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Conserved domains on  [gi|2217344491|ref|XP_047304311|]
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semaphorin-5B isoform X11 [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 ...
60-496 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: 966.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 139
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 219
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  220 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 299
Cdd:cd11264    161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  300 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNENL 379
Cdd:cd11264    241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  380 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 459
Cdd:cd11264    321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2217344491  460 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 496
Cdd:cd11264    401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
798-850 1.95e-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: 1.95e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   798 WAAWGPWSSCSRDCELGFRVRKRTCTNPEPRNGGLPCVGDAAEYQDCNPQACP 850
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
855-907 1.10e-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: 1.10e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   855 WSCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDICLGLHTEEALCATQACP 907
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
609-662 3.54e-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: 67.61  E-value: 3.54e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217344491   609 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRHGGRICVGKSREERFCNENtPCP 662
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
667-713 2.58e-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: 2.58e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   667 WASWGSWSKCSSNCGGGMQSRRRACEN------GNSCLGCGVEFKTCNPEGCP 713
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
497-544 1.80e-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: 51.55  E-value: 1.80e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  497 RCAAYRSQGACLGARDPYCGWDGKQQRCST----LEDSSNMSLWTQNITACP 544
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
911-952 3.75e-05

Thrombospondin type 1 domain;


:

Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 3.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217344491  911 SPWSEWSKCT---DDGAQSRSRHCEELLPGSSACAGNSSQSRPCP 952
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 ...
60-496 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: 966.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 139
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 219
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  220 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 299
Cdd:cd11264    161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  300 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNENL 379
Cdd:cd11264    241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  380 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 459
Cdd:cd11264    321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2217344491  460 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 496
Cdd:cd11264    401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema smart00630
semaphorin domain;
68-467 2.26e-133

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 409.07  E-value: 2.26e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491    68 FSQLALDPSGNQLIVGARNYLFRLSLANVSLL-QATEWASSEDTRRSCQSKGKTE-EECQNYVRVLI-VAGRKVFMCGTN 144
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   145 AFSPMCTSRQVgnlsrtiekingvarcpydprhnstavissqGELYAATVIDFSGRDPAIYRSLG-------SGPPLRTA 217
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSLRTV 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   218 QYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPF 296
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   297 YYNELQSAFHLPE----QDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN-PIPNFQCGTLP 371
Cdd:smart00630  210 YFNELQAAFLLPPgsesDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   372 ETGPN-ENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAkDTLYHVLYIGTESGTILKALSTAS 448
Cdd:smart00630  290 NKPPSsKDLPDETLNFIKSHPLMDEVVQPLTGRPLFvkTDSNYLLTSIAVDRVAT-DGNYTVLFLGTSDGRILKVVLSES 368
                           410       420
                    ....*....|....*....|
gi 2217344491   449 R-SLHGCYLEELHVLPPGRR 467
Cdd:smart00630  369 SsSSESVVLEEISVFPDGSP 388
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
301-477 1.16e-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: 1.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  301 LQSAFHLPE------QDLIYGVFTTN-VNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPET 373
Cdd:pfam01403    1 LQDVFVLKPgagdalDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  374 GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHg 453
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEESH- 159
                          170       180
                   ....*....|....*....|....
gi 2217344491  454 cYLEELHVLPPGrrEPLRSLRILH 477
Cdd:pfam01403  160 -IIEEIQVFPEP--QPVLNLLLSS 180
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
798-850 1.95e-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: 1.95e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   798 WAAWGPWSSCSRDCELGFRVRKRTCTNPEPRNGGLPCVGDAAEYQDCNPQACP 850
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
855-907 1.10e-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: 1.10e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   855 WSCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDICLGLHTEEALCATQACP 907
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
609-662 3.54e-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: 67.61  E-value: 3.54e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217344491   609 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRHGGRICVGKSREERFCNENtPCP 662
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
667-713 2.58e-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: 2.58e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   667 WASWGSWSKCSSNCGGGMQSRRRACEN------GNSCLGCGVEFKTCNPEGCP 713
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
801-849 1.58e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 1.58e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217344491  801 WGPWSSCSRDCELGFRVRKRTCTNPEPrnGGLPCVGDAAEYQDCNPQAC 849
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
497-544 1.80e-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: 51.55  E-value: 1.80e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  497 RCAAYRSQGACLGARDPYCGWDGKQQRCST----LEDSSNMSLWTQNITACP 544
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
610-661 4.86e-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: 4.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  610 TPWSSWALCSTSCGIGFQVRQRSCSNPaPRHGGRICVGKSrEERFCNENtPC 661
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL-ERRPCNLP-PC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
670-712 6.31e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 6.31e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217344491  670 WGSWSKCSSNCGGGMQSRRRAC----ENGNSCLGCGVEFKTCNPEGC 712
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
497-534 3.88e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 44.84  E-value: 3.88e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217344491   497 RCAAYRSQGACLGARDPYCGWDGKQQRCSTLEDSSNMS 534
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRR 38
TSP_1 pfam00090
Thrombospondin type 1 domain;
856-906 4.11e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 4.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217344491  856 SCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEdiCLGLHTEEALCATQAC 906
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEP--CTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
911-952 3.75e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 3.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217344491  911 SPWSEWSKCT---DDGAQSRSRHCEELLPGSSACAGNSSQSRPCP 952
Cdd:pfam00090    1 SPWSPWSPCSvtcGKGIQVRQRTCKSPFPGGEPCTGDDIETQACK 45
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
910-951 1.79e-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: 1.79e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2217344491   910 WSPWSEWSKCT---DDGAQSRSRHCEELLP--GSSACAGNSSQSRPC 951
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 ...
60-496 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: 966.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 139
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 219
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  220 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 299
Cdd:cd11264    161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  300 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNENL 379
Cdd:cd11264    241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  380 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 459
Cdd:cd11264    321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2217344491  460 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 496
Cdd:cd11264    401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
60-496 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: 733.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 139
Cdd:cd11241      1 FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSVEECQNYVRVLLVVGKNLF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 219
Cdd:cd11241     81 TCGTYAFSPVCTIRKLSNLTQILDTISGVARCPYSPAHNSTALISASGELYAGTVYDFSGRDPAIYRSLGGKPPLRTAQY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  220 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYY 298
Cdd:cd11241    161 NSKWLNEPNFVGSYEIGNHTYFFFRENAVEHqDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGEFPFYY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  299 NELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPETGPNEN 378
Cdd:cd11241    241 NEIQGTFYLPETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPTPNPHPNFQCTTSIDRGQPAN 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  379 LTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDT-LYHVLYIGTESGTILKALSTaSRSLHGCYLE 457
Cdd:cd11241    321 TTERDLQDAQKYQLMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRGTqLVHIFYVGTDYGTILKMYQP-HRSQKSCTLE 399
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2217344491  458 ELHVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 496
Cdd:cd11241    400 EIKILPAMKGEPITSLQFLKSEKSLFVGLETGVLRIPLN 438
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
60-496 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 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 139
Cdd:cd11263      1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQY 219
Cdd:cd11263     81 TCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  220 NSKWLNEPNFVAAYDIGLFAYFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 299
Cdd:cd11263    161 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  300 ELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLpETGPNENL 379
Cdd:cd11263    241 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTM-DQGLYVNL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  380 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHGCYLEEL 459
Cdd:cd11263    320 TERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEI 399
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2217344491  460 HVLPPGRREPLRSLRILHSARALFVGLRDGVLRVPLE 496
Cdd:cd11263    400 ELFPKRQREPIRSLQILHSQSVLFVGLQEHVIKIPLK 436
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
60-494 6.95e-162

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: 485.05  E-value: 6.95e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRKVF 139
Cdd:cd11265      1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSQGELYAATVIDFSGRDPAIYRSLG--SGPPLRTA 217
Cdd:cd11265     81 ACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSSSGQLFVGSPTDFSGSDSAIYRTLGtsNKSFLRTK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  218 QYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGR-FLLEDTWTTFMKARLNCSRPGEVP 295
Cdd:cd11265    161 QYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYmNCGKVIYSRIARVCKNDVGGGtMLLKDNWTTFLKARLNCSLPGEYP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  296 FYYNELQSAFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWlpIANPIPN-FQCGTLPETG 374
Cdd:cd11265    241 FYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAW--ERVNVNHrDHFNQCSSSS 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  375 PNenlterSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAK-DTLYHVLYIGTESGTIlKALSTASRSLHG 453
Cdd:cd11265    319 SS------HLLESSRYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKiHQSVHVLYVATTGGLI-KKISVLPRTQET 391
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2217344491  454 CYLEELHVLPPGRRePLRSLRILHSARALFVGLRDGVLRVP 494
Cdd:cd11265    392 CLVEIWQPLPTPDS-PIKTMQYLKVTDSLYVGTELALMRIP 431
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
73-495 1.28e-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: 1.28e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   73 LDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGR-KVFMCGTNAFSPMCT 151
Cdd:cd11235      8 LHEDRSTLYVGARDRVYLVDLDSLYTEQKVAWPSSPDDVDTCYLKGKSKDDCRNFIKVLEKNSDdSLLVCGTNAFNPSCR 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  152 SRQVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVA 231
Cdd:cd11235     88 NYNVETFELVGKEESGRGKCPYDPDHNSTALFA-DGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWLNEPQFVG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  232 AYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSAFHLPEQ 310
Cdd:cd11235    167 AFDIGDYVYFFFREIAVEYiNCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFPFYFNELQDVFDLPSP 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  311 D----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPnfqCGTLPETGPNE--NLTERSL 384
Cdd:cd11235    247 SnkekIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDERV---PEPRPGTCVDDssPLPDDTL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  385 QDAQRLFLMSEAVQPVTPEP--CVTQDSVRFSHLVVDLVQAK-DTLYHVLYIGTESGTILKALSTASRSLHG-CYLEELH 460
Cdd:cd11235    324 NFIKSHPLMDEAVTPILNRPlfIKTDVNYRFTKIAVDRVQAKlGQTYDVLFVGTDRGIILKVVSLPEQGLQAsNILEEMP 403
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2217344491  461 VLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPL 495
Cdd:cd11235    404 VGPPP--EPIQTMQLSRKRRSLYVGSETGVLQVPL 436
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
73-498 1.48e-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: 422.13  E-value: 1.48e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   73 LDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIV--AGRkVFMCGTNAFSPMC 150
Cdd:cd11237     10 LDQDGNSLLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLAKksAGR-LLVCGTNAYKPLC 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  151 tsRQ---VGNLSRTIEKINGVARCPYDPRHNSTAViSSQGELYAATVIDFSGRDPAIYRSlgsgpPLRTAQYNSKWLNEP 227
Cdd:cd11237     89 --REytvKDGGYRVEREFDGQGLCPYDPKHNSTAV-YADGQLYSATVADFSGADPLIYRE-----PLRTERYDLKQLNAP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  228 NFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSAFH 306
Cdd:cd11237    161 NFVSSFAYGDYVYFFFRETAVEYiNCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGEYPFYFNEIQSTSD 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  307 LPE-------QDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIpnfqcgtLPETGPNENL 379
Cdd:cd11237    241 IVEggyggksAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVPSNK-------VPEPRPGQCV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  380 TE-RSLQDAQRLF-----LMSEAVQPVTPEPCVTQDSV--RFSHLVVD-LVQAKDTLYH-VLYIGTESGTILKALSTASR 449
Cdd:cd11237    314 NDsRTLPDVTVNFikshpLMDEAVPSFFGRPILVRTSLqyRFTQIAVDpQVKALDGKYYdVLFIGTDDGKVLKAVNIASA 393
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217344491  450 SLHG----CYLEELHVLPPGrrEPLRSLRILHSARA--LFVGLRDGVLRVPLERC 498
Cdd:cd11237    394 DTVDkvspVVIEETQVFPRG--VPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema smart00630
semaphorin domain;
68-467 2.26e-133

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 409.07  E-value: 2.26e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491    68 FSQLALDPSGNQLIVGARNYLFRLSLANVSLL-QATEWASSEDTRRSCQSKGKTE-EECQNYVRVLI-VAGRKVFMCGTN 144
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   145 AFSPMCTSRQVgnlsrtiekingvarcpydprhnstavissqGELYAATVIDFSGRDPAIYRSLG-------SGPPLRTA 217
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSLRTV 129
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   218 QYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCSRPGEVPF 296
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   297 YYNELQSAFHLPE----QDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN-PIPNFQCGTLP 371
Cdd:smart00630  210 YFNELQAAFLLPPgsesDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   372 ETGPN-ENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAkDTLYHVLYIGTESGTILKALSTAS 448
Cdd:smart00630  290 NKPPSsKDLPDETLNFIKSHPLMDEVVQPLTGRPLFvkTDSNYLLTSIAVDRVAT-DGNYTVLFLGTSDGRILKVVLSES 368
                           410       420
                    ....*....|....*....|
gi 2217344491   449 R-SLHGCYLEELHVLPPGRR 467
Cdd:smart00630  369 SsSSESVVLEEISVFPDGSP 388
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
60-495 2.98e-116

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: 2.98e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVS-LLQAT-EWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGR 136
Cdd:cd11240      1 FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDIStELKDKiKWEASEDKKKECANKGKDNQtDCFNFIRILQFYNS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  137 -KVFMCGTNAFSPMCT--SRQVGNLSRtIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPP 213
Cdd:cd11240     81 tHLYVCGTFAFSPRCTyiNLSDFSLSS-IKFEDGKGRCPFDPAQRYTAIMVD-GELYSATVNNFLGSEPVISRNHSEGNV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  214 LRTaQYNSKWLNEPNFV-AAY---DIGLFA------YFFLRENAVEHDCG-RTVYSRVARVCKNDVGGRFLLEDTWTTFM 282
Cdd:cd11240    159 LKT-ENTLRWLNEPAFVgSAHireSIDSPDgdddkiYFFFTETAVEYDFYeKVTVSRVARVCKGDLGGQRTLQKKWTTFL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  283 KARLNCSRPGEvPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPI 358
Cdd:cd11240    238 KAQLVCSQPDS-GLPFNVLRDVFVLSPDSwdatIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRY 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  359 ANPIPNFQ---CGTLPETGPNE----NLTERSLQDAQRLFLMSEAVQPVTpEPCVTQDSVRFSHLVVDLVQAKD-TLYHV 430
Cdd:cd11240    317 TGPVPDPRpgaCITNSARSQGItsslNLPDNVLTFVKDHPLMDEQVHPIN-RPLLVKSGVNYTRIAVHRVQALDgQTYTV 395
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217344491  431 LYIGTESGTILKALSTASRsLHgcYLEELHVLPPgrREPLRSLRILHSARALFVGLRDGVLRVPL 495
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 ...
80-495 2.06e-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: 2.06e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   80 LIVGARNYLFRLSLANVSLLQAT-----EWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMCGTNAFSPMCTSR 153
Cdd:cd11242     21 LYIAARDHVYTVDLDASHTEEIVpskklTWRSRQADVENCRMKGKHKDECHNFIKVLVPRNDEtLFVCGTNAFNPVCRNY 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  154 QVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVAAY 233
Cdd:cd11242    101 RIDTLEQDGEEISGMARCPFDAKQANVALFA-DGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYDSKWLKEPHFVHAV 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  234 DIGLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQS---AFHLP 308
Cdd:cd11242    180 EYGDYVYFFFREIAVEYNtLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPGDSHFYFDVLQAvtdVIRIN 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  309 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA-NPIPNFQCGTLPETGPNENL-TERSLQD 386
Cdd:cd11242    260 GRPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPeDRVPKPRPGCCAGSGSAEKYkTSNDFPD 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  387 AQRLF-----LMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHG--CYLE 457
Cdd:cd11242    340 DTLNFikthpLMDEAVPSIINRPWFTRTMVRYrlTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARIGPSGSNgsVFLE 419
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2217344491  458 ELHVLPP----GRREPLR---SLRILHSARALFVGLRDGVLRVPL 495
Cdd:cd11242    420 EIDVYNPakcsYDGEEDRriiGLELDRASHALFVAFSGCVIRVPL 464
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
64-498 8.38e-108

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: 8.38e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   64 GARDFSQLALDPSGNQLIVGARNYLFRLSLANVSL-LQATEWASSEDTRRSCQSKGKT-EEECQNYVRVLIVAGRK-VFM 140
Cdd:cd11239      6 NSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQdPKKIYWPASPERIEECKMAGKDpNTECANFVRVLQPYNRThLYA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  141 CGTNAFSPMCTSRQVGN---------LSRTIEkiNGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSG 211
Cdd:cd11239     86 CGTGAFHPICAFINVGRrledpifklDDSSLE--SGRGKCPFDPNQPFASVLID-GELYSGTAIDFMGRDAAIFRSLGHR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  212 PPLRTAQYNSKWLNEPNFVAAYDI-------GLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMK 283
Cdd:cd11239    163 HYIRTEQYDSRWLNEPKFVGAYLIpdsdnpdDDKVYFFFREKAVEAEgSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  284 ARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLP 357
Cdd:cd11239    243 ARLVCSVPGPdgIDTYFDELEDVFLLPTRDpknpLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVE 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  358 IANPIPNFQCGTLPE--TGPNENLTeRSLQD-----AQRLFLMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLY 428
Cdd:cd11239    323 YQGKVPYPRPGTCPSktYGPLYKST-KDFPDdvisfARSHPLMYNPVYPLHGRPLLIRTNVpyRLTQIAVDRVEAEDGQY 401
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  429 HVLYIGTESGTILK--ALSTASRSLHGCYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11239    402 DVLFIGTDSGTVLKvvSLPKENWEMEEVILEELQVFK--HPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
68-490 6.92e-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: 333.62  E-value: 6.92e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   68 FSQLALDPSGNQLIVGARNYLFRLSLANVS----LLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVA--GRKVFM 140
Cdd:cd11238      3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINdtgnNCARDELTLSPSDVSECVSKGKDEEyECRNHVRVIQPMgdGQTLYV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  141 CGTNAFSPmcTSRQV-GNLSRTIEKI----NGVARCPYDPRHNSTAVISSQGE------LYAATVIDFSGRDPAIYRslg 209
Cdd:cd11238     83 CSTNAMNP--KDRVLdANLLHLPEYVpgpgNGIGKCPYDPDDNSTAVWVEWGNpgdlpaLYSGTRTEFTKANTVIYR--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  210 sgPPL------------RTAQYNSKWLNEPNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGRFLLED 276
Cdd:cd11238    158 --PPLynntkgrhesfmRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETAVEYiNCGKVVYSRVARVCKKDTGGKNVLRQ 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  277 TWTTFMKARLNCSRPGEVPFYYNELQSAFHLPEQD--LIYGVFTTNVNSIAASAVCAFNLSAISQAFN-GPFRYQENPRA 353
Cdd:cd11238    236 NWTTFLKARLNCSISGEFPFYFNEIQSVYKVPGRDdtLFYATFTTSENGFTGSAVCVFTLSDINAAFDtGKFKEQASSSS 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  354 AWLPI-ANPIPNFQCGTLpeTGPNENLTERSLQDAQRLFLMSEAVQpvTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLY 432
Cdd:cd11238    316 AWLPVlSSEVPEPRPGTC--VNDSATLSDTVLHFARTHPLMDDAVS--HGPPLLYLRDVVFTHLVVDKLRIDDQEYVVFY 391
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217344491  433 IGTESGTILKALSTASRS-LHGCYLEELHVLPPgrrEPLRSLRILHsARALFVGLRDGV 490
Cdd:cd11238    392 AGSNDGKVYKIVHWKDAGeSKSNLLDVFELTPG---EPIRAMELLP-GEFLYVASDHRV 446
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
78-495 7.11e-100

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: 7.11e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   78 NQLIVGARNYLFRLSLANVSLLQAT-----EWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMCGTNAFSPMCT 151
Cdd:cd11269     19 DTLYIAGRDQVYTVNLNEVPKTEVTpsrklTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEmVFVCGTNAFNPMCR 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  152 SRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVA 231
Cdd:cd11269     99 YYRLSTLEYDGEEISGLARCPFDARQTNVALFAD-GKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLH 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  232 AYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSAFHLPE 309
Cdd:cd11269    178 AIEYGNYVYFFFREIAVEHnNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFFYFDVLQSITDIIE 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  310 QD---LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA-NPIPNFQCGTLPETGPNE------NL 379
Cdd:cd11269    258 INgipTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPeDKVPKPRPGCCAKHGLAEayktsiDF 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  380 TERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALS-TASRSLH-GCY 455
Cdd:cd11269    338 PDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYrlTAIAVDHAAGPHQNYTVIFVGSEAGVVLKILAkTSPFSLNdSVL 417
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2217344491  456 LEEL----HVLPPGRREPLRSLRILHSAR---ALFVGLRDGVLRVPL 495
Cdd:cd11269    418 LEEIeaynHAKCSAENEEDRRVISLQLDRdhhALFVAFSSCVVRIPL 464
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
80-495 4.97e-97

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: 4.97e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   80 LIVGARNYLFRLSLANVS-----LLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMCGTNAFSPMCTSR 153
Cdd:cd11267     21 LYIGDRDNLYRVELDPTAgtemrYHKKLTWRSNKNDINVCRMKGKHEGECRNFIKVLLLRDYGtLFVCGTNAFNPVCANY 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  154 QVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVAAY 233
Cdd:cd11267    101 SIDTLEPVGDNISGMARCPYDPKHANVALFA-DGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEPYFVHAV 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  234 DIGLFAYFFLRENAVE-HDCGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSA---FHLP 308
Cdd:cd11267    180 EWGSHVYFFFREIAMEfNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVsdiLNLG 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  309 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN---PIPNFQCGTLPETGPNenlTERSLQ 385
Cdd:cd11267    260 GRPVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEelvPRPRPGCCAAPGMRYN---SSSTLP 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  386 DAQRLF-----LMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKAL-----STASRSLHG 453
Cdd:cd11267    337 DEVLNFvkthpLMDEAVPSLGHAPWIVRTMTRYqlTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLiipnaSSSEISNQS 416
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217344491  454 CYLEELHVLPPGR--------REPLrSLRILHSARALFVGLRDGVLRVPL 495
Cdd:cd11267    417 VFLEELETYNPERcgwdspqaQKLL-SLELDKGSGGLLLAFPSCVVRVPV 465
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
68-498 1.49e-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: 1.49e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   68 FSQLALDPSGNQLIVGARNYLFRLSLANVSLL-QATEWASSEDTRRSCQSKGK-TEEECQNYVRVLIVAGRK-VFMCGTN 144
Cdd:cd11250     10 YDALLLDEERGRLFVGAKNYLASLSLDNISKQeKKIYWPAPVEWREECNWAGKdINTDCMNYVKILHHYNRThLYACGTG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  145 AFSPMCTSRQVGN-LSRTIEKIN------GVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSLGSGPPLRTA 217
Cdd:cd11250     90 AFHPTCAFVEVGQrMEDHVFRLDpsrvedGKGKSPYDPRHTAASVLVGD-ELYSGVATDLMGRDFTIFRSLGQRPSLRTE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  218 QYNSKWLNEPNFVAAYDIGLF-------AYFFLRENAVE-HDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLNCS 289
Cdd:cd11250    169 QHDSRWLNEPKFVKVFWIPESenpdddkIYFFFRETAVEaAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCS 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  290 RPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIP 363
Cdd:cd11250    249 VPGNegGDTHFDELRDVFLLQTRDkrnpLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGKVP 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  364 NFQCGTLPET-----GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLYHVLYIGTE 436
Cdd:cd11250    329 YPRPGMCPSKtfgsfESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIpyTFTQIAVDRVAAADGHYDVMFIGTD 408
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217344491  437 SGTILKALSTASRSLH---GCYLEELHVLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11250    409 VGSVLKVISVPKGSWPsneELLLEELHVFKDS--SPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
63-498 2.66e-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: 2.66e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   63 PGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGK-TEEECQNYVRVLIVAGRK-VFM 140
Cdd:cd11249     27 ANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKWAGKdILKECANFIKVLKAYNQThLYA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  141 CGTNAFSPMCTSRQVGNLSR-TIEKI------NGVARCPYDPRHnSTAVISSQGELYAATVIDFSGRDPAIYRSLGSGPP 213
Cdd:cd11249    107 CGTGAFHPVCTYIEVGHHPEdNIFRLedshfeNGRGKSPYDPKL-LTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHP 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  214 LRTAQYNSKWLNEPNFVAAYDIGLF-------AYFFLRENAV--EHdCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKA 284
Cdd:cd11249    186 IRTEQHDSRWLNDPRFISAHLIPESdnpeddkIYFFFRENAIdgEH-TGKATHARIGQLCKNDFGGHRSLVNKWTTFLKA 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  285 RLNCSRPGE--VPFYYNELQSAFHL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPI 358
Cdd:cd11249    265 RLICSVPGPngIDTHFDELQDVFLMnskdPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPF 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  359 ANPIPNFQCGTLPETGPNENLTERSLQDAQRLF-----LMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLYHVL 431
Cdd:cd11249    345 QGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFarshpAMYNPVFPINNRPIIIKTDVdyQFTQIVVDRVEAEDGQYDVM 424
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  432 YIGTESGTILKALSTASRSLHG---CYLEELHVLppgrREP--LRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11249    425 FIGTDMGTVLKVVSIPKETWHDleeVLLEEMTVF----REPtaISAMELSTKQQQLYIGSAIGVSQLPLHRC 492
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
80-495 1.67e-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: 1.67e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   80 LIVGARNYLFRLSL-----ANVSLLQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGR-KVFMCGTNAFSPMCTSR 153
Cdd:cd11266     21 LYIAARDHIYTVDIdtshtEEIYFSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKRNDdTLFVCGTNAFNPSCRNY 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  154 QVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNEPNFVAAY 233
Cdd:cd11266    101 KMDTLEFFGDEFSGMARCPYDAKHANVALFA-DGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAV 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  234 DIGLFAYFFLRENAVE-HDCGRTVYSRVARVCKNDVGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQS---AFHLP 308
Cdd:cd11266    180 DYGDYIYFFFREIAVEyNSMGKVVFPRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQAvtdVIHIN 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  309 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN---PIPNFQC----GTLPETGPNENLTE 381
Cdd:cd11266    260 GRDVVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDervPKPRPGCcagsSSLEKYATSNEFPD 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  382 RSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRS--LHGC-YL 456
Cdd:cd11266    340 DTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYrlTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARTGNSgfLNDSlFL 419
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2217344491  457 EELHVLPPGR--REPLRSLRIL-----HSARALFVGLRDGVLRVPL 495
Cdd:cd11266    420 EEMNVYNSEKcsYDGVEDKRIMgmqldKASSALYVAFSTCVIKVPL 465
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
67-498 2.77e-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: 2.77e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   67 DFSQLALDPSGNQLIVGARNYLFRLSLANVS---LLqaTEWASSEDTRRSCQSKGK-TEEECQNYVRVLIVAGRK-VFMC 141
Cdd:cd11254      9 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWPASPQRIEECILSGKgSNGECGNFIRLIQPWNRThLYVC 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  142 GTNAFSPMCTSRQVGNLSRTI------EKI-NGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPPL 214
Cdd:cd11254     87 GTGAYNPVCAYINRGRRAEDYmfrlepDKLeSGKGKCPYDPKQDSVSALIN-GELYAGVYIDFMGTDAAIFRTMGKQPAM 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  215 RTAQYNSKWLNEPNFVAAYDIGLFA-------YFFLRENAVEHDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKARLN 287
Cdd:cd11254    166 RTDQYNSRWLNDPAFVHAHLIPDSSeknddklYFFFREKSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLV 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  288 CSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANP 361
Cdd:cd11254    246 CSVPGAdgIETHFDELRDVFIQPTQDtknpVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGK 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  362 IPNFQCGTLP--ETGPNENLTERSLQDAQRLF----LMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLYHVLYI 433
Cdd:cd11254    326 IPYPRPGTCPggTFTPSMKSTKDYPDEVINFMrthpLMYNAVYPVHRRPLVVRTNVnyRFTTIAVDQVDAADGRYEVLFL 405
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217344491  434 GTESGTILKA--LSTASRSLHGCYLEELHVLP-PGrrePLRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11254    406 GTDRGTVQKVivLPKDDLETEELTLEEVEVFKvPA---PIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
80-495 1.26e-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: 284.69  E-value: 1.26e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   80 LIVGARNYLFRLSL--ANVSLL--QATEWASSEdtRRSCQSKGKTEEECQNYVRVLIVAGRKVFM-CGTNAFSPMCTSRQ 154
Cdd:cd11270     21 VYIAARDHVFAINLsaSLERIVpqQKLTWKTKD--VEKCTVRGKNSDECYNYIKVLVPRNDETLFaCGTNAFNPTCRNYK 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  155 VGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSGPP-LRTAQYNSKWLNEPNFVAAY 233
Cdd:cd11270     99 MSSLEQDGEEVIGQARCPFESRQSNVGLFAG-GDFYSATMTDFLASDAVIYRSLGESSPvLRTVKYDSKWLREPHFLHAI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  234 DIGLFAYFFLRENAVEHDC-GRTVYSRVARVCKNDVGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQSA---FHLP 308
Cdd:cd11270    178 EYGNYVYFFLSEIAVEYTTlGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPGDSFFYFDVLQSLtnvMQIN 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  309 EQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN---PIPNFQC----GTLPETGPNENLTE 381
Cdd:cd11270    258 HRPAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVPDeavPKPRPGScagdGPAAGYKSSTNFPD 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  382 RSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRF--SHLVVDLVQAKDTLYHVLYIGTESGTILKALS--TASRSLHGCYLE 457
Cdd:cd11270    338 ETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFklTQIAVDTAAGPYKNYTVVFLGSENGHVLKVLAsmHPNSSYSTQVLE 417
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2217344491  458 ELHVLPPG----RREPLR--SLRILHSARALFVGLRDGVLRVPL 495
Cdd:cd11270    418 DIDVYNPNkcnvRGEDRRilGLELDKDHHALFVAFTGCVIRVPL 461
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
66-498 8.32e-82

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: 8.32e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   66 RDFSQLALDPSGNQLIVGARNYLFRLSLANVSL-LQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGRK-VFMCG 142
Cdd:cd11252      8 LDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKnPKKIYWPAAKERVELCKLAGKDANtECANFIRVLHPYNRThVYVCG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  143 TNAFSPMCTSRQVGNL---------SRTIEkiNGVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSLGSGPP 213
Cdd:cd11252     88 TGAFHPTCGYIELGTHkedriflldTQNLE--SGRLKCPFDPQQPFASVMTDE-YLYAGTASDFLGKDTTFTRSLGPTPD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  214 ---LRTAQYNSKWLNEPNFVAAYDIGLF-------AYFFLRENAVEHDCG-RTVYSRVARVCKNDVGGRFLLEDTWTTFM 282
Cdd:cd11252    165 hhyIRTDISEHYWLNGAKFIGTFPIPDTynpdddkIYFFFREASQDGSTSdKSVLSRVGRVCKNDVGGQRSLINKWTTFL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  283 KARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWL 356
Cdd:cd11252    245 KARLVCSIPGPdgADTHFDELQDIFLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWV 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  357 PIANPIPNFQCGTLPETGPNENL-TERSLQD-----AQRLFLMSEAVQPVTPEPCVTQDSV--RFSHLVVDLVQAKDTLY 428
Cdd:cd11252    325 QYEGRIPYPRPGTCPSKTYDPLIkSTKDFPDevisfIKRHPLMYKSVYPLTGGPVFTRINVdyRLTQIVVDHVAAEDGQY 404
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  429 HVLYIGTESGTILKALSTASR--SLHGCYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11252    405 DVMFLGTDIGTVLKVVSITKEkwTMEEVVLEELQIFK--HPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
60-495 1.91e-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: 273.28  E-value: 1.91e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVS---LLQATEWASSEDTRRSCQSKGKT-EEECQNYVRVLI-VA 134
Cdd:cd11257      2 FEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISptgEQQELTWSADEEKKQECSFKGKDpQRDCQNYIKILLrLN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  135 GRKVFMCGTNAFSPMCTSRQVGNLSRTIEKI------NGVARCPYDPRHNSTAvISSQGELYAATVIDFSGRDPAIYRSL 208
Cdd:cd11257     82 STHLFTCGTYAFSPICTYIVMTNFSLERDEKgeplleDGKGRCPFDPEYKSTA-IMVDGELYTGTVSNFQGNDPIIYRSL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  209 GSGPPLRTAqyNS-KWLNEPNFVA-AYDIGLFA---------YFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLED 276
Cdd:cd11257    161 GSGTPLKTE--NSlNWLQDPAFVGsAYIQESLPklvgdddkiYFFFSETGKEFDFfENTIVSRIARVCKGDEGGERVLQK 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  277 TWTTFMKARLNCSRPGEvPFYYNELQSAFHLP--EQD----LIYGVFTTNVNSIAA--SAVCAFNLSAISQAFNGPFRYQ 348
Cdd:cd11257    239 RWTTFLKAQLLCSLPDD-GFPFNVLQDVFVLTpsPEDwkdtLFYGVFTSQWHKGTAgsSAVCVFTMDQVQRAFNGLYKEV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  349 ENPRAAWLPIANPIPNFQCGTLPETGPNENLTERSLQDAQRL-------FLMSeavQPVTPEPCVTQDSVRFSHLVVDLV 421
Cdd:cd11257    318 NRETQQWYTYTHPVPEPRPGACITNSARERKINSSLHMPDRVlnfvkdhFLMD---GQVRSQPLLLQPQVRYTQIAVHRV 394
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217344491  422 QAKDTLYHVLYIGTESGTILKALSTASRsLHgcYLEELHVLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPL 495
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 ...
60-495 1.25e-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: 1.25e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLAN---VSLLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLI-VA 134
Cdd:cd11256      2 FRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTpgpIRLKHQIPWPANDSKISECAFKKKSNEtECFNFIRVLVpVN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  135 GRKVFMCGTNAFSPMCTSRQVGNLS-----RTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLG 209
Cdd:cd11256     82 GTHLYTCGTYAFSPACTYIELDHFSlpppnGTIITMDGKGQSPFDPQHNYTAILVD-GELYTGTMNNFRGNEPIIFRNLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  210 SGPPLRTAQYNsKWLN-EPNFVAAYDIGLF--AYFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLEDTWTTFMKAR 285
Cdd:cd11256    161 TKVSLKTDGFL-RWLNaDAVFVASFNPQGDskVYFFFEETAREFDFfEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  286 LNCSRPGEVPFyyNELQSAFHLPEQD----LIYGVFTT--NVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA 359
Cdd:cd11256    240 LTCSQQGHFPF--NVIHHVALLNQPDpnnsVFYAVFTSqwQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYM 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  360 NPIPNFQCGTLpETGPNenlTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYH-VLYIGTESG 438
Cdd:cd11256    318 GPVSDPRPGSC-SGGKS---SDKALNFMKDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSGHNYtVMFLGTDKG 393
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217344491  439 TILKALSTASRSLHgcYLEELHVLPPgrREPLRSLRILHSARALFVGLRDGVLRVPL 495
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 ...
67-498 2.32e-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: 2.32e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   67 DFSQLALDPSGNQLIVGARNYLFRLSLANVSllQATE---WASSEDTRRSCQSKGKTEEE-CQNYVRVLIVAGRK-VFMC 141
Cdd:cd11251      9 DYRILFMDEDQDRIYVGSKDHILSLNINNIS--QDALsifWPASASKVEECKMAGKDPTHgCGNFVRVIQPYNRThLYVC 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  142 GTNAFSPMCTSRQVGNlsRTIEKI--------NGVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSLGSGPP 213
Cdd:cd11251     87 GSGAFSPVCVYVNRGR--RSEEQVfhidskaeSGKGRCSFNPNVNTVSVMINE-ELFSGMYIDFMGTDAAIFRSLTKRNA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  214 LRTAQYNSKWLNEPNFVAAYDI-------GLFAYFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKAR 285
Cdd:cd11251    164 VRTDQHNSKWLSEPIFVDAHLIpdgtdpnDAKLYFFLKERLTDNSgSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKAR 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  286 LNCSRPGE--VPFYYNELQSAFHL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA 359
Cdd:cd11251    244 LVCSVMDEdgTETHFDELEDVFLLetdnPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQ 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  360 NPIPNFQCGTLPETGPNENL-TERSLQDAQRLF-----LMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAKDTLYHVL 431
Cdd:cd11251    324 GRIPYPRPGTCPGGAFTPNMqSTKEFPDDVVTFirnhpLMFNPIYPIGRRPLLvrTGTDYKYTKIAVDRVNAADGRYHVL 403
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217344491  432 YIGTESGTILKALSTASR-SLHG-CYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11251    404 FLGTDKGTVQKVVVLPTNgSLSGeLILEELEVFK--NHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
80-495 4.26e-77

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: 261.56  E-value: 4.26e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   80 LIVGARNYLFRLSLanvsllQATE------------WASSEdtRRSCQSKGKTEEECQNYVRVLIVAGRKVFM-CGTNAF 146
Cdd:cd11268     21 LLVAARDHVFSFDL------QAEEegeglvpnkyltWRSQD--VENCAVRGKLTDECYNYIRVLVPWDSQTLLaCGTNSF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  147 SPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPPLRTAQYNSKWLNE 226
Cdd:cd11268     93 SPVCRSYGITSLQQEGEELSGQARCPFDATQSNVAIFA-EGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLRE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  227 PNFVAAYDIGLFAYFFLRENAVEH-DCGRTVYSRVARVCKNDVGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQS- 303
Cdd:cd11268    172 PHFVQALEHGDHVYFFFREVSVEDaRLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPGDSTFYFDVLQAl 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  304 --AFHLPEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIA-NPIPNFQCGTLPETGPNENL- 379
Cdd:cd11268    252 tgPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVSeDRVPSPRPGSCAGVGGAALFs 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  380 TERSLQDAQRLF-----LMSEAVQPVTPEPCVTQDS-VRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRS--L 451
Cdd:cd11268    332 SSRDLPDDVLTFikahpLLDPAVPPVTHQPLLTLTSrALLTQVAVDGMAGPHSNITVMFLGSNDGTVLKVLPPGGRSggP 411
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491  452 HGCYLEELHVLPP----GRREPLRSLRIL-----HSARALFVGLRDGVLRVPL 495
Cdd:cd11268    412 EPILLEEIDAYSParcsGKRTAQTARRIIgleldTEGHRLFVAFSGCIVYLPL 464
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
64-498 1.08e-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: 260.56  E-value: 1.08e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   64 GARDFSQLALDPSGNQLIVGARNYLFRLSLANVSL-LQATEWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK-VFMC 141
Cdd:cd11253      6 GFLDLHTMLLDEYQERLFVGGRDLLYSLSLERISAnYKEIHWPSTQLQVEDCIMKGRDKPECANYIRVLHHYNRThLLAC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  142 GTNAFSPMCTSRQVGNL---------SRTIEKinGVARCPYDPrhnSTAVISS--QGELYAATVIDFSGRDPAIYRSLGS 210
Cdd:cd11253     86 GTGAFDPVCAFIRVGRGsedhlfqleSDKFER--GRGRCPFDP---NSSFISTliGGELFVGLYSDYWGRDAAIFRTMNH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  211 GPPLRTAQYNSKWLNEPNFVAAYDI-------GLFAYFFLRENAVEHDCG-RTVYSRVARVCKNDVGGRFLLEDTWTTFM 282
Cdd:cd11253    161 LAHIRTEHDDERLLKEPKFVGSYMIpdnedpdDNKVYFFFTEKALEAEGGnHAIYTRVGRVCANDQGGQRMLVNKWSTFL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  283 KARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWL 356
Cdd:cd11253    241 KTRLICSVPGPngIDTHFDELEDVFLLRTRDnknpEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  357 PIANPIPNFQCGTLPET------GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAKDTLY 428
Cdd:cd11253    321 VYEGKVPYPRPGSCASKvngghyGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILvkTDGKYNLKQIAVDRVEAEDGQY 400
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217344491  429 HVLYIGTESGTILKALSTASR---SLHGCYLEELHVLP-PgrrEPLRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11253    401 DVLFIGTDNGIVLKVITIYNQeteTMEEVILEELQVFKvP---VPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
60-495 1.46e-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: 1.46e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQAT-EWASSEDTRRSCQSKGK-TEEECQNYVRVL-IVAGR 136
Cdd:cd11260      1 FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKvLWEVTEEKQKDCTNKGKhADIDCHNYIRILhKMNDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  137 KVFMCGTNAFSPMCTSRQVGNLSRTIEKI--NGVARCPYDPRHNSTAVISSQgELYAATVIDFSGRDPAIYRSlgSGPPL 214
Cdd:cd11260     81 RMYVCGTNAFSPTCDYISYDDGQLTLEGKqeDGKGKCPFDPFQRYSSVMVDQ-DLYSATSMNFLGSEPVIMRS--SPITI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  215 RTaQYNSKWLNEPNFVAAYDIGLFA----------YFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLEDTWTTFMK 283
Cdd:cd11260    158 RT-EFKSSWLNEPNFIYMAAVPESEdspegdddkiYLFFSETAVEYDFyNKLVVSRVARVCKGDLGGQRTLQKKWTSFLK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  284 ARLNCSRP-GEVPFYyneLQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFN-GPFRYQ---ENPRAA 354
Cdd:cd11260    237 ARLDCSVPePSLPYV---IQDVFHVCHQDwrkcVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrGKFKTPvavETSFVK 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  355 WLPIANPIPNFQCGTLPETGPNE-------NLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKD-T 426
Cdd:cd11260    314 WVMYSGELPVPRPGACINNAARTsgikkslNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADgQ 393
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217344491  427 LYHVLYIGTESGTILKALSTASRSLhgcYLEELHVLPPgrREPLRSLRIlhSARALFVGLRDGVLRVPL 495
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); ...
60-495 5.10e-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: 258.63  E-value: 5.10e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQ-ATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGRK 137
Cdd:cd11259     12 FHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNALNISEKQhELYWKVSEDKRTKCAVKGKSKQtECRNYIRVLQPLNDT 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  138 -VFMCGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLgSGPPLRT 216
Cdd:cd11259     92 fLYVCGTNAFQPTCDYLNLTSFRLLGKNEDGKGRCPFDPAQSYTSVMVD-GELYSGTSYNFLGSEPIISRNS-SQSPLRT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  217 aQYNSKWLNEPNFVAAYDIGLFA----------YFFLRENAVEHD-CGRTVYSRVARVCKNDVGGRFLLEDTWTTFMKAR 285
Cdd:cd11259    170 -EYAIPWLNEPSFVFADVIRADPdspdgeddkiYFFFTEVSVEYEfVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKAR 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  286 LNCSRPgEVPFYYNELQSAFHLPEQDL----IYGVFTTNVNSIAASAVCAFNLSAISQAFN-GPFRYQ---ENPRAAWLP 357
Cdd:cd11259    249 LICSIP-DKNLVFNVVNDVFILKSPTLkepvIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHTKWVR 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  358 IANPIPNfqcgtlPETGP---NE----------NLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAK 424
Cdd:cd11259    328 YNGEVPK------PRPGAcinNEaraanytsslNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQAL 401
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217344491  425 D-TLYHVLYIGTESGTILKALSTASrSLHgcYLEELHVLPpgRREPLRSLRIL--HSARALFVGLRDGVLRVPL 495
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 ...
64-498 2.01e-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: 257.15  E-value: 2.01e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   64 GARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLlQATE--WASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAGRK-VF 139
Cdd:cd11255      6 GDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHP-DAKEihWPPLPGQREECIRKGKDPEtECANFVRVLQPFNRThLL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCTSRQVGNLSR--------TIEkiNGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSG 211
Cdd:cd11255     85 ACGTGAFQPVCALINVGHRGEhvfsldptTVE--SGRGRCPHEPKRPFASTFTG-GELYTGLTADFLGRDSVIFRGFGTR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  212 PPLRTaQYNSKWLNEPNFVAAYDIGLFA-------YFFLRENAVE--HDCGRTVYSRVARVCKNDVGGRFLLEDTWTTFM 282
Cdd:cd11255    162 SPLRT-ETDQRLLHEPRFVAAHLIPDNAdrdndkvYFFFTERATEtaEDDDGAIHSRVGRLCANDAGGQRVLVNKWSTFI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  283 KARLNCSRPGE--VPFYYNELQSAFHLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWL 356
Cdd:cd11255    241 KARLVCSVPGPhgIQTHFDQLEDVFLLRTKDgkspEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  357 PIANPIPNFQCGTLPET---------GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCV--TQDSVRFSHLVVDLVQAKD 425
Cdd:cd11255    321 PYEGKVPYPRPGVCPSKitaqpgrafRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLvkTGLPYRLTQIVVDRVEAED 400
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217344491  426 TLYHVLYIGTESGTILKALS-TASRSLHG--CYLEELHVLP-PgrrEPLRSLRILHSARALFVGLRDGVLRVPLERC 498
Cdd:cd11255    401 GYYDVMFIGTDSGSVLKVIVlQKGNSAAGeeVTLEELQVFKvP---TPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
65-495 1.18e-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: 248.91  E-value: 1.18e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   65 ARDFSQLALDPSGNQLIVGARNYLFRLSLANVS--LLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLI-VAGRKVFM 140
Cdd:cd11262      7 AQNYSTLLLEDESGRLYVGARGAIFSLNASDISdsSALTIDWEASPEQKHQCLKKGKNNQtECFNHVRFLQrFNSTHLYT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  141 CGTNAFSPMCTSRQVGNLSRTIEKINGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRdPAIYRSLGSgPPLRTAQYN 220
Cdd:cd11262     87 CGTHAFRPLCAYIDAERFTLSSQFEEGKEKCPYDPAKGYTGLIVD-GQLYTASQYEFRSF-PDIRRNSPQ-PTLRTEEAP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  221 SKWLNEPNFVAAY----DIGLFA------YFFLRENAVEhdcgRTVY------SRVARVCKNDVGGRFLLEDTWTTFMKA 284
Cdd:cd11262    164 TRWLNDADFVGSVlvreSMNSSVgdddkiYFFFTERSQE----ETAYfsqsrvARVARVCKGDRGGKKTLQRKWTSFLKA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  285 RLNCSRPgEVPFYYNELQSAFHL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIAN 360
Cdd:cd11262    240 RLVCYIP-EYEFLFNVLRSVFVLwgstPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYTG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  361 PIPNFQCGT-----LPETGPN--ENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKD-TLYHVLY 432
Cdd:cd11262    319 KVPEPRPGScitdeHRSQGINssQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDgRVYDVLF 398
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217344491  433 IGTESGTILKALSTASRsLHgcYLEELHVLPpgRREPLRSLRILHSARALFVGLRDGVLRVPL 495
Cdd:cd11262    399 LGTDEGWLHKAVVIGSA-VH--IIEELQVFR--EPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
57-495 1.27e-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: 248.56  E-value: 1.27e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   57 VSNFTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQATEWASSEDTRRSCQSKGKTEE-ECQNYVRVLIVAG 135
Cdd:cd11258      1 VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQtECFNYIRFLQPYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  136 RK-VFMCGTNAFSPMCTSRQVGNLSRTIEKI-NGVARCPYDPRHNSTAVISsQGELYAATVIDFSGRDPAIYRSLGSGPP 213
Cdd:cd11258     81 QShLYTCGTYAFQPKCAYINMLTFTLDRAEFeDGKGKCPYDPAKGHTGLIV-DGELYSATLNNFLGTEPVILRNLGQHYS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  214 LRTaQYNSKWLNEPNFV-AAY---DIGLF------AYFFLRENAVEHDC-GRTVYSRVARVCKNDVGGRFLLEDTWTTFM 282
Cdd:cd11258    160 MKT-EYLAFWLNEPHFVgSAFvpeSVGSFtgdddkIYFFFSERAVEYDCdSEQVVARVARVCKGDLGGARTLQKKWTTFL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  283 KARLNCSRPgEVPFYYNELQSAFHLPEQDL----IYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPI 358
Cdd:cd11258    239 KARLLCSIP-EWQLYFNQLKAVFTLEGASWrnttFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRY 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  359 ANPIPNFQCGTLPETGPNENLTERSLQ--DAQRLF-----LMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKD-TLYHV 430
Cdd:cd11258    318 TDPVPSPRPGSCINNWHRDHGYTSSLElpDNTLNFvkkhpLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDgETYSV 397
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217344491  431 LYIGTESGTILKALSTASRSlhgCYLEELHVLppGRREPLRSLRILHSARALFVGLRDGVLRVPL 495
Cdd:cd11258    398 LFIGTLDGWLIKAVSLGSWV---HMIEELQVF--DQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
55-494 1.23e-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: 234.78  E-value: 1.23e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   55 PWVSNFTYPGARDFSQLALDPSGNQLIVGARNYLFRLSLANVS-LLQATEWASSEDTRRSCQSKGKTEEECQNYVRVL-I 132
Cdd:cd11261      1 SALTRFSAPHTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGeRPRRIDWMVPEAHRQNCRKKGKKEAECHNFIRILaI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  133 VAGRKVFMCGTNAFSPMCTSRQVGNLsRTIEKI-NGVARCPYDPRHNSTAVISSqGELYAATVIDFSGRDPAIYRSLGSG 211
Cdd:cd11261     81 ANASHLLTCGTFAFDPKCGVIDVSSF-QQVERLeSGRGKCPFEPAQRSAAIMAG-GVLYAATVKNFLGTEPIISRAVGRA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  212 PPLRTAQYNSKWLNEPNFVAAYDIGLFA----------YFFLRENAVEHDCGRTV-YSRVARVCKNDVGGRFLLEDTWTT 280
Cdd:cd11261    159 EEWIRTETLPSWLNAPAFVAAVFLSPAEwgdedgddeiYFFFTETAREYDSYERIkVPRVARVCAGDLGGRKTLQQRWTT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  281 FMKARLNCSRP--GEVpfyYNELQSAFHLPEQD-----LIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENPRA 353
Cdd:cd11261    239 FLKADLLCPGPehGRA---SSILQDVTTLRPLPgagtpIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCN 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  354 AWLPIA-NPIPNFQCGT-------LPETGPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQA-K 424
Cdd:cd11261    316 RGLPVMdSDVPQPRPGEcitnnmkLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAAHRVTSlS 395
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217344491  425 DTLYHVLYIGTESGTILKALSTASR-SLhgcyLEELHVLPpgRREPLRSLRILHSarALFVGLRDGVLRVP 494
Cdd:cd11261    396 GKEYDVLYLGTEDGHLHRAVRIGAQlSV----LEDLALFP--EPQPVENLQLHHN--WLLVGSDTEVTQIN 458
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
67-496 6.30e-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: 6.30e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   67 DFSQLALDPSGNQLIVGARNYLFRLSLANVSLLQAT-----EWASSEDTRRSCQSKGKTEEECQNYVRVLIVAGRK--VF 139
Cdd:cd09295      1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLSCispelNFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGDLdiLA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTNAFSPMCtsrqvGNLSRTIEKING-------VARCPYDPRHNSTAVISSqGELYAATVIDF-SGRDPAIYRSLGSG 211
Cdd:cd09295     81 VCGSNAAQPSC-----GSYRLDVLVELGkvrwpsgRPRCPIDNKHSNMGVNVD-SKLYSATDHDFkDGDRPALSRRSSNV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  212 PPLRTAQYNSKWLNEPNFVAAYDIGL---FAYFFLRENAVEHDCGRTVY-SRVARVCKNDVGGRFLLEDTWTTFMKARLN 287
Cdd:cd09295    155 HYLRIVVDSSTGLDEITFVYAFVSGDdddEVYFFFRQEPVEYLKKGMVYvPRIARVCKLDVGGCHRLKKKLTSFLKADLN 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  288 CSRPGEvPFYYNELQSAFHL---PEQDLIYGVFTTNVNSIAASAVCAFNLSAISQAFNGPFRYQENpraawlpianpipn 364
Cdd:cd09295    235 CSRPQS-GFAFNLLQDATGDtknLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVFDDPVEAINN-------------- 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  365 fqcgtlpetgpnenlterslqdaqRLFLMSeavqpvtpepcvTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKAL 444
Cdd:cd09295    300 ------------------------RPLYAH------------QNQRSRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKAL 343
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491  445 S-TASRSLHgcYLEELHVLPPGrrEPLRSLRILHSARALFVGLRDGVLRVPLE 496
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 ...
301-477 1.16e-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: 1.16e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  301 LQSAFHLPE------QDLIYGVFTTN-VNSIAASAVCAFNLSAISQAFNGPFRYQENPRAAWLPIANPIPNFQCGTLPET 373
Cdd:pfam01403    1 LQDVFVLKPgagdalDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  374 GPNENLTERSLQDAQRLFLMSEAVQPVTPEPCVTQDSVRFSHLVVDLVQAKDTLYHVLYIGTESGTILKALSTASRSLHg 453
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEESH- 159
                          170       180
                   ....*....|....*....|....
gi 2217344491  454 cYLEELHVLPPGrrEPLRSLRILH 477
Cdd:pfam01403  160 -IIEEIQVFPEP--QPVLNLLLSS 180
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
73-496 2.41e-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: 2.41e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   73 LDPSGNQLIVGARNYLFRLSLANVSLLQatEWASSEDTRRSCQSKGkTEEECQNYVRVLIVAGRKVFMCGTNAFSPMCTs 152
Cdd:cd11243      9 HEAGSSSVYVGGQGALYLLDFTGSAVIV--KKIPDEKTEKDCKKRA-TLDDCENYITLIKKLDYRLLVCGTNAGSPKCW- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  153 RQVGNLSRTIEKINGVArcPYDPRHNStAVISSQGELYAAtvIDFSGRDPAIYRSLGSGPPLRTAqynSKWLNEPNFVAA 232
Cdd:cd11243     85 FLVNQTLVTLSADRGVA--PFLPDENS-LVLIEGNNVYST--ISGKKGNIPRFRRYGGKKELYTS---DTVMQKPQFVKA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  233 --------YDIGLfaYFFLREnaVEHDCGRTV---YSRVARVCKNDVGGRFLLE-DTWTTFMKARLNCSRPGEvPFYYNE 300
Cdd:cd11243    157 tllpedeqYQDKI--YYFFRE--DNEDKGPEAepnISRVARLCKEDQGGTSSLStSKWSTFLKARLVCGDPAT-PMNFNR 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  301 LQSAFHLP----EQDLIYGVFTTNVNSiaaSAVCAFNLSAISQAFngpfryqenpRAAWLPIAN-PIPNFQCGT-LPetg 374
Cdd:cd11243    232 LQDVFLLPkeewREAVVYGVFSNTWGS---SAVCSYSLGDIDKVF----------RTSSLKGYSgSLPNPRPGTcVP--- 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  375 PNENLTERSLQDAQRLFLMSEAVQPVTPEPC-VTQDSVRFSHLVVDLVQAKDTL-YHVLYIGTESGTILKALSTASRSLH 452
Cdd:cd11243    296 PEQTHPSETFSFADEHPELDDRIEPDEPRKLpVFQNKDHYQKVVVDEVRASDGVsYDVLYLATDKGKIHKVVESKGQTHN 375
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2217344491  453 gcyleeLHVLPPGRR-EPLRSLRILHSARALFVGLRDGVLRVPLE 496
Cdd:cd11243    376 ------IMEIQPFKEqEPIQSMILDAERSHLYVGTKAEVTRLPLD 414
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
798-850 1.95e-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: 1.95e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   798 WAAWGPWSSCSRDCELGFRVRKRTCTNPEPRNGGLPCVGDAAEYQDCNPQACP 850
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
855-907 1.10e-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: 1.10e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   855 WSCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDICLGLHTEEALCATQACP 907
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
609-662 3.54e-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: 67.61  E-value: 3.54e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217344491   609 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRHGGRICVGKSREERFCNENtPCP 662
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ-PCP 53
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
71-342 5.63e-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: 68.90  E-value: 5.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   71 LALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRR----SCQSKGKTEEECQNYVRVLIV--AGRKVFMCGTn 144
Cdd:cd11236      5 LAVDNSTGRVYVGAVNRLYQLD-SSLLLEAEVSTGPVLDSPLclppGCCSCDHPRSPTDNYNKILLIdySSGRLITCGS- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  145 AFSPMCTSRQVGNLSRTIEKI--NGVARCPYDprhnSTAVISSQGE------LYAATVIDFSGRDPAIY----RSLGSGP 212
Cdd:cd11236     83 LYQGVCQLRNLSNISVVVERSstPVAANDPNA----STVGFVGPGPynnenvLYVGATYTNNGYRDYRPavssRSLPPDD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  213 PLRTAQYN--SKWLNEPNFVAAYDI--------GLFAYFFLRENAVeHDCGRTVYSRVARVCKNDvgGRFLledtwtTFM 282
Cdd:cd11236    159 DFNAGSLTggSAISIDDEYRDRYSIkyvygfssGGFSYFVTVQRKS-VDDESPYISRLVRVCQSD--SNYY------SYT 229
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217344491  283 KARLNC-SRPGEVpfyYNELQSAF-------------HLPEQDLIYGVFTTNVNSIAA----SAVCAFNLSAISQAFN 342
Cdd:cd11236    230 EVPLQCtGGDGTN---YNLLQAAYvgkagsdlarslgISTDDDVLFGVFSKSKGPSAEpsskSALCVFSMKDIEAAFN 304
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
667-713 2.58e-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: 2.58e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2217344491   667 WASWGSWSKCSSNCGGGMQSRRRACEN------GNSCLGCGVEFKTCNPEGCP 713
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
801-849 1.58e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 1.58e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217344491  801 WGPWSSCSRDCELGFRVRKRTCTNPEPrnGGLPCVGDAAEYQDCNPQAC 849
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 ...
68-525 1.70e-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: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   68 FSQLALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRrSC------QSKGKTEEECQNYVRVLIV--AGRKVF 139
Cdd:cd11272     13 FNHLTVHQSTGAVYVGAINRVYKLS-GNLTILVAHKTGPEEDNK-SCypplivQPCSEVLTLTNNVNKLLIIdySENRLL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTnAFSPMCTSRQVGNLSRTIEKINgvARCPYDPRHNSTA-----VISSQGE---LYAATVIDfsGRD---PAIY-RS 207
Cdd:cd11272     91 ACGS-LYQGVCKLLRLDDLFILVEPSH--KKEHYLSSVNKTGtmygvIVRSEGEdgkLFIGTAVD--GKQdyfPTLSsRK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  208 LGSGPPLRT-------AQYNSKWLNEPN----FVAAYDI--------GLFAYFFL-----RENAVEHDCGRTVY-SRVAR 262
Cdd:cd11272    166 LPRDPESSAmldyelhSDFVSSLIKIPSdtlaLVSHFDIfyiygfasGNFVYFLTvqpetPEGVSINSAGDLFYtSRIVR 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  263 VCKNDvggrflleDTWTTFMKARLNCSRPGEvpfYYNELQSAFH-------------LPEQDLIYGVFTTNVNSIAA--- 326
Cdd:cd11272    246 LCKDD--------PKFHSYVSLPFGCVRGGV---EYRLLQAAYLskpgevlarslniTAQEDVLFAIFSKGQKQYHHppd 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  327 -SAVCAFNLSAISQAFNGPFR--YQE--NPRAAWL----------PIanPIPNFQCGTlpetGPNENLTERSLQDAQRLF 391
Cdd:cd11272    315 dSALCAFPIRAINAQIKERLQscYQGegNLELNWLlgkdvqctkaPV--PIDDNFCGL----DINQPLGGSTPVEGVTLY 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  392 lmseavqpvtpepcvTQDSVRFSHLVVDLVQAkdtlYHVLYIGTESGTILKAlsTASRSLHGCYLEELHVLPPGRREPLR 471
Cdd:cd11272    389 ---------------TSSRDRLTSVASYVYNG----YSVVFVGTKSGKLKKI--RADGPPHGGVQYEMVSVFKDGSPILR 447
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217344491  472 SLRILHSARALFVGLRDGVLRVPLERCAAYRSQGACLGARDPYCGWDGKQQRCS 525
Cdd:cd11272    448 DMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDPHCGWCALHNMCS 501
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
497-544 1.80e-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: 51.55  E-value: 1.80e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  497 RCAAYRSQGACLGARDPYCGWDGKQQRCST----LEDSSNMSLWTQNITACP 544
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
69-496 4.90e-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: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   69 SQLALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRRsCqSKGKTEEECQ------NYVRVLIV--AGRKVFM 140
Cdd:cd11276      9 NHLVVDPQTGRVYLGAVNALYQLD-ADLQLESRVETGPKKDNKK-C-TPPIEENQCTeakmtdNYNKLLLLdsANKTLVV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  141 CGTnAFSPMCTSRQVGNLSRTIEKINGVARCPY----DPRHNSTAVISSQ----------GELYA--------ATVIDFS 198
Cdd:cd11276     86 CGS-LFKGICSLRNLSNISEVIYYSDTSGEKSFvasnDEGVSTVGLISSLkpgndrvffvGKGNGsndngkiiSTRLLQN 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  199 GRDPAIYRSLGSGPPLRTAqYNSKWLNepNFVAAYDIGLFAYFFLRENAVEHDCGRTVysrVARVCKNDVGgrflledtW 278
Cdd:cd11276    165 YDDREVFENYIDAATVKSA-YVSRYTQ--QFRYAFEDNNYVYFLFNQQLGHPDKNRTL---IARLCENDHH--------Y 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  279 TTFMKARLNCSRPGEVpfyYNELQSAF-HLPEQDL-------------IYGVFTTNVNSIAASAVCAFNLSAISQafngp 344
Cdd:cd11276    231 YSYTEMDLNCRDGANA---YNKCQAAYvSTPGKELaqnygnsilsdkvLFAVFSRDEKDSGESALCMFPLKSINA----- 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  345 fRYQENPRAAWLPIANPIPNFQcgtLPETGPNENLTERSLQDAQRLFLM-SEAVqpvtPEPCVTQDSVRFSHLVvdLVQA 423
Cdd:cd11276    303 -KMEANREACYTGTIDDRDVFY---KPFHSQKDIICGSHQQKNSKSFPCgSEHL----PYPLGSRDELALTAPV--LQRG 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  424 KDTL----------YHVLYIGTESGTILK-ALSTASrslhgcylEELHVLPPGRREPL-RSLRILHSARALFVGLRDGVL 491
Cdd:cd11276    373 GLNLtavtvavengHTVAFLGTSDGRILKvHLSPDP--------EEYNSILIEKNKPVnKDLVLDKTLEHLYIMTEDKVF 444

                   ....*
gi 2217344491  492 RVPLE 496
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 ...
60-368 5.31e-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: 56.74  E-value: 5.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   60 FTYPGARdFSQLALDPSGNQLIVGARNYLFRLSlanvSLLQATEWASS---EDT--------RRSCQSKGKTEeecqNYV 128
Cdd:cd11277      1 FSAPNAT-FNHLALDPGSGTLYVGAVNRLYQLS----PDLQLLGEAVTgpvLDSpdclpfrdPADCPQARLTD----NAN 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  129 RVLIVAGR--KVFMCGTnAFSPMCTSRQVGNLS----RTIEKINGVARCPYDPRHNSTAVISSQGE---LYAA---TVID 196
Cdd:cd11277     72 KLLLVSERagELVACGQ-VRQGVCEKRRLGNVAqvlyQAEDPGDGQFVAANDPGVATVGLVVEAPGrdlLLVGrglTGKL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  197 FSGRDPAIYRSLGSGPPLRT-----------AQYNSkwlnepNFVAAYDIGLFAYFFLRENAVEhdcGRTVY-SRVARVC 264
Cdd:cd11277    151 SAGIPPLTIRQLAGAQAFSSeglgklvvgdfSDYNN------SYVGAFAHNGYVYFLFRRRGAR---AQAEYrTYVARVC 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  265 KNDVggrFLLedtwtTFMKARLNCsRPGevpfyYNELQSAFHLPEQDLIYGVFTTNVNSIAA----SAVCAFNLSAI--- 337
Cdd:cd11277    222 LGDT---NLY-----SYVEVPLVC-QGG-----YNLAQAAYLAPGQGTLFVVFAAGQGSTPTptdqTALCAYPLVELdsa 287
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2217344491  338 ---------SQAFNGP-------FRYQENPRAAWLPIANPiPNFQCG 368
Cdd:cd11277    288 merarrlcyTAGGGGPngkeeatIEYGVTSRCVNLPKDSP-ESYPCG 333
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
610-661 4.86e-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: 4.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217344491  610 TPWSSWALCSTSCGIGFQVRQRSCSNPaPRHGGRICVGKSrEERFCNENtPC 661
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 ...
800-849 4.96e-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: 4.96e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217344491  800 AWGPWSSCSRDCELGFRVRKRTCTNPePRNGGLPCvGDAAEYQDCNPQAC 849
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
610-656 6.01e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 6.01e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217344491  610 TPWSSWALCSTSCGIGFQVRQRSCSNPAPrhGGRICVGKSREERFCN 656
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACK 45
TSP_1 pfam00090
Thrombospondin type 1 domain;
670-712 6.31e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 6.31e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217344491  670 WGSWSKCSSNCGGGMQSRRRAC----ENGNSCLGCGVEFKTCNPEGC 712
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
497-534 3.88e-06

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 44.84  E-value: 3.88e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217344491   497 RCAAYRSQGACLGARDPYCGWDGKQQRCSTLEDSSNMS 534
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRR 38
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
68-375 3.93e-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: 50.70  E-value: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491   68 FSQLALDPSGNQLIVGARNYLFRLSlANVSLLQATEWASSEDTRRsCQSKgKTEEEC------QNYVRVLIVAGRK--VF 139
Cdd:cd11245      2 INHLAQDPQTGRLYLGAVNGLFQLS-PNLQLESRADTGPKKDSPQ-CLPP-ITAAECpqaketDNFNKLLLVNSANgtLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  140 MCGTnAFSPMCTSRQVGNLSRTIEKINGVARCPY----DPRHNSTAVISSQGelyAATVIDFSGRDpaiYRSLGSG--PP 213
Cdd:cd11245     79 VCGS-LFQGVCELRNLNSVNKPLYRPETPGDKQYvaanEPSVSTVGLISYFK---DGLSLLFVGRG---YTSSLSGgiPP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  214 LRTAQynskwLNEP------------------------NFVAAYDIGLFAYF-FLRENAVEHDCGRTVysrVARVCKNDv 268
Cdd:cd11245    152 ITTRL-----LQEHgemdafsneveaklvvgsasryhhDFVYAFADNGYIYFlFSRRPGTADSTKRTY---ISRLCEND- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217344491  269 ggrflleDTWTTFMKARLNCSrpGEVPFYYNELQSAFHLP-----EQDLIYGVFTTNVNSIAA----SAVCAFNLSAISQ 339
Cdd:cd11245    223 -------HHYYSYVELPLNCT--VNQENTYNLVQAAYLAKpgkvlNGKVLFGVFSADEASTAApdgrSALCMYPLSSVDA 293
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2217344491  340 AFN--------GPFRYQENPRAAWLPIANpipNFQCGTLPETGP 375
Cdd:cd11245    294 RFErtrescytGEGLEDDKPETAYIEYNV---KSICKTLPDKNV 334
TSP_1 pfam00090
Thrombospondin type 1 domain;
856-906 4.11e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.72  E-value: 4.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217344491  856 SCWTSWSPCSASCGGGHYQRTRSCTSPAPSPGEdiCLGLHTEEALCATQAC 906
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEP--CTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
911-952 3.75e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 3.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217344491  911 SPWSEWSKCT---DDGAQSRSRHCEELLPGSSACAGNSSQSRPCP 952
Cdd:pfam00090    1 SPWSPWSPCSvtcGKGIQVRQRTCKSPFPGGEPCTGDDIETQACK 45
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
910-951 1.79e-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: 1.79e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2217344491   910 WSPWSEWSKCT---DDGAQSRSRHCEELLP--GSSACAGNSSQSRPC 951
Cdd:smart00209    1 WSEWSEWSPCSvtcGGGVQTRTRSCCSPPPqnGGGPCTGEDVETRAC 47
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
670-712 3.91e-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: 3.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2217344491  670 WGSWSKCSSNCGGGMQSRRR-----ACENGNSC--LgcgVEFKTCNPEGC 712
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 ...
858-906 4.15e-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: 4.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217344491  858 WTSWSPCSASCGGGHYQRTRSCTSPAPSPGEDiClGLHTEEALCATQAC 906
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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