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Conserved domains on  [gi|2024422623|ref|XP_040560164|]
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semaphorin-5B isoform X4 [Gallus gallus]

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: 991.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 139
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQY 219
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  220 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPFYYN 299
Cdd:cd11264    161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  300 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 379
Cdd:cd11264    241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  380 TERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 459
Cdd:cd11264    321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2024422623  460 QILPDGQREAIKSLQILHSDRSLFVGLNNGVLKIPLE 496
Cdd:cd11264    401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 855-907 1.19e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.19e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   855 WSCWTPWSQCSATCGGGHYQRTRTCTNPAPSSGEDICIGLHTEEALCNTHPCE 907
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 798-850 3.03e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 3.03e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   798 WSFWGAWSSCSRDCELGFRIRKRTCTNPEPKNGGLPCVGSAMEYQDCNPHPCP 850
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 609-662 7.07e-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: 69.54  E-value: 7.07e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2024422623   609 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRYGGRVCVGQSREERFCNENsPCP 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 6.58e-12

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 61.45  E-value: 6.58e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   667 WSSWGPWNKCSVNCGGGIHSRQRTCEN------GNTCPGCAVEYKTCNPESCP 713
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 497-544 1.48e-08

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


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 51.94  E-value: 1.48e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  497 RCSMYRTEGECLGARDPYCGWDNKQKRCTTIED----SSNMSLWTQNITECP 544
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRRSAcgapEGNCEEWEQASSKCP 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 910-951 2.24e-06

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 2.24e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2024422623   910 WSEWSEWSLCNE---EGIQYRSRYCEVHSP--DSSQCVGNSTQYQDC 951
Cdd:smart00209    1 WSEWSEWSPCSVtcgGGVQTRTRSCCSPPPqnGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 555-606 6.53e-06

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.50  E-value: 6.53e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623   555 GPWSPWQPCEHSDGDSTgscMCRSRSCDSPRPRCGGRSCEGARIEVANCSRN 606
Cdd:smart00209    2 SEWSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
 
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: 991.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 139
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQY 219
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  220 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPFYYN 299
Cdd:cd11264    161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  300 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 379
Cdd:cd11264    241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  380 TERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 459
Cdd:cd11264    321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2024422623  460 QILPDGQREAIKSLQILHSDRSLFVGLNNGVLKIPLE 496
Cdd:cd11264    401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema smart00630
semaphorin domain;
68-467 1.16e-129

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 399.05  E-value: 1.16e-129
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623    68 FSQLALDANRNQLIVGARNYLFRLSLHNVSLI-QATAWGSDEDTRRSCQSKGKTE-EECQNYVRVLIVY-GKKVFTCGTN 144
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLDYnEDRLLVCGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   145 AFSPVCSSRQVgnlskiidringvarcpydprhnstavitsrGELYAATVIDFSGRDPAIYRSLG-------NVPPLRTA 217
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSLRTV 129

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   218 QYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEHD-CGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPF 296
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   297 YYNELQSTFYLPE----QDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN-PIPNFQCGTLS 371
Cdd:smart00630  210 YFNELQAAFLLPPgsesDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   372 DDSPN-ENLTERVLQDAQRLFLMNDVVQPVT-VDPYVTQDS-IRFSKLVVDIVQGkDTLYHVMYIGTEYGTILKALSTTN 448
Cdd:smart00630  290 NKPPSsKDLPDETLNFIKSHPLMDEVVQPLTgRPLFVKTDSnYLLTSIAVDRVAT-DGNYTVLFLGTSDGRILKVVLSES 368

                           410       420
                    ....*....|....*....|
gi 2024422623   449 R-SLRSCYLEEMQILPDGQR 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 4.18e-56

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: 192.10  E-value: 4.18e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  301 LQSTFYLPE------QDLIYGVFTTN-VNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDD 373
Cdd:pfam01403    1 LQDVFVLKPgagdalDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  374 SPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSlrS 453
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEE--S 158

                          170       180
                   ....*....|....*....|....
gi 2024422623  454 CYLEEMQILPDGQreAIKSLQILH 477
Cdd:pfam01403  159 HIIEEIQVFPEPQ--PVLNLLLSS 180
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 855-907 1.19e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.19e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   855 WSCWTPWSQCSATCGGGHYQRTRTCTNPAPSSGEDICIGLHTEEALCNTHPCE 907
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 798-850 3.03e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 3.03e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   798 WSFWGAWSSCSRDCELGFRIRKRTCTNPEPKNGGLPCVGSAMEYQDCNPHPCP 850
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 609-662 7.07e-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: 69.54  E-value: 7.07e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2024422623   609 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRYGGRVCVGQSREERFCNENsPCP 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 6.58e-12

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 61.45  E-value: 6.58e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   667 WSSWGPWNKCSVNCGGGIHSRQRTCEN------GNTCPGCAVEYKTCNPESCP 713
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 497-544 1.48e-08

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 51.94  E-value: 1.48e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  497 RCSMYRTEGECLGARDPYCGWDNKQKRCTTIED----SSNMSLWTQNITECP 544
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRRSAcgapEGNCEEWEQASSKCP 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
856-906 2.43e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.43e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024422623  856 SCWTPWSQCSATCGGGHYQRTRTCTNPAPSSGEdiCIGLHTEEALCNTHPC 906
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEP--CTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
799-849 5.54e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 5.54e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024422623  799 SFWGAWSSCSRDCELGFRIRKRTCTNPEPKNGglPCVGSAMEYQDCNPHPC 849
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
668-712 6.35e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.72  E-value: 6.35e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024422623  668 SSWGPWNKCSVNCGGGIHSRQRTC----ENGNTCPGCAVEYKTCNPESC 712
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
610-661 2.66e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.18  E-value: 2.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  610 TPWSSWALCSTSCGIGFQVRQRSCSNPAPryGGRVCVGQSREERFCNeNSPC 661
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACK-MDKC 49
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
497-534 6.62e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 46.77  E-value: 6.62e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2024422623   497 RCSMYRTEGECLGARDPYCGWDNKQKRCTTIEDSSNMS 534
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRR 38
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 910-951 2.24e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 2.24e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2024422623   910 WSEWSEWSLCNE---EGIQYRSRYCEVHSP--DSSQCVGNSTQYQDC 951
Cdd:smart00209    1 WSEWSEWSPCSVtcgGGVQTRTRSCCSPPPqnGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 555-606 6.53e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.50  E-value: 6.53e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623   555 GPWSPWQPCEHSDGDSTgscMCRSRSCDSPRPRCGGRSCEGARIEVANCSRN 606
Cdd:smart00209    2 SEWSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
908-951 2.50e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.71  E-value: 2.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024422623  908 GGWSEWSEWSLCNEEGIQYRSRYCEVHSPDSSQCVGNSTQYQDC 951
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQAC 44
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 670-720 5.74e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 43.80  E-value: 5.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  670 WGPWNKCSVNCGGGIHSRQRTCENgntcPGCAVEY-KTCNPESCPEVRRNTP 720
Cdd:PTZ00441   243 WDEWTPCSVTCGKGTHSRSRPILH----EGCTTHMvEECEEEECPVEPEPLP 290
 
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: 991.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 139
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQY 219
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  220 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPFYYN 299
Cdd:cd11264    161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  300 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 379
Cdd:cd11264    241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNENL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  380 TERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 459
Cdd:cd11264    321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2024422623  460 QILPDGQREAIKSLQILHSDRSLFVGLNNGVLKIPLE 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: 804.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 139
Cdd:cd11241      1 FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSVEECQNYVRVLLVVGKNLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQY 219
Cdd:cd11241     81 TCGTYAFSPVCTIRKLSNLTQILDTISGVARCPYSPAHNSTALISASGELYAGTVYDFSGRDPAIYRSLGGKPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  220 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPFYY 298
Cdd:cd11241    161 NSKWLNEPNFVGSYEIGNHTYFFFRENAVEHqDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGEFPFYY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  299 NELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDDSPNEN 378
Cdd:cd11241    241 NEIQGTFYLPETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPTPNPHPNFQCTTSIDRGQPAN 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  379 LTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDT-LYHVMYIGTEYGTILKALSTTnRSLRSCYLE 457
Cdd:cd11241    321 TTERDLQDAQKYQLMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRGTqLVHIFYVGTDYGTILKMYQPH-RSQKSCTLE 399

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2024422623  458 EMQILPDGQREAIKSLQILHSDRSLFVGLNNGVLKIPLE 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: 743.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 139
Cdd:cd11263      1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQY 219
Cdd:cd11263     81 TCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  220 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPFYYN 299
Cdd:cd11263    161 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  300 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLsDDSPNENL 379
Cdd:cd11263    241 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTM-DQGLYVNL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  380 TERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 459
Cdd:cd11263    320 TERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEI 399

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2024422623  460 QILPDGQREAIKSLQILHSDRSLFVGLNNGVLKIPLE 496
Cdd:cd11263    400 ELFPKRQREPIRSLQILHSQSVLFVGLQEHVIKIPLK 436
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
 60-494 5.67e-165

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: 492.76  E-value: 5.67e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 139
Cdd:cd11265      1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLG--NVPPLRTA 217
Cdd:cd11265     81 ACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSSSGQLFVGSPTDFSGSDSAIYRTLGtsNKSFLRTK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  218 QYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGGR-FLLEDTWTTFMKARLNCSRAGEIP 295
Cdd:cd11265    161 QYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYmNCGKVIYSRIARVCKNDVGGGtMLLKDNWTTFLKARLNCSLPGEYP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  296 FYYNELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAW--LPTANPIPNFQCGTLSDD 373
Cdd:cd11265    241 FYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWerVNVNHRDHFNQCSSSSSS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  374 SpnenltervLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGK-DTLYHVMYIGTEYGTIlKALSTTNRSLR 452
Cdd:cd11265    321 H---------LLESSRYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKiHQSVHVLYVATTGGLI-KKISVLPRTQE 390

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2024422623  453 SCYLEEMQILPDGQREaIKSLQILHSDRSLFVGLNNGVLKIP 494
Cdd:cd11265    391 TCLVEIWQPLPTPDSP-IKTMQYLKVTDSLYVGTELALMRIP 431
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
 66-495 1.20e-162

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: 486.92  E-value: 1.20e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   66 HDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYG-KKVFTCGTN 144
Cdd:cd11235      1 LKYHTKLLHEDRSTLYVGARDRVYLVDLDSLYTEQKVAWPSSPDDVDTCYLKGKSKDDCRNFIKVLEKNSdDSLLVCGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  145 AFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAvITSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQYNSKWL 224
Cdd:cd11235     81 AFNPSCRNYNVETFELVGKEESGRGKCPYDPDHNSTA-LFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  225 NEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPFYYNELQS 303
Cdd:cd11235    160 NEPQFVGAFDIGDYVYFFFREIAVEYiNCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFPFYFNELQD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  304 TFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPI-PNFQCGTLSDDSPneN 378
Cdd:cd11235    240 VFDLPSPSnkekIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDERvPEPRPGTCVDDSS--P 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  379 LTERVLQDAQRLFLMNDVVQPVTVDP--YVTQDSIRFSKLVVDIVQGK-DTLYHVMYIGTEYGTILKALST-TNRSLRSC 454
Cdd:cd11235    318 LPDDTLNFIKSHPLMDEAVTPILNRPlfIKTDVNYRFTKIAVDRVQAKlGQTYDVLFVGTDRGIILKVVSLpEQGLQASN 397

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2024422623  455 YLEEMQILPDGqrEAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11235    398 ILEEMPVGPPP--EPIQTMQLSRKRRSLYVGSETGVLQVPL 436
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
 73-498 1.62e-132

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: 408.64  E-value: 1.62e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   73 LDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGK-KVFTCGTNAFSPVCS 151
Cdd:cd11237     10 LDQDGNSLLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLAKKSAgRLLVCGTNAYKPLCR 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  152 SRQVGNLSKIIDR-INGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSlgnvpPLRTAQYNSKWLNEPNFI 230
Cdd:cd11237     90 EYTVKDGGYRVEReFDGQGLCPYDPKHNSTAVYAD-GQLYSATVADFSGADPLIYRE-----PLRTERYDLKQLNAPNFV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  231 AAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPFYYNELQSTFYLPE 309
Cdd:cd11237    164 SSFAYGDYVYFFFRETAVEYiNCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGEYPFYFNEIQSTSDIVE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  310 -------QDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPT-ANPIPNFQCGTLSDDSpnenlte 381
Cdd:cd11237    244 ggyggksAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVpSNKVPEPRPGQCVNDS------- 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  382 RVLQDAQRLF-----LMNDVVQPVTVDPYVTQDSI--RFSKLVVD----IVQGKdtLYHVMYIGTEYGTILKALSTTNRS 450
Cdd:cd11237    317 RTLPDVTVNFikshpLMDEAVPSFFGRPILVRTSLqyRFTQIAVDpqvkALDGK--YYDVLFIGTDDGKVLKAVNIASAD 394

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024422623  451 ----LRSCYLEEMQILPDGqrEAIKSLQILHSDR--SLFVGLNNGVLKIPLERC 498
Cdd:cd11237    395 tvdkVSPVVIEETQVFPRG--VPIRNLLIVRGKDdgRLVVVSDDEIVSIPLHRC 446
Sema smart00630
semaphorin domain;
68-467 1.16e-129

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 399.05  E-value: 1.16e-129
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623    68 FSQLALDANRNQLIVGARNYLFRLSLHNVSLI-QATAWGSDEDTRRSCQSKGKTE-EECQNYVRVLIVY-GKKVFTCGTN 144
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLDYnEDRLLVCGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   145 AFSPVCSSRQVgnlskiidringvarcpydprhnstavitsrGELYAATVIDFSGRDPAIYRSLG-------NVPPLRTA 217
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSLRTV 129

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   218 QYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEHD-CGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAGEIPF 296
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   297 YYNELQSTFYLPE----QDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN-PIPNFQCGTLS 371
Cdd:smart00630  210 YFNELQAAFLLPPgsesDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   372 DDSPN-ENLTERVLQDAQRLFLMNDVVQPVT-VDPYVTQDS-IRFSKLVVDIVQGkDTLYHVMYIGTEYGTILKALSTTN 448
Cdd:smart00630  290 NKPPSsKDLPDETLNFIKSHPLMDEVVQPLTgRPLFVKTDSnYLLTSIAVDRVAT-DGNYTVLFLGTSDGRILKVVLSES 368

                           410       420
                    ....*....|....*....|
gi 2024422623   449 R-SLRSCYLEEMQILPDGQR 467
Cdd:smart00630  369 SsSSESVVLEEISVFPDGSP 388
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
 67-495 1.21e-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: 357.21  E-value: 1.21e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFsQLALDANRNqLIVGARNYLFRLSLHNVSLIQAT-----AWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKK-VFT 140
Cdd:cd11242     10 DF-QRMLRINRT-LYIAARDHVYTVDLDASHTEEIVpskklTWRSRQADVENCRMKGKHKDECHNFIKVLVPRNDEtLFV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  141 CGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVItSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQYN 220
Cdd:cd11242     88 CGTNAFNPVCRNYRIDTLEQDGEEISGMARCPFDAKQANVALF-ADGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  221 SKWLNEPNFIAAYDIGLFTYFFFRENAVEHD-CGKTVYSRVARVCKNDIGG-RFLLEDTWTTFMKARLNCSRAGEIPFYY 298
Cdd:cd11242    167 SKWLKEPHFVHAVEYGDYVYFFFREIAVEYNtLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPGDSHFYF 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  299 NELQS---TFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN---PIPNFQC----G 368
Cdd:cd11242    247 DVLQAvtdVIRINGRPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPEdrvPKPRPGCcagsG 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  369 TLSDDSPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRF--SKLVVDIVQGKDTLYHVMYIGTEYGTILKALST 446
Cdd:cd11242    327 SAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYrlTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLAR 406

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  447 TNRSL--RSCYLEEMQIL---------PDGQReaIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11242    407 IGPSGsnGSVFLEEIDVYnpakcsydgEEDRR--IIGLELDRASHALFVAFSGCVIRVPL 464
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
 60-495 1.28e-111

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: 354.02  E-value: 1.28e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLI--QATAWGSDEDTRRSCQSKGKTEE-ECQNYVRVLIVYGK 136
Cdd:cd11240      1 FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDISTElkDKIKWEASEDKKKECANKGKDNQtDCFNFIRILQFYNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  137 -KVFTCGTNAFSPVCS--SRQVGNLSKIiDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVPP 213
Cdd:cd11240     81 tHLYVCGTFAFSPRCTyiNLSDFSLSSI-KFEDGKGRCPFDPAQRYTAIMVD-GELYSATVNNFLGSEPVISRNHSEGNV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  214 LRTaQYNSKWLNEPNFI-AAY---DIGLFT------YFFFRENAVEHDCG-KTVYSRVARVCKNDIGGRFLLEDTWTTFM 282
Cdd:cd11240    159 LKT-ENTLRWLNEPAFVgSAHireSIDSPDgdddkiYFFFTETAVEYDFYeKVTVSRVARVCKGDLGGQRTLQKKWTTFL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  283 KARLNCSRAGEiPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPT 358
Cdd:cd11240    238 KAQLVCSQPDS-GLPFNVLRDVFVLSPDSwdatIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRY 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  359 ANPIPNFQCGTLSDDSPNE-------NLTERVLQDAQRLFLMNDVVQPVtVDPYVTQDSIRFSKLVVDIVQGKD-TLYHV 430
Cdd:cd11240    317 TGPVPDPRPGACITNSARSqgitsslNLPDNVLTFVKDHPLMDEQVHPI-NRPLLVKSGVNYTRIAVHRVQALDgQTYTV 395

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024422623  431 MYIGTEYGTILKALSTTNRSLrscYLEEMQILPDGQreAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11240    396 LFLGTEDGFLHKAVSLDGGMH---IIEEIQLFDQPQ--PVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
 67-498 2.74e-110

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: 351.28  E-value: 2.74e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFSQLALDANRNQLIVGARNYLFRLSLHNVSL-IQATAWGSDEDTRRSCQSKGKT-EEECQNYVRVLIVYGKK-VFTCGT 143
Cdd:cd11239      9 DYRSLLLDEDRDRLYVGGKDHILSLSLDNINQdPKKIYWPASPERIEECKMAGKDpNTECANFVRVLQPYNRThLYACGT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  144 NAFSPVCSSRQVG-NLSKIIDRI------NGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVPPLRT 216
Cdd:cd11239     89 GAFHPICAFINVGrRLEDPIFKLddssleSGRGKCPFDPNQPFASVLID-GELYSGTAIDFMGRDAAIFRSLGHRHYIRT 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  217 AQYNSKWLNEPNFIAAYDIGLFT-------YFFFRENAVEHD-CGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNC 288
Cdd:cd11239    168 EQYDSRWLNEPKFVGAYLIPDSDnpdddkvYFFFREKAVEAEgSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLKARLVC 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  289 SRAGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPI 362
Cdd:cd11239    248 SVPGPdgIDTYFDELEDVFLLPTRDpknpLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVEYQGKV 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  363 PNFQCGTL-----------SDDSPNEnlterVLQDAQRLFLMNDVVQPVTVDPYVTQDSI--RFSKLVVDIVQGKDTLYH 429
Cdd:cd11239    328 PYPRPGTCpsktygplyksTKDFPDD-----VISFARSHPLMYNPVYPLHGRPLLIRTNVpyRLTQIAVDRVEAEDGQYD 402

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024422623  430 VMYIGTEYGTILK--ALSTTNRSLRSCYLEEMQILPDgqREAIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11239    403 VLFIGTDSGTVLKvvSLPKENWEMEEVILEELQVFKH--PSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
 68-495 1.78e-102

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: 329.77  E-value: 1.78e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   68 FSQLALDANRNQLIVGARNYLFRLSLHNVSLI-------QATAWGSDEDTrrsCQSKGKTEE-ECQNYVRVLIVY--GKK 137
Cdd:cd11238      3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINDTgnncardELTLSPSDVSE---CVSKGKDEEyECRNHVRVIQPMgdGQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  138 VFTCGTNAFSPVCSSRQVGNLSKIIDRI---NGVARCPYDPRHNSTAVITSRGE------LYAATVIDFSGRDPAIYRsl 208
Cdd:cd11238     80 LYVCSTNAMNPKDRVLDANLLHLPEYVPgpgNGIGKCPYDPDDNSTAVWVEWGNpgdlpaLYSGTRTEFTKANTVIYR-- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  209 gnvPPL------------RTAQYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGGRFLLE 275
Cdd:cd11238    158 ---PPLynntkgrhesfmRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETAVEYiNCGKVVYSRVARVCKKDTGGKNVLR 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  276 DTWTTFMKARLNCSRAGEIPFYYNELQSTFYLPEQD--LIYGVFTTNVNSIAASAVCAFNLSAITQAFN-GPFRYQENPR 352
Cdd:cd11238    235 QNWTTFLKARLNCSISGEFPFYFNEIQSVYKVPGRDdtLFYATFTTSENGFTGSAVCVFTLSDINAAFDtGKFKEQASSS 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  353 SAWLPT-ANPIPNFQCGTLSDDSpnENLTERVLQDAQRLFLMNDVVQPVTvdPYVTQDSIRFSKLVVDIVQGKDTLYHVM 431
Cdd:cd11238    315 SAWLPVlSSEVPEPRPGTCVNDS--ATLSDTVLHFARTHPLMDDAVSHGP--PLLYLRDVVFTHLVVDKLRIDDQEYVVF 390

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024422623  432 YIGTEYGTILKALSTTNRSLR-SCYLEEMQILPDgqrEAIKSLQILHSdRSLFVGLNNGVLKIPL 495
Cdd:cd11238    391 YAGSNDGKVYKIVHWKDAGESkSNLLDVFELTPG---EPIRAMELLPG-EFLYVASDHRVSQIDL 451
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
 67-495 3.05e-99

The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed predominantly in the nervous system during embryogenesis and it uses Plexin-A1 as a receptor. It displays repellent activity for dorsal root ganglion axons. Sema6D also acts as a regulator of late phase primary immune responses. In addition, Sema6D is overexpressed in gastric carcinoma, indicating that it may have an important role in the occurrence and development of the cancer. Sema6D is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200530 [Multi-domain]  Cd Length: 465  Bit Score: 321.59  E-value: 3.05e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFsQLALDAnRNQLIVGARNYLFRLSLHNVSLIQAT-----AWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKK-VFT 140
Cdd:cd11269     10 DF-QLMLKI-RDTLYIAGRDQVYTVNLNEVPKTEVTpsrklTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEmVFV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  141 CGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQYN 220
Cdd:cd11269     88 CGTNAFNPMCRYYRLSTLEYDGEEISGLARCPFDARQTNVALFAD-GKLYSATVADFLASDAVIYRSMGDGSALRTIKYD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  221 SKWLNEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGG-RFLLEDTWTTFMKARLNCSRAGEIPFYY 298
Cdd:cd11269    167 SKWIKEPHFLHAIEYGNYVYFFFREIAVEHnNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFFYF 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  299 NELQSTFYLPEQD---LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN---PIPNFQC----G 368
Cdd:cd11269    247 DVLQSITDIIEINgipTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEdkvPKPRPGCcakhG 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  369 TLSDDSPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRF--SKLVVDIVQGKDTLYHVMYIGTEYGTILKALST 446
Cdd:cd11269    327 LAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYrlTAIAVDHAAGPHQNYTVIFVGSEAGVVLKILAK 406

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024422623  447 TNR-SLR-SCYLEEMQILP----DGQREAIKSLQILHSDR---SLFVGLNNGVLKIPL 495
Cdd:cd11269    407 TSPfSLNdSVLLEEIEAYNhakcSAENEEDRRVISLQLDRdhhALFVAFSSCVVRIPL 464
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
 70-495 1.62e-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: 316.77  E-value: 1.62e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   70 QLALDANRNqLIVGARNYLFRLSLHNVS-----LIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKK-VFTCGT 143
Cdd:cd11267     12 QRVLRVNRT-LYIGDRDNLYRVELDPTAgtemrYHKKLTWRSNKNDINVCRMKGKHEGECRNFIKVLLLRDYGtLFVCGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  144 NAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQYNSKW 223
Cdd:cd11267     91 NAFNPVCANYSIDTLEPVGDNISGMARCPYDPKHANVALFAD-GMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKW 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  224 LNEPNFIAAYDIGLFTYFFFRENAVE-HDCGKTVYSRVARVCKNDIGG-RFLLEDTWTTFMKARLNCSRAGEIPFYYNEL 301
Cdd:cd11267    170 FKEPYFVHAVEWGSHVYFFFREIAMEfNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNVL 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  302 QST---FYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN-----PIPNFQCGTLSDD 373
Cdd:cd11267    250 QAVsdiLNLGGRPVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEelvprPRPGCCAAPGMRY 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  374 SPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRF--SKLVVDIVQGKDTLYHVMYIGTEYGTILKAL-----ST 446
Cdd:cd11267    330 NSSSTLPDEVLNFVKTHPLMDEAVPSLGHAPWIVRTMTRYqlTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLiipnaSS 409

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024422623  447 TNRSLRSCYLEEMQILPDG-------QREAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11267    410 SEISNQSVFLEELETYNPErcgwdspQAQKLLSLELDKGSGGLLLAFPSCVVRVPV 465
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
 68-498 6.21e-97

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: 315.70  E-value: 6.21e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   68 FSQLALDANRNQLIVGARNYLFRLSLHNVS-LIQATAWGSDEDTRRSCQSKGK-TEEECQNYVRVLIVYGKK-VFTCGTN 144
Cdd:cd11250     10 YDALLLDEERGRLFVGAKNYLASLSLDNISkQEKKIYWPAPVEWREECNWAGKdINTDCMNYVKILHHYNRThLYACGTG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  145 AFSPVCSSRQVG----------NLSKIIDrinGVARCPYDPRHNSTAVITSRgELYAATVIDFSGRDPAIYRSLGNVPPL 214
Cdd:cd11250     90 AFHPTCAFVEVGqrmedhvfrlDPSRVED---GKGKSPYDPRHTAASVLVGD-ELYSGVATDLMGRDFTIFRSLGQRPSL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  215 RTAQYNSKWLNEPNFIAAYDIGLF-------TYFFFRENAVE-HDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARL 286
Cdd:cd11250    166 RTEQHDSRWLNEPKFVKVFWIPESenpdddkIYFFFRETAVEaAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARL 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  287 NCSRAGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN 360
Cdd:cd11250    246 VCSVPGNegGDTHFDELRDVFLLQTRDkrnpLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQG 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  361 PIPNFQCG-----TLSDDSPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSI--RFSKLVVDIVQGKDTLYHVMYI 433
Cdd:cd11250    326 KVPYPRPGmcpskTFGSFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIpyTFTQIAVDRVAAADGHYDVMFI 405

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024422623  434 GTEYGTILKALSTTNRSLRS---CYLEEMQILPDGQreAIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11250    406 GTDVGSVLKVISVPKGSWPSneeLLLEELHVFKDSS--PITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
 68-498 2.10e-96

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: 315.02  E-value: 2.10e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   68 FSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGK-TEEECQNYVRVLIVYGKK-VFTCGTNA 145
Cdd:cd11249     32 YHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKWAGKdILKECANFIKVLKAYNQThLYACGTGA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  146 FSPVCSSRQVG-----NLSKIIDRI--NGVARCPYDPRHnSTAVITSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQ 218
Cdd:cd11249    112 FHPVCTYIEVGhhpedNIFRLEDSHfeNGRGKSPYDPKL-LTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQ 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  219 YNSKWLNEPNFIAAYDIGLF-------TYFFFRENAV--EHdCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCS 289
Cdd:cd11249    191 HDSRWLNDPRFISAHLIPESdnpeddkIYFFFRENAIdgEH-TGKATHARIGQLCKNDFGGHRSLVNKWTTFLKARLICS 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  290 RAGE--IPFYYNELQSTFYL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIP 363
Cdd:cd11249    270 VPGPngIDTHFDELQDVFLMnskdPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPFQGRVP 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  364 NFQCGTLSDDS-----PNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSI--RFSKLVVDIVQGKDTLYHVMYIGTE 436
Cdd:cd11249    350 YPRPGTCPSKTfggfdSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKTDVdyQFTQIVVDRVEAEDGQYDVMFIGTD 429

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024422623  437 YGTILKALST---TNRSLRSCYLEEMQILpdgqRE--AIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11249    430 MGTVLKVVSIpkeTWHDLEEVLLEEMTVF----REptAISAMELSTKQQQLYIGSAIGVSQLPLHRC 492
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
 70-495 1.97e-94

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


Pssm-ID: 200527 [Multi-domain]  Cd Length: 466  Bit Score: 308.50  E-value: 1.97e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   70 QLALDANRNqLIVGARNYLFRLSL-----HNVSLIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGK-KVFTCGT 143
Cdd:cd11266     12 QMIMIMNRT-LYIAARDHIYTVDIdtshtEEIYFSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKRNDdTLFVCGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  144 NAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVItSRGELYAATVIDFSGRDPAIYRSLGNVPPLRTAQYNSKW 223
Cdd:cd11266     91 NAFNPSCRNYKMDTLEFFGDEFSGMARCPYDAKHANVALF-ADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKW 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  224 LNEPNFIAAYDIGLFTYFFFRENAVE-HDCGKTVYSRVARVCKNDIGG-RFLLEDTWTTFMKARLNCSRAGEIPFYYNEL 301
Cdd:cd11266    170 LKEPYFVQAVDYGDYIYFFFREIAVEyNSMGKVVFPRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNIL 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  302 QS---TFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN---PIPNFQC----GTLS 371
Cdd:cd11266    250 QAvtdVIHINGRDVVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDervPKPRPGCcagsSSLE 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  372 DDSPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRF--SKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNR 449
Cdd:cd11266    330 KYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYrlTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARTGN 409

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024422623  450 S---LRSCYLEEMQILP------DG-QREAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11266    410 SgflNDSLFLEEMNVYNsekcsyDGvEDKRIMGMQLDKASSALYVAFSTCVIKVPL 465
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
 67-498 1.16e-86

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: 287.49  E-value: 1.16e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFSQLALDANRNQLIVGARNYLFRLSLHNVS---LIqaTAWGSDEDTRRSCQSKGK-TEEECQNYVRVLIVYGKK-VFTC 141
Cdd:cd11254      9 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWPASPQRIEECILSGKgSNGECGNFIRLIQPWNRThLYVC 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  142 GTNAFSPVCSSRQVGNLSK-IIDRI------NGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVPPL 214
Cdd:cd11254     87 GTGAYNPVCAYINRGRRAEdYMFRLepdkleSGKGKCPYDPKQDSVSALIN-GELYAGVYIDFMGTDAAIFRTMGKQPAM 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  215 RTAQYNSKWLNEPNFIAAYDIGLFT-------YFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLN 287
Cdd:cd11254    166 RTDQYNSRWLNDPAFVHAHLIPDSSeknddklYFFFREKSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLV 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  288 CSRAGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANP 361
Cdd:cd11254    246 CSVPGAdgIETHFDELRDVFIQPTQDtknpVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGK 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  362 IPNFQCGTLSDD--SPNENLTERVLQDAQRLF----LMNDVVQPVTVDPYV--TQDSIRFSKLVVDIVQGKDTLYHVMYI 433
Cdd:cd11254    326 IPYPRPGTCPGGtfTPSMKSTKDYPDEVINFMrthpLMYNAVYPVHRRPLVvrTNVNYRFTTIAVDQVDAADGRYEVLFL 405

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024422623  434 GTEYGTILKA--LSTTNRSLRSCYLEEMQILPdgQREAIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11254    406 GTDRGTVQKVivLPKDDLETEELTLEEVEVFK--VPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
 67-498 6.47e-84

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: 280.26  E-value: 6.47e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFSQLALDANRNQLIVGARNYLFRLSLHNVSL-IQATAWGSDEDTRRSCQSKGKTEE-ECQNYVRVLIVYGKK-VFTCGT 143
Cdd:cd11252      9 DFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKnPKKIYWPAAKERVELCKLAGKDANtECANFIRVLHPYNRThVYVCGT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  144 NAFSPVCSSRQVGNLSKiiDRI---------NGVARCPYDPRHNSTAVITSRgELYAATVIDFSGRDPAIYRSLGNVPP- 213
Cdd:cd11252     89 GAFHPTCGYIELGTHKE--DRIflldtqnleSGRLKCPFDPQQPFASVMTDE-YLYAGTASDFLGKDTTFTRSLGPTPDh 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  214 --LRTAQYNSKWLNEPNFIAAYDIGLF-------TYFFFRENAVEHDCG-KTVYSRVARVCKNDIGGRFLLEDTWTTFMK 283
Cdd:cd11252    166 hyIRTDISEHYWLNGAKFIGTFPIPDTynpdddkIYFFFREASQDGSTSdKSVLSRVGRVCKNDVGGQRSLINKWTTFLK 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  284 ARLNCSRAGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLP 357
Cdd:cd11252    246 ARLVCSIPGPdgADTHFDELQDIFLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWVQ 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  358 TANPIPNFQCGTL-----------SDDSPNEnlterVLQDAQRLFLMNDVVQPVTVDPYVTQDSI--RFSKLVVDIVQGK 424
Cdd:cd11252    326 YEGRIPYPRPGTCpsktydpliksTKDFPDE-----VISFIKRHPLMYKSVYPLTGGPVFTRINVdyRLTQIVVDHVAAE 400

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024422623  425 DTLYHVMYIGTEYGTILKALSTT--NRSLRSCYLEEMQILPdgQREAIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11252    401 DGQYDVMFLGTDIGTVLKVVSITkeKWTMEEVVLEELQIFK--HPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
 67-495 1.34e-81

The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed predominantly in the nervous system during embryogenesis. It binds Plexin A1 and might utilize it as a receptor to repel axons of specific types during development. Sema6E acts as a repellent to dorsal root ganglion axons as well as sympathetic axons. Sema6E is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200531 [Multi-domain]  Cd Length: 462  Bit Score: 273.52  E-value: 1.34e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFSQLALDANR----NQ-LIVGARNYLFRLSLHNV--SLI--QATAWGSDEdtRRSCQSKGKTEEECQNYVRVLIVYGKK 137
Cdd:cd11270      3 DTARLGLDFQRmlriNHmVYIAARDHVFAINLSASleRIVpqQKLTWKTKD--VEKCTVRGKNSDECYNYIKVLVPRNDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  138 VFT-CGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVPP-LR 215
Cdd:cd11270     81 TLFaCGTNAFNPTCRNYKMSSLEQDGEEVIGQARCPFESRQSNVGLFAG-GDFYSATMTDFLASDAVIYRSLGESSPvLR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  216 TAQYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDC-GKTVYSRVARVCKNDIGGR-FLLEDTWTTFMKARLNCSRAGE 293
Cdd:cd11270    160 TVKYDSKWLREPHFLHAIEYGNYVYFFLSEIAVEYTTlGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPGD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  294 IPFYYNELQST---FYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN---PIPNFQC 367
Cdd:cd11270    240 SFFYFDVLQSLtnvMQINHRPAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVPDeavPKPRPGS 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  368 ----GTLSDDSPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRF--SKLVVDIVQGKDTLYHVMYIGTEYGTIL 441
Cdd:cd11270    320 cagdGPAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFklTQIAVDTAAGPYKNYTVVFLGSENGHVL 399

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  442 KALS--TTNRSLRSCYLEEMQILPDG------QREAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11270    400 KVLAsmHPNSSYSTQVLEDIDVYNPNkcnvrgEDRRILGLELDKDHHALFVAFTGCVIRVPL 461
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
 60-495 2.54e-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: 272.89  E-value: 2.54e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVS---LIQATAWGSDEDTRRSCQSKGKT-EEECQNYVRVLI-VY 134
Cdd:cd11257      2 FEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISptgEQQELTWSADEEKKQECSFKGKDpQRDCQNYIKILLrLN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  135 GKKVFTCGTNAFSPVCSSRQVGNLSKIIDRI------NGVARCPYDPRHNSTAvITSRGELYAATVIDFSGRDPAIYRSL 208
Cdd:cd11257     82 STHLFTCGTYAFSPICTYIVMTNFSLERDEKgeplleDGKGRCPFDPEYKSTA-IMVDGELYTGTVSNFQGNDPIIYRSL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  209 GNVPPLRTAqyNS-KWLNEPNFIA-AYDIGLFT---------YFFFRENAVEHDC-GKTVYSRVARVCKNDIGGRFLLED 276
Cdd:cd11257    161 GSGTPLKTE--NSlNWLQDPAFVGsAYIQESLPklvgdddkiYFFFSETGKEFDFfENTIVSRIARVCKGDEGGERVLQK 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  277 TWTTFMKARLNCSRAGEiPFYYNELQSTFYLP--EQD----LIYGVFTTNVNSIAA--SAVCAFNLSAITQAFNGPFRYQ 348
Cdd:cd11257    239 RWTTFLKAQLLCSLPDD-GFPFNVLQDVFVLTpsPEDwkdtLFYGVFTSQWHKGTAgsSAVCVFTMDQVQRAFNGLYKEV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  349 ENPRSAWLPTANPIPNFQCGTLSDDSPNE-------NLTERVLQDAQRLFLMNDVVQPvtvDPYVTQDSIRFSKLVVDIV 421
Cdd:cd11257    318 NRETQQWYTYTHPVPEPRPGACITNSARErkinsslHMPDRVLNFVKDHFLMDGQVRS---QPLLLQPQVRYTQIAVHRV 394

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024422623  422 QGKDTLYHVMYIGTEYGTILKALSTTNRSLrscYLEEMQILPDGQreAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11257    395 KGLHKTYDVLFLGTDDGRLHKAVSVGPMVH---IIEELQIFSEGQ--PVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
 60-495 5.83e-80

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: 269.42  E-value: 5.83e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATA-WGSDEDTRRSCQSKGKTEE-ECQNYVRVLIVYGKK 137
Cdd:cd11259     12 FHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNALNISEKQHELyWKVSEDKRTKCAVKGKSKQtECRNYIRVLQPLNDT 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  138 -VFTCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNvPPLRT 216
Cdd:cd11259     92 fLYVCGTNAFQPTCDYLNLTSFRLLGKNEDGKGRCPFDPAQSYTSVMVD-GELYSGTSYNFLGSEPIISRNSSQ-SPLRT 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  217 aQYNSKWLNEPNFIAAYDIGL----------FTYFFFRENAVEHD-CGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKAR 285
Cdd:cd11259    170 -EYAIPWLNEPSFVFADVIRAdpdspdgeddKIYFFFTEVSVEYEfVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKAR 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  286 LNCSRAgEIPFYYNELQSTFYLPEQDL----IYGVFTTNVNSIAASAVCAFNLSAITQAFN-GPFRYQ---ENPRSAWLP 357
Cdd:cd11259    249 LICSIP-DKNLVFNVVNDVFILKSPTLkepvIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHTKWVR 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  358 TANPIPNFQCGTLSDD-------SPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKD-TLYH 429
Cdd:cd11259    328 YNGEVPKPRPGACINNearaanyTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDgTIYD 407

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024422623  430 VMYIGTEYGTILKALSTTNRSLrscYLEEMQILPDGQREAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11259    408 VMFISTDRGALHKAISLENEVH---IIEETQLFPDFEPVQTLLLSSKKGRRFLYAGSNSGVVQSPL 470
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
 60-495 7.87e-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: 268.32  E-value: 7.87e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATA---WGSDEDTRRSCQSKGKTEE-ECQNYVRVLIVY- 134
Cdd:cd11256      2 FRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTPGPIRLKHqipWPANDSKISECAFKKKSNEtECFNFIRVLVPVn 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  135 GKKVFTCGTNAFSPVCSSRQVGNLSKI-----IDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLG 209
Cdd:cd11256     82 GTHLYTCGTYAFSPACTYIELDHFSLPppngtIITMDGKGQSPFDPQHNYTAILVD-GELYTGTMNNFRGNEPIIFRNLG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  210 NVPPLRTAQYNsKWLN-EPNFIAAYDIGLFT--YFFFRENAVEHDC-GKTVYSRVARVCKNDIGGRFLLEDTWTTFMKAR 285
Cdd:cd11256    161 TKVSLKTDGFL-RWLNaDAVFVASFNPQGDSkvYFFFEETAREFDFfEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  286 LNCSRAGEIPFyyNELQSTFYLPEQD----LIYGVFTT--NVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWL--- 356
Cdd:cd11256    240 LTCSQQGHFPF--NVIHHVALLNQPDpnnsVFYAVFTSqwQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTrym 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  357 -PTANPIPNFQCGTLSDDspnenlteRVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDTLYH-VMYIG 434
Cdd:cd11256    318 gPVSDPRPGSCSGGKSSD--------KALNFMKDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSGHNYtVMFLG 389

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024422623  435 TEYGTILKALSTTNRSLRscYLEEMQILPDgqREAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11256    390 TDKGFLHKAVLMGGSESH--IIEEIELLTP--PEPVENLLLAANEGVVYIGYSAGVWRVPL 446
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
 64-498 3.80e-79

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: 267.10  E-value: 3.80e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   64 GVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSL-IQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKK-VFTC 141
Cdd:cd11253      6 GFLDLHTMLLDEYQERLFVGGRDLLYSLSLERISAnYKEIHWPSTQLQVEDCIMKGRDKPECANYIRVLHHYNRThLLAC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  142 GTNAFSPVCSSRQVGNLSKiiDRI---------NGVARCPYDPRHNSTAVITsRGELYAATVIDFSGRDPAIYRSLGNVP 212
Cdd:cd11253     86 GTGAFDPVCAFIRVGRGSE--DHLfqlesdkfeRGRGRCPFDPNSSFISTLI-GGELFVGLYSDYWGRDAAIFRTMNHLA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  213 PLRTAQYNSKWLNEPNFIAAYDI-------GLFTYFFFRENAVEHDCG-KTVYSRVARVCKNDIGGRFLLEDTWTTFMKA 284
Cdd:cd11253    163 HIRTEHDDERLLKEPKFVGSYMIpdnedpdDNKVYFFFTEKALEAEGGnHAIYTRVGRVCANDQGGQRMLVNKWSTFLKT 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  285 RLNCSRAGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPT 358
Cdd:cd11253    243 RLICSVPGPngIDTHFDELEDVFLLRTRDnknpEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVY 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  359 ANPIPNFQCG-----------TLSDDSPNEnlterVLQDAQRLFLMNDVVQPVTVDPYV--TQDSIRFSKLVVDIVQGKD 425
Cdd:cd11253    323 EGKVPYPRPGscaskvngghyGTTKDYPDE-----ALRFARSHPLMYQAVKPVHKRPILvkTDGKYNLKQIAVDRVEAED 397

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024422623  426 TLYHVMYIGTEYGTILKALSTTNR---SLRSCYLEEMQILPDgqREAIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11253    398 GQYDVLFIGTDNGIVLKVITIYNQeteTMEEVILEELQVFKV--PVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
 69-495 1.03e-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: 263.10  E-value: 1.03e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   69 SQLALDANR-----NQLIVGARNYLFRLSLH----NVSLI--QATAWGSDEdtRRSCQSKGKTEEECQNYVRVLIVY-GK 136
Cdd:cd11268      5 AELGLDFQRfltlnRTLLVAARDHVFSFDLQaeeeGEGLVpnKYLTWRSQD--VENCAVRGKLTDECYNYIRVLVPWdSQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  137 KVFTCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVItSRGELYAATVIDFSGRDPAIYRSLGNVPPLRT 216
Cdd:cd11268     83 TLLACGTNSFSPVCRSYGITSLQQEGEELSGQARCPFDATQSNVAIF-AEGSLYSATAADFQASDAVVYRSLGPQPPLRS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  217 AQYNSKWLNEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGGR-FLLEDTWTTFMKARLNCSRAGEI 294
Cdd:cd11268    162 AKYDSKWLREPHFVQALEHGDHVYFFFREVSVEDaRLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPGDS 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  295 PFYYNELQS---TFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTA-NPIPNFQCGTL 370
Cdd:cd11268    242 TFYFDVLQAltgPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVSeDRVPSPRPGSC 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  371 SDD------SPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDS-IRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKA 443
Cdd:cd11268    322 AGVggaalfSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLTLTSrALLTQVAVDGMAGPHSNITVMFLGSNDGTVLKV 401

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024422623  444 LSTTNRS--LRSCYLEEMQILP----DGQREA-----IKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11268    402 LPPGGRSggPEPILLEEIDAYSparcSGKRTAqtarrIIGLELDTEGHRLFVAFSGCIVYLPL 464
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
 67-498 1.75e-76

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: 259.82  E-value: 1.75e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFSQLALDANRNQLIVGARNYLFRLSLHNVSL-IQATAWGSDEDTRRSCQSKGKTEEE-CQNYVRVLIVYGKK-VFTCGT 143
Cdd:cd11251      9 DYRILFMDEDQDRIYVGSKDHILSLNINNISQdALSIFWPASASKVEECKMAGKDPTHgCGNFVRVIQPYNRThLYVCGS 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  144 NAFSPVCSSRQVGNLSKiiDRI--------NGVARCPYDPRHNSTAVITSRgELYAATVIDFSGRDPAIYRSLGNVPPLR 215
Cdd:cd11251     89 GAFSPVCVYVNRGRRSE--EQVfhidskaeSGKGRCSFNPNVNTVSVMINE-ELFSGMYIDFMGTDAAIFRSLTKRNAVR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  216 TAQYNSKWLNEPNFIAAYDIGLFT-------YFFFRENAVEHD-CGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLN 287
Cdd:cd11251    166 TDQHNSKWLSEPIFVDAHLIPDGTdpndaklYFFLKERLTDNSgSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKARLV 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  288 CSRAGE--IPFYYNELQSTFYL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANP 361
Cdd:cd11251    246 CSVMDEdgTETHFDELEDVFLLetdnPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQGR 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  362 IPNFQCGTLSDD--SPNENLTERVLQDAQRLF----LMNDVVQPVTVDPYV--TQDSIRFSKLVVDIVQGKDTLYHVMYI 433
Cdd:cd11251    326 IPYPRPGTCPGGafTPNMQSTKEFPDDVVTFIrnhpLMFNPIYPIGRRPLLvrTGTDYKYTKIAVDRVNAADGRYHVLFL 405

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024422623  434 GTEYGTILK--ALSTTNRSLRSCYLEEMQILPDgqREAIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11251    406 GTDKGTVQKvvVLPTNGSLSGELILEELEVFKN--HAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
 60-495 7.15e-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: 257.53  E-value: 7.15e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQAT-AWGSDEDTRRSCQSKGK-TEEECQNYVRVLIVYGK- 136
Cdd:cd11260      1 FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKvLWEVTEEKQKDCTNKGKhADIDCHNYIRILHKMNDs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  137 KVFTCGTNAFSPVCS--SRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSlgNVPPL 214
Cdd:cd11260     81 RMYVCGTNAFSPTCDyiSYDDGQLTLEGKQEDGKGKCPFDPFQRYSSVMVD-QDLYSATSMNFLGSEPVIMRS--SPITI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  215 RTaQYNSKWLNEPNFIAAYDIGLF----------TYFFFRENAVEHDC-GKTVYSRVARVCKNDIGGRFLLEDTWTTFMK 283
Cdd:cd11260    158 RT-EFKSSWLNEPNFIYMAAVPESedspegdddkIYLFFSETAVEYDFyNKLVVSRVARVCKGDLGGQRTLQKKWTSFLK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  284 ARLNCS-RAGEIPFYyneLQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFN-GPFRYQENPRSA--- 354
Cdd:cd11260    237 ARLDCSvPEPSLPYV---IQDVFHVCHQDwrkcVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrGKFKTPVAVETSfvk 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  355 WLPTANPIPNFQCGTLSDDSPNE-------NLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKD-T 426
Cdd:cd11260    314 WVMYSGELPVPRPGACINNAARTsgikkslNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADgQ 393

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024422623  427 LYHVMYIGTEYGTILKALSttnrslrscYLEEMQILPDGQ----REAIKSLQIlhSDRSLFVGLNNGVLKIPL 495
Cdd:cd11260    394 SYPVMFIGTANGYVLKAVN---------YDGEMHIIEEVQlfepEEPIDILRL--SQNQLYAGSASGVVQMPV 455
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
 57-495 1.78e-73

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: 250.87  E-value: 1.78e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   57 VSNFTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSLIQATAWGSDEDTRRSCQSKGKTEE-ECQNYVRVLIVYG 135
Cdd:cd11258      1 VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQtECFNYIRFLQPYN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  136 KK-VFTCGTNAFSPVCSSRQVGNLSkiIDRIN---GVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNV 211
Cdd:cd11258     81 QShLYTCGTYAFQPKCAYINMLTFT--LDRAEfedGKGKCPYDPAKGHTGLIVD-GELYSATLNNFLGTEPVILRNLGQH 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  212 PPLRTaQYNSKWLNEPNFI-AAY---DIGLFT------YFFFRENAVEHDC-GKTVYSRVARVCKNDIGGRFLLEDTWTT 280
Cdd:cd11258    158 YSMKT-EYLAFWLNEPHFVgSAFvpeSVGSFTgdddkiYFFFSERAVEYDCdSEQVVARVARVCKGDLGGARTLQKKWTT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  281 FMKARLNCSrAGEIPFYYNELQSTFYLPEQDL----IYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWL 356
Cdd:cd11258    237 FLKARLLCS-IPEWQLYFNQLKAVFTLEGASWrnttFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  357 PTANPIPNFQCGT--LSDDSPNENLTERVLQDAQRLF-----LMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKD-TLY 428
Cdd:cd11258    316 RYTDPVPSPRPGSciNNWHRDHGYTSSLELPDNTLNFvkkhpLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGLDgETY 395

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024422623  429 HVMYIGTEYGTILKALSTTNrslRSCYLEEMQILpdGQREAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11258    396 SVLFIGTLDGWLIKAVSLGS---WVHMIEELQVF--DQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
 64-498 3.63e-73

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: 250.60  E-value: 3.63e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   64 GVHDFSQLALDANRNQLIVGARNYLFRLSLHNVSL-IQATAWGSDEDTRRSCQSKGKTEE-ECQNYVRVLIVYGKK-VFT 140
Cdd:cd11255      6 GDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPdAKEIHWPPLPGQREECIRKGKDPEtECANFVRVLQPFNRThLLA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  141 CGTNAFSPVCSSRQVGNLSKIIDRI------NGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVPPL 214
Cdd:cd11255     86 CGTGAFQPVCALINVGHRGEHVFSLdpttveSGRGRCPHEPKRPFASTFTG-GELYTGLTADFLGRDSVIFRGFGTRSPL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  215 RTaQYNSKWLNEPNFIAAYDI-------GLFTYFFFRENAVEHDCGK--TVYSRVARVCKNDIGGRFLLEDTWTTFMKAR 285
Cdd:cd11255    165 RT-ETDQRLLHEPRFVAAHLIpdnadrdNDKVYFFFTERATETAEDDdgAIHSRVGRLCANDAGGQRVLVNKWSTFIKAR 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  286 LNCSRAGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTA 359
Cdd:cd11255    244 LVCSVPGPhgIQTHFDQLEDVFLLRTKDgkspEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPYE 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  360 NPIPNFQCGTLSDDSPNE---------NLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSI--RFSKLVVDIVQGKDTLY 428
Cdd:cd11255    324 GKVPYPRPGVCPSKITAQpgrafrstkDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLpyRLTQIVVDRVEAEDGYY 403

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024422623  429 HVMYIGTEYGTILKALST---TNRSLRSCYLEEMQILPdgQREAIKSLQILHSDRSLFVGLNNGVLKIPLERC 498
Cdd:cd11255    404 DVMFIGTDSGSVLKVIVLqkgNSAAGEEVTLEELQVFK--VPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
 67-495 1.27e-71

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: 245.83  E-value: 1.27e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFSQLALDANRNQLIVGARNYLFRLSLHNVS--LIQATAWGSDEDTRRSCQSKGKTEE-ECQNYVRVLIVYGKK-VFTCG 142
Cdd:cd11262      9 NYSTLLLEDESGRLYVGARGAIFSLNASDISdsSALTIDWEASPEQKHQCLKKGKNNQtECFNHVRFLQRFNSThLYTCG 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  143 TNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRdPAIYRSLGNvPPLRTAQYNSK 222
Cdd:cd11262     89 THAFRPLCAYIDAERFTLSSQFEEGKEKCPYDPAKGYTGLIVD-GQLYTASQYEFRSF-PDIRRNSPQ-PTLRTEEAPTR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  223 WLNEPNFIAAY----DIGLFT------YFFFRENAVEhdcgKTVY------SRVARVCKNDIGGRFLLEDTWTTFMKARL 286
Cdd:cd11262    166 WLNDADFVGSVlvreSMNSSVgdddkiYFFFTERSQE----ETAYfsqsrvARVARVCKGDRGGKKTLQRKWTSFLKARL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  287 NCSrageIPFY---YNELQSTFYL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTA 359
Cdd:cd11262    242 VCY----IPEYeflFNVLRSVFVLwgstPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYT 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  360 NPIPNFQCGTLSDDS-------PNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKD-TLYHVM 431
Cdd:cd11262    318 GKVPEPRPGSCITDEhrsqginSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQTVRGLDgRVYDVL 397

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024422623  432 YIGTEYGTILKALsttNRSLRSCYLEEMQILPDGQreAIKSLQILHSDRSLFVGLNNGVLKIPL 495
Cdd:cd11262    398 FLGTDEGWLHKAV---VIGSAVHIIEELQVFREPQ--PVENLVISKKQNSLYVGARSGVVQVPL 456
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
 67-496 1.26e-66

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: 229.78  E-value: 1.26e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   67 DFSQLALDANRNQLIVGARNYLFRLSLHNVSL-----IQATAWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKK--VF 139
Cdd:cd09295      1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLllsciSPELNFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGDLdiLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTNAFSPVCSSRQVGNLSKIID--RINGVARCPYDPRHNSTAVITsRGELYAATVIDF-SGRDPAIYRSLGNVPPLRT 216
Cdd:cd09295     81 VCGSNAAQPSCGSYRLDVLVELGKvrWPSGRPRCPIDNKHSNMGVNV-DSKLYSATDHDFkDGDRPALSRRSSNVHYLRI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  217 AQYNSKWLNEPNFIAAYDIGL---FTYFFFRENAVEHDCGKTVY-SRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRAG 292
Cdd:cd09295    160 VVDSSTGLDEITFVYAFVSGDdddEVYFFFRQEPVEYLKKGMVYvPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSRPQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  293 EiPFYYNELQSTFYL---PEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENprSAWLPTANpipnfqcgt 369
Cdd:cd09295    240 S-GFAFNLLQDATGDtknLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVFDDPVEAINN--RPLYAHQN--------- 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  370 lsddspnenltervlqdaqrlflmndvvqpvtvdpyvtqDSIRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALStTNR 449
Cdd:cd09295    308 ---------------------------------------QRSRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKALA-FFF 347

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2024422623  450 SLRSCYLEEMQILPDGQReaIKSLQILHSDRSLFVGLNNGVLKIPLE 496
Cdd:cd09295    348 LYKGHIIEEWKVFKDSSR--ITNLDLSRPPLYLYVGSESGVLGVPVQ 392
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
 55-494 2.71e-66

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: 230.93  E-value: 2.71e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   55 PWVSNFTYPGVHDFSQLALDANRNQLIVGARNYLFRLSLHNVS-LIQATAWGSDEDTRRSCQSKGKTEEECQNYVRVL-I 132
Cdd:cd11261      1 SALTRFSAPHTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGeRPRRIDWMVPEAHRQNCRKKGKKEAECHNFIRILaI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  133 VYGKKVFTCGTNAFSPVCSSRQVGNLSKIIDRINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGNVP 212
Cdd:cd11261     81 ANASHLLTCGTFAFDPKCGVIDVSSFQQVERLESGRGKCPFEPAQRSAAIMAG-GVLYAATVKNFLGTEPIISRAVGRAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  213 PLRTAQYNSKWLNEPNFIAAYDIGLFT----------YFFFRENAVEHDCGKTV-YSRVARVCKNDIGGRFLLEDTWTTF 281
Cdd:cd11261    160 EWIRTETLPSWLNAPAFVAAVFLSPAEwgdedgddeiYFFFTETAREYDSYERIkVPRVARVCAGDLGGRKTLQQRWTTF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  282 MKARLNCS--RAGEIpfyYNELQSTFYLPEQD-----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSA 354
Cdd:cd11261    240 LKADLLCPgpEHGRA---SSILQDVTTLRPLPgagtpIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  355 WLP-TANPIPNFQCGTLSDDS-------PNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLV---VDIVQG 423
Cdd:cd11261    317 GLPvMDSDVPQPRPGECITNNmkllgfgSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAahrVTSLSG 396

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  424 KDtlYHVMYIGTEYGTILKALSTTNR-SLrscyLEEMQILPDGQreAIKSLQILHSdrSLFVGLNNGVLKIP 494
Cdd:cd11261    397 KE--YDVLYLGTEDGHLHRAVRIGAQlSV----LEDLALFPEPQ--PVENLQLHHN--WLLVGSDTEVTQIN 458
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
 301-477 4.18e-56

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: 192.10  E-value: 4.18e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  301 LQSTFYLPE------QDLIYGVFTTN-VNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLSDD 373
Cdd:pfam01403    1 LQDVFVLKPgagdalDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  374 SPNENLTERVLQDAQRLFLMNDVVQPVTVDPYVTQDSIRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSlrS 453
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEE--S 158

                          170       180
                   ....*....|....*....|....
gi 2024422623  454 CYLEEMQILPDGQreAIKSLQILH 477
Cdd:pfam01403  159 HIIEEIQVFPEPQ--PVLNLLLSS 180
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
 73-496 2.23e-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: 2.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   73 LDANRNQLIVGARNYLFRLSLHNVSLIQATAwgSDEDTRRSCQSKGkTEEECQNYVRVLIVYGKKVFTCGTNAFSPVCSS 152
Cdd:cd11243      9 HEAGSSSVYVGGQGALYLLDFTGSAVIVKKI--PDEKTEKDCKKRA-TLDDCENYITLIKKLDYRLLVCGTNAGSPKCWF 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  153 RQVGNLSKIIDrINGVArcPYDPRHNStAVITSRGELYAAtvIDFSGRDPAIYRSLGNVPPLRTAqynSKWLNEPNFIAA 232
Cdd:cd11243     86 LVNQTLVTLSA-DRGVA--PFLPDENS-LVLIEGNNVYST--ISGKKGNIPRFRRYGGKKELYTS---DTVMQKPQFVKA 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  233 --------YDIGLftYFFFRENAVEHDCGKTVY-SRVARVCKNDIGGRFLLE-DTWTTFMKARLNCSRAGEiPFYYNELQ 302
Cdd:cd11243    157 tllpedeqYQDKI--YYFFREDNEDKGPEAEPNiSRVARLCKEDQGGTSSLStSKWSTFLKARLVCGDPAT-PMNFNRLQ 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  303 STFYLP----EQDLIYGVFTTNVNSiaaSAVCAFNLSAITQAFngpfryqenpRSAWLPTAN-PIPNFQCGT-LSDDSPN 376
Cdd:cd11243    234 DVFLLPkeewREAVVYGVFSNTWGS---SAVCSYSLGDIDKVF----------RTSSLKGYSgSLPNPRPGTcVPPEQTH 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  377 enlTERVLQDAQRLFLMNDVVQPVTVDP-YVTQDSIRFSKLVVDIVQGKDTL-YHVMYIGTEYGTILKALSTTNRSLRSc 454
Cdd:cd11243    301 ---PSETFSFADEHPELDDRIEPDEPRKlPVFQNKDHYQKVVVDEVRASDGVsYDVLYLATDKGKIHKVVESKGQTHNI- 376

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2024422623  455 yleeMQILPDGQREAIKSLQILHSDRSLFVGLNNGVLKIPLE 496
Cdd:cd11243    377 ----MEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPLD 414
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 855-907 1.19e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.19e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   855 WSCWTPWSQCSATCGGGHYQRTRTCTNPAPSSGEDICIGLHTEEALCNTHPCE 907
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 798-850 3.03e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 3.03e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   798 WSFWGAWSSCSRDCELGFRIRKRTCTNPEPKNGGLPCVGSAMEYQDCNPHPCP 850
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 609-662 7.07e-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: 69.54  E-value: 7.07e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2024422623   609 WTPWSSWALCSTSCGIGFQVRQRSCSNPAPRYGGRVCVGQSREERFCNENsPCP 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 8.19e-14

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: 74.67  E-value: 8.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   71 LALDANRNQLIVGARNYLFRLSlHNVSLIQATAWGSDEDTRR----SCQSKGKTEEECQNYVRVLIVY--GKKVFTCGTn 144
Cdd:cd11236      5 LAVDNSTGRVYVGAVNRLYQLD-SSLLLEAEVSTGPVLDSPLclppGCCSCDHPRSPTDNYNKILLIDysSGRLITCGS- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  145 AFSPVCSSRQVGNLSKIIDRI--NGVARCPYDprhnSTAVITSRGE------LYAATVIDFSGRDPAIY----RSLGNVP 212
Cdd:cd11236     83 LYQGVCQLRNLSNISVVVERSstPVAANDPNA----STVGFVGPGPynnenvLYVGATYTNNGYRDYRPavssRSLPPDD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  213 PLRTAQYN--SKWLNEPNFIAAYDI--------GLFTYFFFRENAVeHDCGKTVYSRVARVCKNDIGgrflledtWTTFM 282
Cdd:cd11236    159 DFNAGSLTggSAISIDDEYRDRYSIkyvygfssGGFSYFVTVQRKS-VDDESPYISRLVRVCQSDSN--------YYSYT 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024422623  283 KARLNCsrAGEIPFYYNELQStFYLPE--------------QDLIYGVFTTNVNSIAA----SAVCAFNLSAITQAFN 342
Cdd:cd11236    230 EVPLQC--TGGDGTNYNLLQA-AYVGKagsdlarslgistdDDVLFGVFSKSKGPSAEpsskSALCVFSMKDIEAAFN 304
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 667-713 6.58e-12

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 61.45  E-value: 6.58e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 2024422623   667 WSSWGPWNKCSVNCGGGIHSRQRTCEN------GNTCPGCAVEYKTCNPESCP 713
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqngGGPCTGEDVETRACNEQPCP 53
Sema_plexin_B3 cd11277
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of ...
 60-401 2.05e-10

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: 64.06  E-value: 2.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   60 FTYPGVhDFSQLALDANRNQLIVGARNYLFRLSlhnvSLIQATAW---GSDEDT--------RRSCQSKGKTEeecqNYV 128
Cdd:cd11277      1 FSAPNA-TFNHLALDPGSGTLYVGAVNRLYQLS----PDLQLLGEavtGPVLDSpdclpfrdPADCPQARLTD----NAN 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  129 RVLIV--YGKKVFTCGTnAFSPVCSSRQVGNLSKIIDRingvarcPYDPRHNSTAVITSRGELYAATVIDFSGRDPA-IY 205
Cdd:cd11277     72 KLLLVseRAGELVACGQ-VRQGVCEKRRLGNVAQVLYQ-------AEDPGDGQFVAANDPGVATVGLVVEAPGRDLLlVG 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  206 RSL-----GNVPPLRTAQ----------------------YNSkwlnepNFIAAYDIGLFTYFFFRENAVEhdcGKTVY- 257
Cdd:cd11277    144 RGLtgklsAGIPPLTIRQlagaqafsseglgklvvgdfsdYNN------SYVGAFAHNGYVYFLFRRRGAR---AQAEYr 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  258 SRVARVCKNDIggrFLLedtwtTFMKARLNCsRAGeipfyYNELQSTFYLPEQDLIYGVFTTNVNSIAA----SAVCAFN 333
Cdd:cd11277    215 TYVARVCLGDT---NLY-----SYVEVPLVC-QGG-----YNLAQAAYLAPGQGTLFVVFAAGQGSTPTptdqTALCAYP 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  334 LSAI------------TQAFNGP-------FRYQENPRSAWLPTANPiPNFQCGTLSDDSPnenLTERVLQDAQRLFlmn 394
Cdd:cd11277    281 LVELdsamerarrlcyTAGGGGPngkeeatIEYGVTSRCVNLPKDSP-ESYPCGDEHTPSP---IASRQPLEAEPLL--- 353


                   ....*..
gi 2024422623  395 DVVQPVT 401
Cdd:cd11277    354 TLTPPLT 360
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
 68-375 5.38e-10

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: 63.03  E-value: 5.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   68 FSQLALDANRNQLIVGARNYLFRLSlHNVSLIQATAWGSDEDTRRsCQSKgKTEEEC------QNYVRVLIV--YGKKVF 139
Cdd:cd11245      2 INHLAQDPQTGRLYLGAVNGLFQLS-PNLQLESRADTGPKKDSPQ-CLPP-ITAAECpqaketDNFNKLLLVnsANGTLV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTnAFSPVCSSRQVGNLSKIIDRINGVARCPY----DPRHNSTAVITSRGelyAATVIDFSGRDPAiYRSLGNVPPLR 215
Cdd:cd11245     79 VCGS-LFQGVCELRNLNSVNKPLYRPETPGDKQYvaanEPSVSTVGLISYFK---DGLSLLFVGRGYT-SSLSGGIPPIT 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  216 TAQynskwLNEP------------------------NFIAAYDIGLFTYFFFRENAVEHDCGKTVYsrVARVCKNDiggr 271
Cdd:cd11245    154 TRL-----LQEHgemdafsneveaklvvgsasryhhDFVYAFADNGYIYFLFSRRPGTADSTKRTY--ISRLCEND---- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  272 flleDTWTTFMKARLNCSRAGEipFYYNELQSTFYLP-----EQDLIYGVFTTNVNSIAA----SAVCAFNLSAITQAFN 342
Cdd:cd11245    223 ----HHYYSYVELPLNCTVNQE--NTYNLVQAAYLAKpgkvlNGKVLFGVFSADEASTAApdgrSALCMYPLSSVDARFE 296

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2024422623  343 --------GPFRYQENPRSAWLPTANpipNFQCGTLSDDSP 375
Cdd:cd11245    297 rtrescytGEGLEDDKPETAYIEYNV---KSICKTLPDKNV 334
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 497-544 1.48e-08

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 51.94  E-value: 1.48e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  497 RCSMYRTEGECLGARDPYCGWDNKQKRCTTIED----SSNMSLWTQNITECP 544
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRRSAcgapEGNCEEWEQASSKCP 52
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
 68-517 1.67e-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: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623   68 FSQLALDANRNQLIVGARNYLFRLSlHNVSLIQATAWGSDEDTRrSC------QSKGKTEEECQNYVRVLIV-YGK-KVF 139
Cdd:cd11272     13 FNHLTVHQSTGAVYVGAINRVYKLS-GNLTILVAHKTGPEEDNK-SCypplivQPCSEVLTLTNNVNKLLIIdYSEnRLL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  140 TCGTnAFSPVCSSRQVGNLSKIIDRINgvARCPYDPRHNSTA-----VITSRGE---LYAATVIDfsGRD---PAIY-RS 207
Cdd:cd11272     91 ACGS-LYQGVCKLLRLDDLFILVEPSH--KKEHYLSSVNKTGtmygvIVRSEGEdgkLFIGTAVD--GKQdyfPTLSsRK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  208 LGNVPPLRT-------AQYNSKWLNEPN----FIAAYDI--------GLFTYFFF-----RENAVEHDCGKTVY-SRVAR 262
Cdd:cd11272    166 LPRDPESSAmldyelhSDFVSSLIKIPSdtlaLVSHFDIfyiygfasGNFVYFLTvqpetPEGVSINSAGDLFYtSRIVR 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  263 VCKNDiggrflleDTWTTFMKARLNCSRAGEipfYYNELQSTfYLP--------------EQDLIYGVFTTNVNSIAA-- 326
Cdd:cd11272    246 LCKDD--------PKFHSYVSLPFGCVRGGV---EYRLLQAA-YLSkpgevlarslnitaQEDVLFAIFSKGQKQYHHpp 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  327 --SAVCAFNLSAITQAFNGPFR--YQE--NPRSAWL------PTANPIP---NFqCGTlsddSPNENLTERVLQDAQRLF 391
Cdd:cd11272    314 ddSALCAFPIRAINAQIKERLQscYQGegNLELNWLlgkdvqCTKAPVPiddNF-CGL----DINQPLGGSTPVEGVTLY 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024422623  392 lmndvvqpvtvdpyvTQDSIRFSKLVVDIVQGkdtlYHVMYIGTEYGTiLKALSTTNRSLRSCYLEEMQILPDGQrEAIK 471
Cdd:cd11272    389 ---------------TSSRDRLTSVASYVYNG----YSVVFVGTKSGK-LKKIRADGPPHGGVQYEMVSVFKDGS-PILR 447

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2024422623  472 SLQILHSDRSLFVGLNNGVLKIPLERCSMYRTEGECLGARDPYCGW 517
Cdd:cd11272    448 DMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDPHCGW 493
TSP_1 pfam00090
Thrombospondin type 1 domain;
856-906 2.43e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.88  E-value: 2.43e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024422623  856 SCWTPWSQCSATCGGGHYQRTRTCTNPAPSSGEdiCIGLHTEEALCNTHPC 906
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEP--CTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
799-849 5.54e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 50.11  E-value: 5.54e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024422623  799 SFWGAWSSCSRDCELGFRIRKRTCTNPEPKNGglPCVGSAMEYQDCNPHPC 849
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
668-712 6.35e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 49.72  E-value: 6.35e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024422623  668 SSWGPWNKCSVNCGGGIHSRQRTC----ENGNTCPGCAVEYKTCNPESC 712
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 801-849 6.38e-08

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 49.97  E-value: 6.38e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024422623  801 WGAWSSCSRDCELGFRIRKRTCTNPePKNGGLPCvGSAMEYQDCNPHPC 849
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
610-661 2.66e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.18  E-value: 2.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  610 TPWSSWALCSTSCGIGFQVRQRSCSNPAPryGGRVCVGQSREERFCNeNSPC 661
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACK-MDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 858-906 3.06e-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: 48.04  E-value: 3.06e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024422623  858 WTPWSQCSATCGGGHYQRTRTCTNPAPSSGEDiCiGLHTEEALCNTHPC 906
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVEPQNGGRP-C-PELLERRPCNLPPC 52
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
497-534 6.62e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 46.77  E-value: 6.62e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2024422623   497 RCSMYRTEGECLGARDPYCGWDNKQKRCTTIEDSSNMS 534
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRR 38
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 610-661 1.16e-06

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 46.50  E-value: 1.16e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  610 TPWSSWALCSTSCGIGFQVRQRSCSNPaPRYGGRVCVGQSrEERFCNENsPC 661
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELL-ERRPCNLP-PC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 910-951 2.24e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 2.24e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2024422623   910 WSEWSEWSLCNE---EGIQYRSRYCEVHSP--DSSQCVGNSTQYQDC 951
Cdd:smart00209    1 WSEWSEWSPCSVtcgGGVQTRTRSCCSPPPqnGGGPCTGEDVETRAC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 555-606 6.53e-06

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.50  E-value: 6.53e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623   555 GPWSPWQPCEHSDGDSTgscMCRSRSCDSPRPRCGGRSCEGARIEVANCSRN 606
Cdd:smart00209    2 SEWSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 668-712 8.41e-05

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: 41.11  E-value: 8.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024422623  668 SSWGPWNKCSVNCGGGIHSRQRTC-----ENGNTCPGcAVEYKTCNPESC 712
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVivepqNGGRPCPE-LLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
908-951 2.50e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.71  E-value: 2.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024422623  908 GGWSEWSEWSLCNEEGIQYRSRYCEVHSPDSSQCVGNSTQYQDC 951
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQAC 44
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 610-661 4.24e-04

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 39.36  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024422623  610 TPWSSwalCSTSCGIGFQVRQRSCSNPAPR--YGGRVCVGQSR--EERFCNeNSPC 661
Cdd:pfam19030    4 GPWGE---CSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCN-LKPC 55
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 670-720 5.74e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 43.80  E-value: 5.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  670 WGPWNKCSVNCGGGIHSRQRTCENgntcPGCAVEY-KTCNPESCPEVRRNTP 720
Cdd:PTZ00441   243 WDEWTPCSVTCGKGTHSRSRPILH----EGCTTHMvEECEEEECPVEPEPLP 290
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 859-906 1.03e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 38.20  E-value: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024422623  859 TPWSQCSATCGGGHYQRTRTCTNPAPSSGED--ICIGLH--TEEALCNTHPC 906
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGGSIVPdsECSAQKkpPETQSCNLKPC 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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