cdd:cd11264  161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  358 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNENL 437
Cdd:cd11264  241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  438 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 517
Cdd:cd11264  321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 91982767  518 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 554
Cdd:cd11264  401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema smart00630
semaphorin domain;
126-525 5.09e-133

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 409.84  E-value: 5.09e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     126 FSQLALDPSGNQLIVGARNYLFRLSLANVSLL-QATEWASSEDTRRSCQSKGKTE-EECQNYVRVLI-VAGRKVFMCGTN 202
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     203 AFSPMCTSRQVgnlsrtiekingvarcpydprhnstavissqGELYAATVIDFSGRDPAIYRSLG-------SGPPLRTA 275
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSLRTV 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     276 QYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPF 354
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     355 YYNELQSAFHLPE----QDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN-PIPNFQCGTLP 429
Cdd:smart00630  210 YFNELQAAFLLPPgsesDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     430 ETGPN-ENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAkDTLYHVLYIGTESGTILKALSTAS 506
Cdd:smart00630  290 NKPPSsKDLPDETLNFIKSHPLMDEVVQPLTGRPLFvkTDSNYLLTSIAVDRVAT-DGNYTVLFLGTSDGRILKVVLSES 368
                           410       420
                    ....*....|....*....|
gi 91982767     507 R-SLHGCYLEELHVLPPGRR 525
Cdd:smart00630  369 SsSSESVVLEEISVFPDGSP 388
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
359-535 1.31e-55

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: 190.94  E-value: 1.31e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767    359 LQSAFHLPE------QDLIYGVFTTN-VNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPET 431
Cdd:pfam01403    1 LQDVFVLKPgagdalDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767    432 GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHg 511
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEESH- 159
                          170       180
                   ....*....|....*....|....
gi 91982767    512 cYLEELHVLPPGrrEPLRSLRILH 535
Cdd:pfam01403  160 -IIEEIQVFPEP--QPVLNLLLSS 180
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
856-908 1.93e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.93e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     856 WAAWGPWSSCSRDCELGFRVRKRTCTNPEPRNGGLPCVGDAAEYQDCNPQACP 908
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
913-965 1.07e-14

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: 69.15  E-value: 1.07e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     913 WSCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDICLGLHTEEALCATQACP 965
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
667-720 3.37e-14

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: 68.00  E-value: 3.37e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 91982767     667 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRHGGRICVGKSREERFCNENtPCP 720
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
725-771 2.47e-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: 56.83  E-value: 2.47e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     725 WASWGSWSKCSSNCGGGMQSRRRACEN------GNSCLGCGVEFKTCNPEGCP 771
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
555-602 1.56e-08

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 51.94  E-value: 1.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91982767    555 RCAAYRSQGACLGARDPYCGWDGKQQRCST----LEDSSNMSLWTQNITACP 602
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
859-907 1.76e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 1.76e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 91982767    859 WGPWSSCSRDCELGFRVRKRTCTNPEPrnGGLPCVGDAAEYQDCNPQAC 907
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
668-719 5.19e-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: 47.27  E-value: 5.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91982767    668 TPWSSWALCSTSCGIGFQVRQRSCSNPaPRHGGRICVGKSrEERFCNENtPC 719
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL-ERRPCNLP-PC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
728-770 7.15e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 7.15e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 91982767    728 WGSWSKCSSNCGGGMQSRRRAC----ENGNSCLGCGVEFKTCNPEGC 770
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
555-592 3.83e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 44.84  E-value: 3.83e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 91982767     555 RCAAYRSQGACLGARDPYCGWDGKQQRCSTLEDSSNMS 592
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRR 38
TSP_1 pfam00090
Thrombospondin type 1 domain;
914-964 4.66e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 4.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 91982767    914 SCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEdiCLGLHTEEALCATQAC 964
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEP--CTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
969-1010 4.25e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 4.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 91982767    969 SPWSEWSKCT---DDGAQSRSRHCEELLPGSSACAGNSSQSRPCP 1010
Cdd:pfam00090    1 SPWSPWSPCSvtcGKGIQVRQRTCKSPFPGGEPCTGDDIETQACK 45
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
968-1009 1.77e-04

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: 40.26  E-value: 1.77e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 91982767     968 WSPWSEWSKCT---DDGAQSRSRHCEELLP--GSSACAGNSSQSRPC 1009
Cdd:smart00209    1 WSEWSEWSPCSvtcGGGVQTRTRSCCSPPPqnGGGPCTGEDVETRAC 47
 
Name Accession Description Interval E-value
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
118-554 0e+00

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


Pssm-ID: 200525 [Multi-domain]  Cd Length: 437  Bit Score: 967.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 197
Cdd:cd11264    1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 277
Cdd:cd11264   81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  278 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 357
Cdd:cd11264  161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  358 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNENL 437
Cdd:cd11264  241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  438 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 517
Cdd:cd11264  321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 91982767  518 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 554
Cdd:cd11264  401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
118-554 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: 735.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 197
Cdd:cd11241    1 FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSVEECQNYVRVLLVVGKNLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 277
Cdd:cd11241   81 TCGTYAFSPVCTIRKLSNLTQILDTISGVARCPYSPAHNSTALISASGELYAGTVYDFSGRDPAIYRSLGGKPPLRTAQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  278 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYY 356
Cdd:cd11241  161 NSKWLNEPNFVGSYEIGNHTYFFFRENAVEHqDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGEFPFYY 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  357 NELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNEN 436
Cdd:cd11241  241 NEIQGTFYLPETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPTPNPHPNFQCTTSIDRGQPAN 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  437 LTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDT-LYHVLYIGTESGTILKALSTaSRSLHGCYLE 515
Cdd:cd11241  321 TTERDLQDAQKYQLMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRGTqLVHIFYVGTDYGTILKMYQP-HRSQKSCTLE 399
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 91982767  516 ELHVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 554
Cdd:cd11241  400 EIKILPAMKGEPITSLQFLKSEKSLFVGLETGVLRIPLN 438
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
118-554 0e+00

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


Pssm-ID: 200524 [Multi-domain]  Cd Length: 436  Bit Score: 729.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 197
Cdd:cd11263    1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 277
Cdd:cd11263   81 TCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  278 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 357
Cdd:cd11263  161 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  358 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLpETGPNENL 437
Cdd:cd11263  241 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTM-DQGLYVNL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  438 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 517
Cdd:cd11263  320 TERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEI 399
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 91982767  518 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 554
Cdd:cd11263  400 ELFPKRQREPIRSLQILHSQSVLFVGLQEHVIKIPLK 436
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
118-552 2.26e-161

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: 485.83  E-value: 2.26e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 197
Cdd:cd11265    1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLG--SGPPLRTA 275
Cdd:cd11265   81 ACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSSSGQLFVGSPTDFSGSDSAIYRTLGtsNKSFLRTK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  276 QYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGR-FLLEDTWTTFMKARLNCSRPGEVP 353
Cdd:cd11265  161 QYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYmNCGKVIYSRIARVCKNDVGGGtMLLKDNWTTFLKARLNCSLPGEYP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  354 FYYNELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWlpIANPIPN-FQCGTLPETG 432
Cdd:cd11265  241 FYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAW--ERVNVNHrDHFNQCSSSS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  433 PNenlterSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAK-DTLYHVLYIGTESGTIlKALSTASRSLHG 511
Cdd:cd11265  319 SS------HLLESSRYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKiHQSVHVLYVATTGGLI-KKISVLPRTQET 391
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 91982767  512 CYLEELHVLPPGRRePLRSLRILHSARALFVGLRDGVLRVP 552
Cdd:cd11265  392 CLVEIWQPLPTPDS-PIKTMQYLKVTDSLYVGTELALMRIP 431
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
131-553 7.26e-156

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: 471.51  E-value: 7.26e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  131 LDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGR-KVFMCGTNAFSPMCT 209
Cdd:cd11235    8 LHEDRSTLYVGARDRVYLVDLDSLYTEQKVAWPSSPDDVDTCYLKGKSKDDCRNFIKVLEKNSDdSLLVCGTNAFNPSCR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  210 SRQVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVA 289
Cdd:cd11235   88 NYNVETFELVGKEESGRGKCPYDPDHNSTALFA-DGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWLNEPQFVG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  290 AYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSAFHLPEQ 368
Cdd:cd11235  167 AFDIGDYVYFFFREIAVEYiNCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFPFYFNELQDVFDLPSP 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  369 D----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPnfqCGTLPETGPNE--NLTERSL 442
Cdd:cd11235  247 SnkekIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDERV---PEPRPGTCVDDssPLPDDTL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  443 QDAQRLFLMSEAVQPVTPEP--CVTQDSVRFSHLVVDLVQAK-DTLYHVLYIGTESGTILKALSTASRSLHG-CYLEELH 518
Cdd:cd11235  324 NFIKSHPLMDEAVTPILNRPlfIKTDVNYRFTKIAVDRVQAKlGQTYDVLFVGTDRGIILKVVSLPEQGLQAsNILEEMP 403
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 91982767  519 VLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11235  404 VGPPP--EPIQTMQLSRKRRSLYVGSETGVLQVPL 436
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
131-556 3.47e-137

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: 423.28  E-value: 3.47e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  131 LDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIV--AGRkVFMCGTNAFSPMC 208
Cdd:cd11237   10 LDQDGNSLLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLAKksAGR-LLVCGTNAYKPLC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  209 tsRQ---VGNLSRTIEKINGVARCPYDPRHNSTAViSSQGELYAATVIDFSGRDPAIYRSlgsgpPLRTAQYNSKWLNEP 285
Cdd:cd11237   89 --REytvKDGGYRVEREFDGQGLCPYDPKHNSTAV-YADGQLYSATVADFSGADPLIYRE-----PLRTERYDLKQLNAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  286 NFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSAFH 364
Cdd:cd11237  161 NFVSSFAYGDYVYFFFRETAVEYiNCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGEYPFYFNEIQSTSD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  365 LPE-------QDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIpnfqcgtLPETGPNENL 437
Cdd:cd11237  241 IVEggyggksAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVPSNK-------VPEPRPGQCV 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  438 TE-RSLQDAQRLF-----LMSEAVQPVTPEPCVTQDSV--RFSHLVVD-LVQAKDTLYH-VLYIGTESGTILKALSTASR 507
Cdd:cd11237  314 NDsRTLPDVTVNFikshpLMDEAVPSFFGRPILVRTSLqyRFTQIAVDpQVKALDGKYYdVLFIGTDDGKVLKAVNIASA 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 91982767  508 SLHG----CYLEELHVLPPGrrEPLRSLRILHSARA--LFVGLRDGVLRVPLERC 556
Cdd:cd11237  394 DTVDkvspVVIEETQVFPRG--VPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema smart00630
semaphorin domain;
126-525 5.09e-133

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 409.84  E-value: 5.09e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     126 FSQLALDPSGNQLIVGARNYLFRLSLANVSLL-QATEWASSEDTRRSCQSKGKTE-EECQNYVRVLI-VAGRKVFMCGTN 202
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     203 AFSPMCTSRQVgnlsrtiekingvarcpydprhnstavissqGELYAATVIDFSGRDPAIYRSLG-------SGPPLRTA 275
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSLRTV 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     276 QYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPF 354
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     355 YYNELQSAFHLPE----QDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN-PIPNFQCGTLP 429
Cdd:smart00630  210 YFNELQAAFLLPPgsesDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767     430 ETGPN-ENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAkDTLYHVLYIGTESGTILKALSTAS 506
Cdd:smart00630  290 NKPPSsKDLPDETLNFIKSHPLMDEVVQPLTGRPLFvkTDSNYLLTSIAVDRVAT-DGNYTVLFLGTSDGRILKVVLSES 368
                           410       420
                    ....*....|....*....|
gi 91982767     507 R-SLHGCYLEELHVLPPGRR 525
Cdd:smart00630  369 SsSSESVVLEEISVFPDGSP 388
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
118-553 1.10e-115

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: 366.74  E-value: 1.10e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVS-LLQAT-EWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGR 194
Cdd:cd11240    1 FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDIStELKDKiKWEASEDKKKECANKGKDNQtDCFNFIRILQFYNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  195 -KVFMCGTNAFSPMCT--SRQVGNLSRtIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPP 271
Cdd:cd11240   81 tHLYVCGTFAFSPRCTyiNLSDFSLSS-IKFEDGKGRCPFDPAQRYTAIMVD-GELYSATVNNFLGSEPVISRNHSEGNV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  272 LRTaQYNSKWLNEPNFV-AAY---DIGLFA------YFFLRENAVEHDCG-RTVYSRVARVCKNDVGGRFLLEDTWTTFM 340
Cdd:cd11240  159 LKT-ENTLRWLNEPAFVgSAHireSIDSPDgdddkiYFFFTETAVEYDFYeKVTVSRVARVCKGDLGGQRTLQKKWTTFL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  341 KARLNCSRPGEvPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPI 416
Cdd:cd11240  238 KAQLVCSQPDS-GLPFNVLRDVFVLSPDSwdatIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  417 ANPIPNFQ---CGTLPETGPNE----NLTERSLQDAQRLFLMSEAVQPVTpEPCVTQDSVRFSHLVVDLVQAKD-TLYHV 488
Cdd:cd11240  317 TGPVPDPRpgaCITNSARSQGItsslNLPDNVLTFVKDHPLMDEQVHPIN-RPLLVKSGVNYTRIAVHRVQALDgQTYTV 395
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982767  489 LYIGTESGTILKALSTASRsLHgcYLEELHVLPPgrREPLRSLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11240  396 LFLGTEDGFLHKAVSLDGG-MH--IIEEIQLFDQ--PQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
138-553 7.39e-112

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: 356.83  E-value: 7.39e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  138 LIVGARNYLFRLSLANVSLLQAT-----EWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMCGTNAFSPMCTSR 211
Cdd:cd11242   21 LYIAARDHVYTVDLDASHTEEIVpskklTWRSRQADVENCRMKGKHKDECHNFIKVLVPRNDEtLFVCGTNAFNPVCRNY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  212 QVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVAAY 291
Cdd:cd11242  101 RIDTLEQDGEEISGMARCPFDAKQANVALFA-DGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYDSKWLKEPHFVHAV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  292 DIGLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQS---AFHLP 366
Cdd:cd11242  180 EYGDYVYFFFREIAVEYNtLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPGDSHFYFDVLQAvtdVIRIN 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  367 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA-NPIPNFQCGTLPETGPNENL-TERSLQD 444
Cdd:cd11242  260 GRPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPeDRVPKPRPGCCAGSGSAEKYkTSNDFPD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  445 AQRLF-----LMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHG--CYLE 515
Cdd:cd11242  340 DTLNFikthpLMDEAVPSIINRPWFTRTMVRYrlTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARIGPSGSNgsVFLE 419
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 91982767  516 ELHVLPP----GRREPLR---SLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11242  420 EIDVYNPakcsYDGEEDRriiGLELDRASHALFVAFSGCVIRVPL 464
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
122-556 2.75e-107

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: 344.73  E-value: 2.75e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  122 GARDFSQLALDPSGNQLIVGARNYLFRLSLANVSL-LQATEWASSEDTRRSCQSKGKT-EEECQNYVRVLIVAGRK-VFM 198
Cdd:cd11239    6 NSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQdPKKIYWPASPERIEECKMAGKDpNTECANFVRVLQPYNRThLYA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  199 CGTNAFSPMCTSRQVGN---------LSRTIEkiNGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSG 269
Cdd:cd11239   86 CGTGAFHPICAFINVGRrledpifklDDSSLE--SGRGKCPFDPNQPFASVLID-GELYSGTAIDFMGRDAAIFRSLGHR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  270 PPLRTAQYNSKWLNEPNFVAAYDI-------GLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMK 341
Cdd:cd11239  163 HYIRTEQYDSRWLNEPKFVGAYLIpdsdnpdDDKVYFFFREKAVEAEgSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  342 ARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLP 415
Cdd:cd11239  243 ARLVCSVPGPdgIDTYFDELEDVFLLPTRDpknpLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVE 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  416 IANPIPNFQCGTLPE--TGPNENLTeRSLQD-----AQRLFLMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLY 486
Cdd:cd11239  323 YQGKVPYPRPGTCPSktYGPLYKST-KDFPDdvisfARSHPLMYNPVYPLHGRPLLIRTNVpyRLTQIAVDRVEAEDGQY 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982767  487 HVLYIGTESGTILK--ALSTASRSLHGCYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11239  402 DVLFIGTDSGTVLKvvSLPKENWEMEEVILEELQVFK--HPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
126-548 6.57e-104

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: 335.16  E-value: 6.57e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  126 FSQLALDPSGNQLIVGARNYLFRLSLANVS----LLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVA--GRKVFM 198
Cdd:cd11238    3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINdtgnNCARDELTLSPSDVSECVSKGKDEEyECRNHVRVIQPMgdGQTLYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  199 CGTNAFSPmcTSRQV-GNLSRTIEKI----NGVARCPYDPRHNSTAVISSQGE------LYAATVIDFSGRDPAIYRslg 267
Cdd:cd11238   83 CSTNAMNP--KDRVLdANLLHLPEYVpgpgNGIGKCPYDPDDNSTAVWVEWGNpgdlpaLYSGTRTEFTKANTVIYR--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  268 sgPPL------------RTAQYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLED 334
Cdd:cd11238  158 --PPLynntkgrhesfmRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETAVEYiNCGKVVYSRVARVCKKDTGGKNVLRQ 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  335 TWTTFMKARLNCSRPGEVPFYYNELQSAFHLPEQD--LIYGVFTTNVNSIAASAVCAFNLSAISQAFN-GPFRYQENPRA 411
Cdd:cd11238  236 NWTTFLKARLNCSISGEFPFYFNEIQSVYKVPGRDdtLFYATFTTSENGFTGSAVCVFTLSDINAAFDtGKFKEQASSSS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  412 AWLPI-ANPIPNFQCGTLpeTGPNENLTERSLQDAQRLFLMSEAVQpvTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLY 490
Cdd:cd11238  316 AWLPVlSSEVPEPRPGTC--VNDSATLSDTVLHFARTHPLMDDAVS--HGPPLLYLRDVVFTHLVVDKLRIDDQEYVVFY 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91982767  491 IGTESGTILKALSTASRS-LHGCYLEELHVLPPgrrEPLRSLRILHsARALFVGLRDGV 548
Cdd:cd11238  392 AGSNDGKVYKIVHWKDAGeSKSNLLDVFELTPG---EPIRAMELLP-GEFLYVASDHRV 446
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
136-553 2.05e-99

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: 323.52  E-value: 2.05e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  136 NQLIVGARNYLFRLSLANVSLLQAT-----EWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMCGTNAFSPMCT 209
Cdd:cd11269   19 DTLYIAGRDQVYTVNLNEVPKTEVTpsrklTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEmVFVCGTNAFNPMCR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  210 SRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVA 289
Cdd:cd11269   99 YYRLSTLEYDGEEISGLARCPFDARQTNVALFAD-GKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLH 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  290 AYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSAFHLPE 367
Cdd:cd11269  178 AIEYGNYVYFFFREIAVEHnNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFFYFDVLQSITDIIE 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  368 QD---LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA-NPIPNFQCGTLPETGPNE------NL 437
Cdd:cd11269  258 INgipTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPeDKVPKPRPGCCAKHGLAEayktsiDF 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  438 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALS-TASRSLH-GCY 513
Cdd:cd11269  338 PDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYrlTAIAVDHAAGPHQNYTVIFVGSEAGVVLKILAkTSPFSLNdSVL 417
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 91982767  514 LEEL----HVLPPGRREPLRSLRILHSAR---ALFVGLRDGVLRVPL 553
Cdd:cd11269  418 LEEIeaynHAKCSAENEEDRRVISLQLDRdhhALFVAFSSCVVRIPL 464
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
138-553 1.53e-96

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


Pssm-ID: 200528 [Multi-domain]  Cd Length: 466  Bit Score: 315.62  E-value: 1.53e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  138 LIVGARNYLFRLSLANVS-----LLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMCGTNAFSPMCTSR 211
Cdd:cd11267   21 LYIGDRDNLYRVELDPTAgtemrYHKKLTWRSNKNDINVCRMKGKHEGECRNFIKVLLLRDYGtLFVCGTNAFNPVCANY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  212 QVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVAAY 291
Cdd:cd11267  101 SIDTLEPVGDNISGMARCPYDPKHANVALFA-DGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEPYFVHAV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  292 DIGLFAYFFLRENAVE-HDCGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSA---FHLP 366
Cdd:cd11267  180 EWGSHVYFFFREIAMEfNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVsdiLNLG 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  367 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN---PIPNFQCGTLPETGPNenlTERSLQ 443
Cdd:cd11267  260 GRPVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEelvPRPRPGCCAAPGMRYN---SSSTLP 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  444 DAQRLF-----LMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKAL-----STASRSLHG 511
Cdd:cd11267  337 DEVLNFvkthpLMDEAVPSLGHAPWIVRTMTRYqlTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLiipnaSSSEISNQS 416
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 91982767  512 CYLEELHVLPPGR--------REPLrSLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11267  417 VFLEELETYNPERcgwdspqaQKLL-SLELDKGSGGLLLAFPSCVVRVPV 465
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
126-556 4.00e-93

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: 306.45  E-value: 4.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  126 FSQLALDPSGNQLIVGARNYLFRLSLANVSLL-QATEWASSEDTRRSCQSKGK-TEEECQNYVRVLIVAGRK-VFMCGTN 202
Cdd:cd11250   10 YDALLLDEERGRLFVGAKNYLASLSLDNISKQeKKIYWPAPVEWREECNWAGKdINTDCMNYVKILHHYNRThLYACGTG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  203 AFSPMCTSRQVGN-LSRTIEKIN------GVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSLGSGPPLRTA 275
Cdd:cd11250   90 AFHPTCAFVEVGQrMEDHVFRLDpsrvedGKGKSPYDPRHTAASVLVGD-ELYSGVATDLMGRDFTIFRSLGQRPSLRTE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  276 QYNSKWLNEPNFVAAYDIGLF-------AYFFLRENAVE-HDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCS 347
Cdd:cd11250  169 QHDSRWLNEPKFVKVFWIPESenpdddkIYFFFRETAVEaAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCS 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  348 RPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIP 421
Cdd:cd11250  249 VPGNegGDTHFDELRDVFLLQTRDkrnpLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGKVP 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  422 NFQCGTLPET-----GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLYHVLYIGTE 494
Cdd:cd11250  329 YPRPGMCPSKtfgsfESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIpyTFTQIAVDRVAAADGHYDVMFIGTD 408
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982767  495 SGTILKALSTASRSLH---GCYLEELHVLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11250  409 VGSVLKVISVPKGSWPsneELLLEELHVFKDS--SPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
121-556 6.87e-93

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: 306.54  E-value: 6.87e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  121 PGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGK-TEEECQNYVRVLIVAGRK-VFM 198
Cdd:cd11249   27 ANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKWAGKdILKECANFIKVLKAYNQThLYA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  199 CGTNAFSPMCTSRQVGNLSR-TIEKI------NGVARCPYDPRHnSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPP 271
Cdd:cd11249  107 CGTGAFHPVCTYIEVGHHPEdNIFRLedshfeNGRGKSPYDPKL-LTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  272 LRTAQYNSKWLNEPNFVAAYDIGLF-------AYFFLRENAV--EHdCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKA 342
Cdd:cd11249  186 IRTEQHDSRWLNDPRFISAHLIPESdnpeddkIYFFFRENAIdgEH-TGKATHARIGQLCKNDFGGHRSLVNKWTTFLKA 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  343 RLNCSRPGE--VPFYYNELQSAFHL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPI 416
Cdd:cd11249  265 RLICSVPGPngIDTHFDELQDVFLMnskdPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPF 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  417 ANPIPNFQCGTLPETGPNENLTERSLQDAQRLF-----LMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLYHVL 489
Cdd:cd11249  345 QGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFarshpAMYNPVFPINNRPIIIKTDVdyQFTQIVVDRVEAEDGQYDVM 424
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982767  490 YIGTESGTILKALSTASRSLHG---CYLEELHVLppgrREP--LRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11249  425 FIGTDMGTVLKVVSIPKETWHDleeVLLEEMTVF----REPtaISAMELSTKQQQLYIGSAIGVSQLPLHRC 492
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
138-553 4.21e-92

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: 303.49  E-value: 4.21e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  138 LIVGARNYLFRLSL-----ANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGR-KVFMCGTNAFSPMCTSR 211
Cdd:cd11266   21 LYIAARDHIYTVDIdtshtEEIYFSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKRNDdTLFVCGTNAFNPSCRNY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  212 QVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVAAY 291
Cdd:cd11266  101 KMDTLEFFGDEFSGMARCPYDAKHANVALFA-DGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  292 DIGLFAYFFLRENAVE-HDCGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQS---AFHLP 366
Cdd:cd11266  180 DYGDYIYFFFREIAVEyNSMGKVVFPRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQAvtdVIHIN 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  367 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN---PIPNFQC----GTLPETGPNENLTE 439
Cdd:cd11266  260 GRDVVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDervPKPRPGCcagsSSLEKYATSNEFPD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  440 RSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRS--LHGC-YL 514
Cdd:cd11266  340 DTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYrlTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARTGNSgfLNDSlFL 419
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 91982767  515 EELHVLPPGR--REPLRSLRIL-----HSARALFVGLRDGVLRVPL 553
Cdd:cd11266  420 EEMNVYNSEKcsYDGVEDKRIMgmqldKASSALYVAFSTCVIKVPL 465
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
125-556 7.44e-89

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: 294.81  E-value: 7.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  125 DFSQLALDPSGNQLIVGARNYLFRLSLANVS---LLqaTEWASSEDTRRSCQSKGK-TEEECQNYVRVLIVAGRK-VFMC 199
Cdd:cd11254    9 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWPASPQRIEECILSGKgSNGECGNFIRLIQPWNRThLYVC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  200 GTNAFSPMCTSRQVGNLSRTI------EKI-NGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPPL 272
Cdd:cd11254   87 GTGAYNPVCAYINRGRRAEDYmfrlepDKLeSGKGKCPYDPKQDSVSALIN-GELYAGVYIDFMGTDAAIFRTMGKQPAM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  273 RTAQYNSKWLNEPNFVAAYDIGLFA-------YFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLN 345
Cdd:cd11254  166 RTDQYNSRWLNDPAFVHAHLIPDSSeknddklYFFFREKSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLV 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  346 CSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANP 419
Cdd:cd11254  246 CSVPGAdgIETHFDELRDVFIQPTQDtknpVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGK 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  420 IPNFQCGTLP--ETGPNENLTERSLQDAQRLF----LMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLYHVLYI 491
Cdd:cd11254  326 IPYPRPGTCPggTFTPSMKSTKDYPDEVINFMrthpLMYNAVYPVHRRPLVVRTNVnyRFTTIAVDQVDAADGRYEVLFL 405
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982767  492 GTESGTILKA--LSTASRSLHGCYLEELHVLP-PGrrePLRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11254  406 GTDRGTVQKVivLPKDDLETEELTLEEVEVFKvPA---PIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
138-553 1.13e-85

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: 285.85  E-value: 1.13e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  138 LIVGARNYLFRLSL--ANVSLL--QATEWASSEdtRRSCQSKGKTEEECQNYVRVLIVAGRKVFM-CGTNAFSPMCTSRQ 212
Cdd:cd11270   21 VYIAARDHVFAINLsaSLERIVpqQKLTWKTKD--VEKCTVRGKNSDECYNYIKVLVPRNDETLFaCGTNAFNPTCRNYK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  213 VGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPP-LRTAQYNSKWLNEPNFVAAY 291
Cdd:cd11270   99 MSSLEQDGEEVIGQARCPFESRQSNVGLFAG-GDFYSATMTDFLASDAVIYRSLGESSPvLRTVKYDSKWLREPHFLHAI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  292 DIGLFAYFFLRENAVEHDC-GRTVYSRVARVCKNDVGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQSA---FHLP 366
Cdd:cd11270  178 EYGNYVYFFLSEIAVEYTTlGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPGDSFFYFDVLQSLtnvMQIN 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  367 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN---PIPNFQC----GTLPETGPNENLTE 439
Cdd:cd11270  258 HRPAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVPDeavPKPRPGScagdGPAAGYKSSTNFPD 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  440 RSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALS--TASRSLHGCYLE 515
Cdd:cd11270  338 ETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFklTQIAVDTAAGPYKNYTVVFLGSENGHVLKVLAsmHPNSSYSTQVLE 417
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 91982767  516 ELHVLPPG----RREPLR--SLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11270  418 DIDVYNPNkcnvRGEDRRilGLELDKDHHALFVAFTGCVIRVPL 461
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
124-556 1.70e-81

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: 274.86  E-value: 1.70e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  124 RDFSQLALDPSGNQLIVGARNYLFRLSLANVSL-LQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGRK-VFMCG 200
Cdd:cd11252    8 LDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKnPKKIYWPAAKERVELCKLAGKDANtECANFIRVLHPYNRThVYVCG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  201 TNAFSPMCTSRQVGNL---------SRTIEkiNGVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSLGSGPP 271
Cdd:cd11252   88 TGAFHPTCGYIELGTHkedriflldTQNLE--SGRLKCPFDPQQPFASVMTDE-YLYAGTASDFLGKDTTFTRSLGPTPD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  272 ---LRTAQYNSKWLNEPNFVAAYDIGLF-------AYFFLRENAVEHDCG-RTVYSRVARVCKNDVGGRFLLEDTWTTFM 340
Cdd:cd11252  165 hhyIRTDISEHYWLNGAKFIGTFPIPDTynpdddkIYFFFREASQDGSTSdKSVLSRVGRVCKNDVGGQRSLINKWTTFL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  341 KARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWL 414
Cdd:cd11252  245 KARLVCSIPGPdgADTHFDELQDIFLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  415 PIANPIPNFQCGTLPETGPNENL-TERSLQD-----AQRLFLMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLY 486
Cdd:cd11252  325 QYEGRIPYPRPGTCPSKTYDPLIkSTKDFPDevisfIKRHPLMYKSVYPLTGGPVFTRINVdyRLTQIVVDHVAAEDGQY 404
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982767  487 HVLYIGTESGTILKALSTASR--SLHGCYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11252  405 DVMFLGTDIGTVLKVVSITKEkwTMEEVVLEELQIFK--HPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
118-553 2.73e-81

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: 273.66  E-value: 2.73e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVS---LLQATEWASSEDTRRSCQSKGKT-EEECQNYVRVLI-VA 192
Cdd:cd11257    2 FEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISptgEQQELTWSADEEKKQECSFKGKDpQRDCQNYIKILLrLN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  193 GRKVFMCGTNAFSPMCTSRQVGNLSRTIEKI------NGVARCPYDPRHNSTAvISSQGELYAATVIDFSGRDPAIYRSL 266
Cdd:cd11257   82 STHLFTCGTYAFSPICTYIVMTNFSLERDEKgeplleDGKGRCPFDPEYKSTA-IMVDGELYTGTVSNFQGNDPIIYRSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  267 GSGPPLRTAqyNS-KWLNEPNFVA-AYDIGLFA---------YFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLED 334
Cdd:cd11257  161 GSGTPLKTE--NSlNWLQDPAFVGsAYIQESLPklvgdddkiYFFFSETGKEFDFfENTIVSRIARVCKGDEGGERVLQK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  335 TWTTFMKARLNCSRPGEvPFYYNELQSAFHLP--EQD----LIYGVFTTNVNSIAA--SAVCAFNLSAISQAFNGPFRYQ 406
Cdd:cd11257  239 RWTTFLKAQLLCSLPDD-GFPFNVLQDVFVLTpsPEDwkdtLFYGVFTSQWHKGTAgsSAVCVFTMDQVQRAFNGLYKEV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  407 ENPRAAWLPIANPIPNFQCGTLPETGPNENLTERSLQDAQRL-------FLMSeavQPVTPEPCVTQDSVRFSHLVVDLV 479
Cdd:cd11257  318 NRETQQWYTYTHPVPEPRPGACITNSARERKINSSLHMPDRVlnfvkdhFLMD---GQVRSQPLLLQPQVRYTQIAVHRV 394
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982767  480 QAKDTLYHVLYIGTESGTILKALSTASRsLHgcYLEELHVLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11257  395 KGLHKTYDVLFLGTDDGRLHKAVSVGPM-VH--IIEELQIFSEG--QPVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
118-553 2.73e-80

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: 270.63  E-value: 2.73e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLAN---VSLLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLI-VA 192
Cdd:cd11256    2 FRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTpgpIRLKHQIPWPANDSKISECAFKKKSNEtECFNFIRVLVpVN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  193 GRKVFMCGTNAFSPMCTSRQVGNLS-----RTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLG 267
Cdd:cd11256   82 GTHLYTCGTYAFSPACTYIELDHFSlpppnGTIITMDGKGQSPFDPQHNYTAILVD-GELYTGTMNNFRGNEPIIFRNLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  268 SGPPLRTAQYNsKWLN-EPNFVAAYDIGLF--AYFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLEDTWTTFMKAR 343
Cdd:cd11256  161 TKVSLKTDGFL-RWLNaDAVFVASFNPQGDskVYFFFEETAREFDFfEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  344 LNCSRPGEVPFyyNELQSAFHLPEQD----LIYGVFTT--NVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA 417
Cdd:cd11256  240 LTCSQQGHFPF--NVIHHVALLNQPDpnnsVFYAVFTSqwQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYM 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  418 NPIPNFQCGTLpETGPNenlTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYH-VLYIGTESG 496
Cdd:cd11256  318 GPVSDPRPGSC-SGGKS---SDKALNFMKDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSGHNYtVMFLGTDKG 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 91982767  497 TILKALSTASRSLHgcYLEELHVLPPgrREPLRSLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11256  394 FLHKAVLMGGSESH--IIEEIELLTP--PEPVENLLLAANEGVVYIGYSAGVWRVPL 446
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
125-556 4.41e-79

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: 267.91  E-value: 4.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  125 DFSQLALDPSGNQLIVGARNYLFRLSLANVSllQATE---WASSEDTRRSCQSKGKTEEE-CQNYVRVLIVAGRK-VFMC 199
Cdd:cd11251    9 DYRILFMDEDQDRIYVGSKDHILSLNINNIS--QDALsifWPASASKVEECKMAGKDPTHgCGNFVRVIQPYNRThLYVC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  200 GTNAFSPMCTSRQVGNlsRTIEKI--------NGVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSLGSGPP 271
Cdd:cd11251   87 GSGAFSPVCVYVNRGR--RSEEQVfhidskaeSGKGRCSFNPNVNTVSVMINE-ELFSGMYIDFMGTDAAIFRSLTKRNA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  272 LRTAQYNSKWLNEPNFVAAYDI-------GLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKAR 343
Cdd:cd11251  164 VRTDQHNSKWLSEPIFVDAHLIpdgtdpnDAKLYFFLKERLTDNSgSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKAR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  344 LNCSRPGE--VPFYYNELQSAFHL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA 417
Cdd:cd11251  244 LVCSVMDEdgTETHFDELEDVFLLetdnPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  418 NPIPNFQCGTLPETGPNENL-TERSLQDAQRLF-----LMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAKDTLYHVL 489
Cdd:cd11251  324 GRIPYPRPGTCPGGAFTPNMqSTKEFPDDVVTFirnhpLMFNPIYPIGRRPLLvrTGTDYKYTKIAVDRVNAADGRYHVL 403
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982767  490 YIGTESGTILKALSTASR-SLHG-CYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11251  404 FLGTDKGTVQKVVVLPTNgSLSGeLILEELEVFK--NHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
138-553 1.49e-76

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


Pssm-ID: 200529 [Multi-domain]  Cd Length: 465  Bit Score: 260.79  E-value: 1.49e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  138 LIVGARNYLFRLSLanvsllQATE------------WASSEdtRRSCQSKGKTEEECQNYVRVLIVAGRKVFM-CGTNAF 204
Cdd:cd11268   21 LLVAARDHVFSFDL------QAEEegeglvpnkyltWRSQD--VENCAVRGKLTDECYNYIRVLVPWDSQTLLaCGTNSF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  205 SPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNE 284
Cdd:cd11268   93 SPVCRSYGITSLQQEGEELSGQARCPFDATQSNVAIFA-EGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLRE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  285 PNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQS- 361
Cdd:cd11268  172 PHFVQALEHGDHVYFFFREVSVEDaRLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPGDSTFYFDVLQAl 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  362 --AFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA-NPIPNFQCGTLPETGPNENL- 437
Cdd:cd11268  252 tgPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVSeDRVPSPRPGSCAGVGGAALFs 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  438 TERSLQDAQRLF-----LMSEAVQPVTPEPCVTQDS-VRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRS--L 509
Cdd:cd11268  332 SSRDLPDDVLTFikahpLLDPAVPPVTHQPLLTLTSrALLTQVAVDGMAGPHSNITVMFLGSNDGTVLKVLPPGGRSggP 411
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 91982767  510 HGCYLEELHVLPP----GRREPLRSLRIL-----HSARALFVGLRDGVLRVPL 553
Cdd:cd11268  412 EPILLEEIDAYSParcsGKRTAQTARRIIgleldTEGHRLFVAFSGCIVYLPL 464
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
122-556 1.50e-76

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


Pssm-ID: 200514 [Multi-domain]  Cd Length: 471  Bit Score: 260.94  E-value: 1.50e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  122 GARDFSQLALDPSGNQLIVGARNYLFRLSLANVSL-LQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMC 199
Cdd:cd11253    6 GFLDLHTMLLDEYQERLFVGGRDLLYSLSLERISAnYKEIHWPSTQLQVEDCIMKGRDKPECANYIRVLHHYNRThLLAC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  200 GTNAFSPMCTSRQVGNL---------SRTIEKinGVARCPYDPrhnSTAVISS--QGELYAATVIDFSGRDPAIYRSLGS 268
Cdd:cd11253   86 GTGAFDPVCAFIRVGRGsedhlfqleSDKFER--GRGRCPFDP---NSSFISTliGGELFVGLYSDYWGRDAAIFRTMNH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  269 GPPLRTAQYNSKWLNEPNFVAAYDI-------GLFAYFFLRENAVEHDCG-RTVYSRVARVCKNDVGGRFLLEDTWTTFM 340
Cdd:cd11253  161 LAHIRTEHDDERLLKEPKFVGSYMIpdnedpdDNKVYFFFTEKALEAEGGnHAIYTRVGRVCANDQGGQRMLVNKWSTFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  341 KARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWL 414
Cdd:cd11253  241 KTRLICSVPGPngIDTHFDELEDVFLLRTRDnknpEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWS 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  415 PIANPIPNFQCGTLPET------GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAKDTLY 486
Cdd:cd11253  321 VYEGKVPYPRPGSCASKvngghyGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILvkTDGKYNLKQIAVDRVEAEDGQY 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982767  487 HVLYIGTESGTILKALSTASR---SLHGCYLEELHVLP-PgrrEPLRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11253  401 DVLFIGTDNGIVLKVITIYNQeteTMEEVILEELQVFKvP---VPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
118-553 2.64e-76

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: 259.84  E-value: 2.64e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQAT-EWASSEDTRRSCQSKGK-TEEECQNYVRVL-IVAGR 194
Cdd:cd11260    1 FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKvLWEVTEEKQKDCTNKGKhADIDCHNYIRILhKMNDS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  195 KVFMCGTNAFSPMCTSRQVGNLSRTIEKI--NGVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSlgSGPPL 272
Cdd:cd11260   81 RMYVCGTNAFSPTCDYISYDDGQLTLEGKqeDGKGKCPFDPFQRYSSVMVDQ-DLYSATSMNFLGSEPVIMRS--SPITI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  273 RTaQYNSKWLNEPNFVAAYDIGLFA----------YFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLEDTWTTFMK 341
Cdd:cd11260  158 RT-EFKSSWLNEPNFIYMAAVPESEdspegdddkiYLFFSETAVEYDFyNKLVVSRVARVCKGDLGGQRTLQKKWTSFLK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  342 ARLNCSRP-GEVPFYyneLQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFN-GPFRYQ---ENPRAA 412
Cdd:cd11260  237 ARLDCSVPePSLPYV---IQDVFHVCHQDwrkcVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrGKFKTPvavETSFVK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  413 WLPIANPIPNFQCGTLPETGPNE-------NLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKD-T 484
Cdd:cd11260  314 WVMYSGELPVPRPGACINNAARTsgikkslNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADgQ 393
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982767  485 LYHVLYIGTESGTILKALSTASRSLhgcYLEELHVLPPgrREPLRSLRIlhSARALFVGLRDGVLRVPL 553
Cdd:cd11260  394 SYPVMFIGTANGYVLKAVNYDGEMH---IIEEVQLFEP--EEPIDILRL--SQNQLYAGSASGVVQMPV 455
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
118-553 5.12e-76

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: 259.40  E-value: 5.12e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQ-ATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGRK 195
Cdd:cd11259   12 FHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNALNISEKQhELYWKVSEDKRTKCAVKGKSKQtECRNYIRVLQPLNDT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  196 -VFMCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLgSGPPLRT 274
Cdd:cd11259   92 fLYVCGTNAFQPTCDYLNLTSFRLLGKNEDGKGRCPFDPAQSYTSVMVD-GELYSGTSYNFLGSEPIISRNS-SQSPLRT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  275 aQYNSKWLNEPNFVAAYDIGLFA----------YFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKAR 343
Cdd:cd11259  170 -EYAIPWLNEPSFVFADVIRADPdspdgeddkiYFFFTEVSVEYEfVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKAR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  344 LNCSRPgEVPFYYNELQSAFHLPEQDL----IYGVFTTNVNSIAASAVCAFNLSAISQAFN-GPFRYQ---ENPRAAWLP 415
Cdd:cd11259  249 LICSIP-DKNLVFNVVNDVFILKSPTLkepvIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHTKWVR 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  416 IANPIPNfqcgtlPETGP---NE----------NLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAK 482
Cdd:cd11259  328 YNGEVPK------PRPGAcinNEaraanytsslNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQAL 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982767  483 D-TLYHVLYIGTESGTILKALSTASrSLHgcYLEELHVLPpgRREPLRSLRIL--HSARALFVGLRDGVLRVPL 553
Cdd:cd11259  402 DgTIYDVMFISTDRGALHKAISLEN-EVH--IIEETQLFP--DFEPVQTLLLSskKGRRFLYAGSNSGVVQSPL 470
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
122-556 9.40e-75

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: 255.99  E-value: 9.40e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  122 GARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLlQATE--WASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGRK-VF 197
Cdd:cd11255    6 GDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHP-DAKEihWPPLPGQREECIRKGKDPEtECANFVRVLQPFNRThLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCTSRQVGNLSR--------TIEkiNGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSG 269
Cdd:cd11255   85 ACGTGAFQPVCALINVGHRGEhvfsldptTVE--SGRGRCPHEPKRPFASTFTG-GELYTGLTADFLGRDSVIFRGFGTR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  270 PPLRTaQYNSKWLNEPNFVAAYDIGLFA-------YFFLRENAVE--HDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFM 340
Cdd:cd11255  162 SPLRT-ETDQRLLHEPRFVAAHLIPDNAdrdndkvYFFFTERATEtaEDDDGAIHSRVGRLCANDAGGQRVLVNKWSTFI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  341 KARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWL 414
Cdd:cd11255  241 KARLVCSVPGPhgIQTHFDQLEDVFLLRTKDgkspEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  415 PIANPIPNFQCGTLPET---------GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAKD 483
Cdd:cd11255  321 PYEGKVPYPRPGVCPSKitaqpgrafRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLvkTGLPYRLTQIVVDRVEAED 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982767  484 TLYHVLYIGTESGTILKALS-TASRSLHG--CYLEELHVLP-PgrrEPLRSLRILHSARALFVGLRDGVLRVPLERC 556
Cdd:cd11255  401 GYYDVMFIGTDSGSVLKVIVlQKGNSAAGeeVTLEELQVFKvP---TPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
115-553 1.20e-72

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: 249.33  E-value: 1.20e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  115 VSNFTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAG 193
Cdd:cd11258    1 VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQtECFNYIRFLQPYN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  194 RK-VFMCGTNAFSPMCTSRQVGNLSRTIEKI-NGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPP 271
Cdd:cd11258   81 QShLYTCGTYAFQPKCAYINMLTFTLDRAEFeDGKGKCPYDPAKGHTGLIV-DGELYSATLNNFLGTEPVILRNLGQHYS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  272 LRTaQYNSKWLNEPNFV-AAY---DIGLF------AYFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLEDTWTTFM 340
Cdd:cd11258  160 MKT-EYLAFWLNEPHFVgSAFvpeSVGSFtgdddkIYFFFSERAVEYDCdSEQVVARVARVCKGDLGGARTLQKKWTTFL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  341 KARLNCSRPgEVPFYYNELQSAFHLPEQDL----IYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPI 416
Cdd:cd11258  239 KARLLCSIP-EWQLYFNQLKAVFTLEGASWrnttFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRY 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  417 ANPIPNFQCGTLPETGPNENLTERSLQ--DAQRLF-----LMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKD-TLYHV 488
Cdd:cd11258  318 TDPVPSPRPGSCINNWHRDHGYTSSLElpDNTLNFvkkhpLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDgETYSV 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982767  489 LYIGTESGTILKALSTASRSlhgCYLEELHVLppGRREPLRSLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11258  398 LFIGTLDGWLIKAVSLGSWV---HMIEELQVF--DQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
123-553 1.34e-72

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: 249.29  E-value: 1.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  123 ARDFSQLALDPSGNQLIVGARNYLFRLSLANVS--LLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLI-VAGRKVFM 198
Cdd:cd11262    7 AQNYSTLLLEDESGRLYVGARGAIFSLNASDISdsSALTIDWEASPEQKHQCLKKGKNNQtECFNHVRFLQrFNSTHLYT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  199 CGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRdPAIYRSLGSgPPLRTAQYN 278
Cdd:cd11262   87 CGTHAFRPLCAYIDAERFTLSSQFEEGKEKCPYDPAKGYTGLIVD-GQLYTASQYEFRSF-PDIRRNSPQ-PTLRTEEAP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  279 SKWLNEPNFVAAY----DIGLFA------YFFLRENAVEhdcgRTVY------SRVARVCKNDVGGRFLLEDTWTTFMKA 342
Cdd:cd11262  164 TRWLNDADFVGSVlvreSMNSSVgdddkiYFFFTERSQE----ETAYfsqsrvARVARVCKGDRGGKKTLQRKWTSFLKA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  343 RLNCSRPgEVPFYYNELQSAFHL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN 418
Cdd:cd11262  240 RLVCYIP-EYEFLFNVLRSVFVLwgstPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYTG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  419 PIPNFQCGT-----LPETGPN--ENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKD-TLYHVLY 490
Cdd:cd11262  319 KVPEPRPGScitdeHRSQGINssQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDgRVYDVLF 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982767  491 IGTESGTILKALSTASRsLHgcYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPL 553
Cdd:cd11262  399 LGTDEGWLHKAVVIGSA-VH--IIEELQVFR--EPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
113-552 3.44e-67

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: 234.01  E-value: 3.44e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  113 PWVSNFTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVS-LLQATEWASSEDTRRSCQSKGKTEEECQNYVRVL-I 190
Cdd:cd11261    1 SALTRFSAPHTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGeRPRRIDWMVPEAHRQNCRKKGKKEAECHNFIRILaI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  191 VAGRKVFMCGTNAFSPMCTSRQVGNLsRTIEKI-NGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSG 269
Cdd:cd11261   81 ANASHLLTCGTFAFDPKCGVIDVSSF-QQVERLeSGRGKCPFEPAQRSAAIMAG-GVLYAATVKNFLGTEPIISRAVGRA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  270 PPLRTAQYNSKWLNEPNFVAAYDIGLFA----------YFFLRENAVEHDCGRTV-YSRVARVCKNDVGGRFLLEDTWTT 338
Cdd:cd11261  159 EEWIRTETLPSWLNAPAFVAAVFLSPAEwgdedgddeiYFFFTETAREYDSYERIkVPRVARVCAGDLGGRKTLQQRWTT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  339 FMKARLNCSRP--GEVpfyYNELQSAFHLPEQD-----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRA 411
Cdd:cd11261  239 FLKADLLCPGPehGRA---SSILQDVTTLRPLPgagtpIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  412 AWLPIA-NPIPNFQCGT-------LPETGPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQA-K 482
Cdd:cd11261  316 RGLPVMdSDVPQPRPGEcitnnmkLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAAHRVTSlS 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982767  483 DTLYHVLYIGTESGTILKALSTASR-SLhgcyLEELHVLPpgRREPLRSLRILHSarALFVGLRDGVLRVP 552
Cdd:cd11261  396 GKEYDVLYLGTEDGHLHRAVRIGAQlSV----LEDLALFP--EPQPVENLQLHHN--WLLVGSDTEVTQIN 458
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
125-554 8.20e-62

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: 216.30  E-value: 8.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  125 DFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQAT-----EWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK--VF 197
Cdd:cd09295    1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLSCispelNFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGDLdiLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTNAFSPMCtsrqvGNLSRTIEKING-------VARCPYDPRHNSTAVISSqGELYAATVIDF-SGRDPAIYRSLGSG 269
Cdd:cd09295   81 VCGSNAAQPSC-----GSYRLDVLVELGkvrwpsgRPRCPIDNKHSNMGVNVD-SKLYSATDHDFkDGDRPALSRRSSNV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  270 PPLRTAQYNSKWLNEPNFVAAYDIGL---FAYFFLRENAVEHDCGRTVY-SRVARVCKNDVGGRFLLEDTWTTFMKARLN 345
Cdd:cd09295  155 HYLRIVVDSSTGLDEITFVYAFVSGDdddEVYFFFRQEPVEYLKKGMVYvPRIARVCKLDVGGCHRLKKKLTSFLKADLN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  346 CSRPGEvPFYYNELQSAFHL---PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENpraawlpianpipn 422
Cdd:cd09295  235 CSRPQS-GFAFNLLQDATGDtknLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVFDDPVEAINN-------------- 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  423 fqcgtlpetgpnenlterslqdaqRLFLMSeavqpvtpepcvTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKAL 502
Cdd:cd09295  300 ------------------------RPLYAH------------QNQRSRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKAL 343
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 91982767  503 S-TASRSLHgcYLEELHVLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPLE 554
Cdd:cd09295  344 AfFFLYKGH--IIEEWKVFKDS--SRITNLDLSRPPLYLYVGSESGVLGVPVQ 392
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
359-535 1.31e-55

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: 190.94  E-value: 1.31e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767    359 LQSAFHLPE------QDLIYGVFTTN-VNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPET 431
Cdd:pfam01403    1 LQDVFVLKPgagdalDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767    432 GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHg 511
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEESH- 159
                          170       180
                   ....*....|....*....|....
gi 91982767    512 cYLEELHVLPPGrrEPLRSLRILH 535
Cdd:pfam01403  160 -IIEEIQVFPEP--QPVLNLLLSS 180
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
131-554 2.69e-48

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: 178.12  E-value: 2.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  131 LDPSGNQLIVGARNYLFRLSLANVSLLQatEWASSEDTRRSCQSKGkTEEECQNYVRVLIVAGRKVFMCGTNAFSPMCTs 210
Cdd:cd11243    9 HEAGSSSVYVGGQGALYLLDFTGSAVIV--KKIPDEKTEKDCKKRA-TLDDCENYITLIKKLDYRLLVCGTNAGSPKCW- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  211 RQVGNLSRTIEKINGVArcPYDPRHNStAVISSQGELYAAtvIDFSGRDPAIYRSLGSGPPLRTAqynSKWLNEPNFVAA 290
Cdd:cd11243   85 FLVNQTLVTLSADRGVA--PFLPDENS-LVLIEGNNVYST--ISGKKGNIPRFRRYGGKKELYTS---DTVMQKPQFVKA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  291 --------YDIGLfaYFFLREnaVEHDCGRTV---YSRVARVCKNDVGGRFLLE-DTWTTFMKARLNCSRPGEvPFYYNE 358
Cdd:cd11243  157 tllpedeqYQDKI--YYFFRE--DNEDKGPEAepnISRVARLCKEDQGGTSSLStSKWSTFLKARLVCGDPAT-PMNFNR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  359 LQSAFHLP----EQDLIYGVFTTNVNSiaaSAVCAFNLSAISQAFngpfryqenpRAAWLPIAN-PIPNFQCGT-LPetg 432
Cdd:cd11243  232 LQDVFLLPkeewREAVVYGVFSNTWGS---SAVCSYSLGDIDKVF----------RTSSLKGYSgSLPNPRPGTcVP--- 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  433 PNENLTERSLQDAQRLFLMSEAVQPVTPEPC-VTQDSVRFSHLVVDLVQAKDTL-YHVLYIGTESGTILKALSTASRSLH 510
Cdd:cd11243  296 PEQTHPSETFSFADEHPELDDRIEPDEPRKLpVFQNKDHYQKVVVDEVRASDGVsYDVLYLATDKGKIHKVVESKGQTHN 375
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 91982767  511 gcyleeLHVLPPGRR-EPLRSLRILHSARALFVGLRDGVLRVPLE 554
Cdd:cd11243  376 ------IMEIQPFKEqEPIQSMILDAERSHLYVGTKAEVTRLPLD 414
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
856-908 1.93e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.93e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     856 WAAWGPWSSCSRDCELGFRVRKRTCTNPEPRNGGLPCVGDAAEYQDCNPQACP 908
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
913-965 1.07e-14

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: 69.15  E-value: 1.07e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     913 WSCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDICLGLHTEEALCATQACP 965
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
667-720 3.37e-14

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: 68.00  E-value: 3.37e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 91982767     667 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRHGGRICVGKSREERFCNENtPCP 720
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
129-400 4.73e-12

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: 69.28  E-value: 4.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  129 LALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRR----SCQSKGKTEEECQNYVRVLIV--AGRKVFMCGTn 202
Cdd:cd11236    5 LAVDNSTGRVYVGAVNRLYQLD-SSLLLEAEVSTGPVLDSPLclppGCCSCDHPRSPTDNYNKILLIdySSGRLITCGS- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  203 AFSPMCTSRQVGNLSRTIEKI--NGVARCPYDprhnSTAVISSQGE------LYAATVIDFSGRDPAIY----RSLGSGP 270
Cdd:cd11236   83 LYQGVCQLRNLSNISVVVERSstPVAANDPNA----STVGFVGPGPynnenvLYVGATYTNNGYRDYRPavssRSLPPDD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  271 PLRTAQYN--SKWLNEPNFVAAYDI--------GLFAYFFLRENAVeHDCGRTVYSRVARVCKNDvgGRFLledtwtTFM 340
Cdd:cd11236  159 DFNAGSLTggSAISIDDEYRDRYSIkyvygfssGGFSYFVTVQRKS-VDDESPYISRLVRVCQSD--SNYY------SYT 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982767  341 KARLNC-SRPGEVpfyYNELQSAF-------------HLPEQDLIYGVFTTNVNSIAA----SAVCAFNLSAISQAFN 400
Cdd:cd11236  230 EVPLQCtGGDGTN---YNLLQAAYvgkagsdlarslgISTDDDVLFGVFSKSKGPSAEpsskSALCVFSMKDIEAAFN 304
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
725-771 2.47e-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: 56.83  E-value: 2.47e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 91982767     725 WASWGSWSKCSSNCGGGMQSRRRACEN------GNSCLGCGVEFKTCNPEGCP 771
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
555-602 1.56e-08

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 51.94  E-value: 1.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91982767    555 RCAAYRSQGACLGARDPYCGWDGKQQRCST----LEDSSNMSLWTQNITACP 602
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
859-907 1.76e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 1.76e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 91982767    859 WGPWSSCSRDCELGFRVRKRTCTNPEPrnGGLPCVGDAAEYQDCNPQAC 907
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
126-583 1.84e-08

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


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 58.40  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  126 FSQLALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRrSC------QSKGKTEEECQNYVRVLIV--AGRKVF 197
Cdd:cd11272   13 FNHLTVHQSTGAVYVGAINRVYKLS-GNLTILVAHKTGPEEDNK-SCypplivQPCSEVLTLTNNVNKLLIIdySENRLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  198 MCGTnAFSPMCTSRQVGNLSRTIEKINgvARCPYDPRHNSTA-----VISSQGE---LYAATVIDfsGRD---PAIY-RS 265
Cdd:cd11272   91 ACGS-LYQGVCKLLRLDDLFILVEPSH--KKEHYLSSVNKTGtmygvIVRSEGEdgkLFIGTAVD--GKQdyfPTLSsRK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  266 LGSGPPLRT-------AQYNSKWLNEPN----FVAAYDI--------GLFAYFFL-----RENAVEHDCGRTVY-SRVAR 320
Cdd:cd11272  166 LPRDPESSAmldyelhSDFVSSLIKIPSdtlaLVSHFDIfyiygfasGNFVYFLTvqpetPEGVSINSAGDLFYtSRIVR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  321 VCKNDvggrflleDTWTTFMKARLNCSRPGEvpfYYNELQSAFH-------------LPEQDLIYGVFTTNVNSIAA--- 384
Cdd:cd11272  246 LCKDD--------PKFHSYVSLPFGCVRGGV---EYRLLQAAYLskpgevlarslniTAQEDVLFAIFSKGQKQYHHppd 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  385 -SAVCAFNLSAISQAFNGPFR--YQE--NPRAAWL----------PIanPIPNFQCGTlpetGPNENLTERSLQDAQRLF 449
Cdd:cd11272  315 dSALCAFPIRAINAQIKERLQscYQGegNLELNWLlgkdvqctkaPV--PIDDNFCGL----DINQPLGGSTPVEGVTLY 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  450 lmseavqpvtpepcvTQDSVRFSHLVVDLVQAkdtlYHVLYIGTESGTILKAlsTASRSLHGCYLEELHVLPPGRREPLR 529
Cdd:cd11272  389 ---------------TSSRDRLTSVASYVYNG----YSVVFVGTKSGKLKKI--RADGPPHGGVQYEMVSVFKDGSPILR 447
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 91982767  530 SLRILHSARALFVGLRDGVLRVPLERCAAYRSQGACLGARDPYCGWDGKQQRCS 583
Cdd:cd11272  448 DMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDPHCGWCALHNMCS 501
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
127-554 5.31e-08

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


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 56.71  E-value: 5.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  127 SQLALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRRsCqSKGKTEEECQ------NYVRVLIV--AGRKVFM 198
Cdd:cd11276    9 NHLVVDPQTGRVYLGAVNALYQLD-ADLQLESRVETGPKKDNKK-C-TPPIEENQCTeakmtdNYNKLLLLdsANKTLVV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  199 CGTnAFSPMCTSRQVGNLSRTIEKINGVARCPY----DPRHNSTAVISSQ----------GELYA--------ATVIDFS 256
Cdd:cd11276   86 CGS-LFKGICSLRNLSNISEVIYYSDTSGEKSFvasnDEGVSTVGLISSLkpgndrvffvGKGNGsndngkiiSTRLLQN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  257 GRDPAIYRSLGSGPPLRTAqYNSKWLNepNFVAAYDIGLFAYFFLRENAVEHDCGRTVysrVARVCKNDVGgrflledtW 336
Cdd:cd11276  165 YDDREVFENYIDAATVKSA-YVSRYTQ--QFRYAFEDNNYVYFLFNQQLGHPDKNRTL---IARLCENDHH--------Y 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  337 TTFMKARLNCSRPGEVpfyYNELQSAF-HLPEQDL-------------IYGVFTTNVNSIAASAVCAFNLSAISQafngp 402
Cdd:cd11276  231 YSYTEMDLNCRDGANA---YNKCQAAYvSTPGKELaqnygnsilsdkvLFAVFSRDEKDSGESALCMFPLKSINA----- 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  403 fRYQENPRAAWLPIANPIPNFQcgtLPETGPNENLTERSLQDAQRLFLM-SEAVqpvtPEPCVTQDSVRFSHLVvdLVQA 481
Cdd:cd11276  303 -KMEANREACYTGTIDDRDVFY---KPFHSQKDIICGSHQQKNSKSFPCgSEHL----PYPLGSRDELALTAPV--LQRG 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  482 KDTL----------YHVLYIGTESGTILK-ALSTASrslhgcylEELHVLPPGRREPL-RSLRILHSARALFVGLRDGVL 549
Cdd:cd11276  373 GLNLtavtvavengHTVAFLGTSDGRILKvHLSPDP--------EEYNSILIEKNKPVnKDLVLDKTLEHLYIMTEDKVF 444

                 ....*
gi 91982767  550 RVPLE 554
Cdd:cd11276  445 RLPVQ 449
Sema_plexin_B3 cd11277
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of ...
118-398 9.43e-08

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: 55.97  E-value: 9.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  118 FTYPGARdFSQLALDPSGNQLIVGARNYLFRLSlanvSLLQATEWASS---EDT--------RRSCQSKGKTEeecqNYV 186
Cdd:cd11277    1 FSAPNAT-FNHLALDPGSGTLYVGAVNRLYQLS----PDLQLLGEAVTgpvLDSpdclpfrdPADCPQARLTD----NAN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  187 RVLIVAGR--KVFMCGTnAFSPMCTSRQVGNLS----RTIEKINGVARCPYDPRHNSTAVISSQGE---LYAA---TVID 254
Cdd:cd11277   72 KLLLVSERagELVACGQ-VRQGVCEKRRLGNVAqvlyQAEDPGDGQFVAANDPGVATVGLVVEAPGrdlLLVGrglTGKL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  255 FSGRDPAIYRSLGSGPPLRT-----------AQYNSkwlnepNFVAAYDIGLFAYFFLRENAVEhdcGRTVY-SRVARVC 322
Cdd:cd11277  151 SAGIPPLTIRQLAGAQAFSSeglgklvvgdfSDYNN------SYVGAFAHNGYVYFLFRRRGAR---AQAEYrTYVARVC 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  323 KNDVggrFLLedtwtTFMKARLNCsRPGevpfyYNELQSAFHLPEQDLIYGVFTTNVNSIAA----SAVCAFNLSAISQA 398
Cdd:cd11277  222 LGDT---NLY-----SYVEVPLVC-QGG-----YNLAQAAYLAPGQGTLFVVFAAGQGSTPTptdqTALCAYPLVELDSA 287
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
668-719 5.19e-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: 47.27  E-value: 5.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 91982767    668 TPWSSWALCSTSCGIGFQVRQRSCSNPaPRHGGRICVGKSrEERFCNENtPC 719
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL-ERRPCNLP-PC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
858-907 5.30e-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: 47.27  E-value: 5.30e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 91982767    858 AWGPWSSCSRDCELGFRVRKRTCTNPePRNGGLPCvGDAAEYQDCNPQAC 907
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
668-714 6.87e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 6.87e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 91982767    668 TPWSSWALCSTSCGIGFQVRQRSCSNPAPrhGGRICVGKSREERFCN 714
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACK 45
TSP_1 pfam00090
Thrombospondin type 1 domain;
728-770 7.15e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 7.15e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 91982767    728 WGSWSKCSSNCGGGMQSRRRAC----ENGNSCLGCGVEFKTCNPEGC 770
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
555-592 3.83e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 44.84  E-value: 3.83e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 91982767     555 RCAAYRSQGACLGARDPYCGWDGKQQRCSTLEDSSNMS 592
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRR 38
TSP_1 pfam00090
Thrombospondin type 1 domain;
914-964 4.66e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 4.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 91982767    914 SCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEdiCLGLHTEEALCATQAC 964
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEP--CTGDDIETQACKMDKC 49
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
126-433 5.33e-06

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


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 50.31  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  126 FSQLALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRRSCQSKGKTE----EECQNYVRVLIVAGRK--VFMC 199
Cdd:cd11245    2 INHLAQDPQTGRLYLGAVNGLFQLS-PNLQLESRADTGPKKDSPQCLPPITAAEcpqaKETDNFNKLLLVNSANgtLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  200 GTnAFSPMCTSRQVGNLSRTIEKINGVARCPY----DPRHNSTAVISSQGelyAATVIDFSGRDpaiYRSLGSG--PPLR 273
Cdd:cd11245   81 GS-LFQGVCELRNLNSVNKPLYRPETPGDKQYvaanEPSVSTVGLISYFK---DGLSLLFVGRG---YTSSLSGgiPPIT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  274 TAQynskwLNEP------------------------NFVAAYDIGLFAYF-FLRENAVEHDCGRTVysrVARVCKNDvgg 328
Cdd:cd11245  154 TRL-----LQEHgemdafsneveaklvvgsasryhhDFVYAFADNGYIYFlFSRRPGTADSTKRTY---ISRLCEND--- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982767  329 rflleDTWTTFMKARLNCSrpGEVPFYYNELQSAFHLP-----EQDLIYGVFTTNVNSIAA----SAVCAFNLSAISQAF 399
Cdd:cd11245  223 -----HHYYSYVELPLNCT--VNQENTYNLVQAAYLAKpgkvlNGKVLFGVFSADEASTAApdgrSALCMYPLSSVDARF 295
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 91982767  400 N--------GPFRYQENPRAAWLPIANpipNFQCGTLPETGP 433
Cdd:cd11245  296 ErtrescytGEGLEDDKPETAYIEYNV---KSICKTLPDKNV 334
TSP_1 pfam00090
Thrombospondin type 1 domain;
969-1010 4.25e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 4.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 91982767    969 SPWSEWSKCT---DDGAQSRSRHCEELLPGSSACAGNSSQSRPCP 1010
Cdd:pfam00090    1 SPWSPWSPCSvtcGKGIQVRQRTCKSPFPGGEPCTGDDIETQACK 45
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
968-1009 1.77e-04

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: 40.26  E-value: 1.77e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 91982767     968 WSPWSEWSKCT---DDGAQSRSRHCEELLP--GSSACAGNSSQSRPC 1009
Cdd:smart00209    1 WSEWSEWSPCSvtcGGGVQTRTRSCCSPPPqnGGGPCTGEDVETRAC 47
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
728-770 4.17e-04

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.18  E-value: 4.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 91982767    728 WGSWSKCSSNCGGGMQSRRR-----ACENGNSC--LgcgVEFKTCNPEGC 770
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRtvivePQNGGRPCpeL---LERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
916-964 4.43e-04

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.18  E-value: 4.43e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 91982767    916 WTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDiClGLHTEEALCATQAC 964
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVEPQNGGRP-C-PELLERRPCNLPPC 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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