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Conserved domains on  [gi|1622942836|ref|XP_028704925|]
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semaphorin-5A isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
 50-485 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: 973.35  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 129
Cdd:cd11263      1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 209
Cdd:cd11263     81 TCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  210 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 289
Cdd:cd11263    161 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  290 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGTVDQGLYVNLT 369
Cdd:cd11263    241 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  370 ERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTASSCLLEEIE 449
Cdd:cd11263    321 ERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEIE 400

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1622942836  450 LFPERRREPIRSLQILHSQSVLLVGLWEHVVKIPLK 485
Cdd:cd11263    401 LFPKRQREPIRSLQILHSQSVLFVGLQEHVIKIPLK 436
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 850-902 2.23e-17

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 76.86  E-value: 2.23e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   850 WSCWSPWTKCSATCGGGHYMRTRSCSNPAPAYGGDICLGLHTEEALCNTQPCP 902
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 793-845 1.64e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.64e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   793 WSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEYQECNILPCP 845
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 598-657 1.25e-13

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 66.07  E-value: 1.25e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   598 WTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERKihpalyCNEHlLCP 657
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRA------CNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 662-708 2.02e-12

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.60  E-value: 2.02e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   662 WTGWGPWERCTAQCGGGIQARRRTCENGP------DCAGCNVEYQPCNTNPCP 708
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggPCTGEDVETRACNEQPCP 53
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 486-533 6.08e-08

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


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 50.01  E-value: 6.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622942836  486 RCQFYRTHSTCIGAQDPYCGWDVVMKKCTS----LEESLSMTQWEQSISACP 533
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 546-595 7.05e-08

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.89  E-value: 7.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622942836   546 WSPWTPCTHTDGSAVgscLCRTRSCDSPAPQCGGWQCEGPSMEIANCSRN 595
Cdd:smart00209    4 WSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
906-949 9.18e-07

Thrombospondin type 1 domain;


:

Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.64  E-value: 9.18e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622942836  906 SEWSDWSECEAS---GVQVRARQCILLFPVGSQCSGNTTESRPCVFD 949
Cdd:pfam00090    1 SPWSPWSPCSVTcgkGIQVRQRTCKSPFPGGEPCTGDDIETQACKMD 47
 
Name Accession Description Interval E-value
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
 50-485 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: 973.35  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 129
Cdd:cd11263      1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 209
Cdd:cd11263     81 TCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  210 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 289
Cdd:cd11263    161 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  290 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGTVDQGLYVNLT 369
Cdd:cd11263    241 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  370 ERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTASSCLLEEIE 449
Cdd:cd11263    321 ERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEIE 400

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1622942836  450 LFPERRREPIRSLQILHSQSVLLVGLWEHVVKIPLK 485
Cdd:cd11263    401 LFPKRQREPIRSLQILHSQSVLFVGLQEHVIKIPLK 436
Sema smart00630
semaphorin domain;
58-460 2.12e-128

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 396.35  E-value: 2.12e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836    58 FSQLTFDPGQKELVVGARNYLFRLQLEDLSLI-QAVEWECDEATKKACYSKGKSK-EECQNYIRVLL-VGGDRLFTCGTN 134
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   135 AFTPVCTNRSLsnlteihdqisgmarcpyspqhnstalltagGELYAATAMDFPGRDPAIYRSLGILP-------PLRTA 207
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTV 129

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   208 QYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPF 286
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   287 YYNELQSTFFLPEL----DLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPN-PNPNFQCGTVD 361
Cdd:smart00630  210 YFNELQAAFLLPPGsesdDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   362 QGLY--VNLTERNLQDAQKFILMHEVVQPVTTVPSFME--DNSRFSHVVVDVVQGREAlVHIIYLATDYGTIKKVRAPLN 437
Cdd:smart00630  290 NKPPssKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKtdSNYLLTSIAVDRVATDGN-YTVLFLGTSDGRILKVVLSES 368

                           410       420
                    ....*....|....*....|....
gi 1622942836   438 QTAS-SCLLEEIELFPErrREPIR 460
Cdd:smart00630  369 SSSSeSVVLEEISVFPD--GSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
 291-466 2.57e-50

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: 175.54  E-value: 2.57e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  291 LQSTFFLPEL------DLIYGIFTTN-VNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGT-VDQ 362
Cdd:pfam01403    1 LQDVFVLKPGagdaldTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTcIND 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  363 GLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTasS 442
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEE--S 158

                          170       180
                   ....*....|....*....|....
gi 1622942836  443 CLLEEIELFPErrREPIRSLQILH 466
Cdd:pfam01403  159 HIIEEIQVFPE--PQPVLNLLLSS 180
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 850-902 2.23e-17

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 76.86  E-value: 2.23e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   850 WSCWSPWTKCSATCGGGHYMRTRSCSNPAPAYGGDICLGLHTEEALCNTQPCP 902
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 793-845 1.64e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.64e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   793 WSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEYQECNILPCP 845
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 598-657 1.25e-13

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 66.07  E-value: 1.25e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   598 WTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERKihpalyCNEHlLCP 657
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRA------CNEQ-PCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 662-708 2.02e-12

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.60  E-value: 2.02e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   662 WTGWGPWERCTAQCGGGIQARRRTCENGP------DCAGCNVEYQPCNTNPCP 708
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
851-901 2.44e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 2.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622942836  851 SCWSPWTKCSATCGGGHYMRTRSCSNPAPayGGDICLGLHTEEALCNTQPC 901
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
794-844 5.90e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.81  E-value: 5.90e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622942836  794 SAWTSWSQCSRDCSRGIRNRKRVCNNPEPkyGGMPCLGPSLEYQECNILPC 844
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
599-643 2.37e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 2.37e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622942836  599 TPWTSWSPCSTTCGIGFQVRQRSCSNPTPrhGGRVCVGQNREERK 643
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQA 43
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 486-533 6.08e-08

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 50.01  E-value: 6.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622942836  486 RCQFYRTHSTCIGAQDPYCGWDVVMKKCTS----LEESLSMTQWEQSISACP 533
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 546-595 7.05e-08

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.89  E-value: 7.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622942836   546 WSPWTPCTHTDGSAVgscLCRTRSCDSPAPQCGGWQCEGPSMEIANCSRN 595
Cdd:smart00209    4 WSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
665-707 1.93e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.57  E-value: 1.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622942836  665 WGPWERCTAQCGGGIQARRRTC----ENGPDCAGCNVEYQPCNTNPC 707
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
906-949 9.18e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.64  E-value: 9.18e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622942836  906 SEWSDWSECEAS---GVQVRARQCILLFPVGSQCSGNTTESRPCVFD 949
Cdd:pfam00090    1 SPWSPWSPCSVTcgkGIQVRQRTCKSPFPGGEPCTGDDIETQACKMD 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 905-946 9.29e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.81  E-value: 9.29e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1622942836   905 WSEWSDWSECEAS---GVQVRARQCIL--LFPVGSQCSGNTTESRPC 946
Cdd:smart00209    1 WSEWSEWSPCSVTcggGVQTRTRSCCSppPQNGGGPCTGEDVETRAC 47
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
486-524 3.76e-05

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 42.15  E-value: 3.76e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1622942836   486 RCQFYRTHSTCIGAQDPYCGWDVVMKKCTSLEESLSMTQ 524
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRRQ 39
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 905-947 9.26e-04

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 42.63  E-value: 9.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622942836  905 WSEWSDWSEC-----EASGVQVRARQCIllFPVGSQCSGNTTESRPCV 947
Cdd:PTZ00087   233 YTEWGEWSNCsmecdHPDNVQIRERKCA--HPSGDCFKGDLKETRPCQ 278
TSP_1 pfam00090
Thrombospondin type 1 domain;
546-593 3.34e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.63  E-value: 3.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622942836  546 WSPWTPCTHTDGSAVGSclcRTRSCDSPAPqcGGWQCEGPSMEIANCS 593
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQV---RQRTCKSPFP--GGEPCTGDDIETQACK 45
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 660-710 6.25e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 39.93  E-value: 6.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942836  660 MFWTGWGPWERCTAQCG--GGIQARRRTCEN-GPDC-AGCNVEYQPCNT--NPCPEL 710
Cdd:PTZ00087   231 MFYTEWGEWSNCSMECDhpDNVQIRERKCAHpSGDCfKGDLKETRPCQVplPPCNSL 287
 
Name Accession Description Interval E-value
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
 50-485 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: 973.35  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 129
Cdd:cd11263      1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 209
Cdd:cd11263     81 TCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLTSSGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  210 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 289
Cdd:cd11263    161 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  290 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGTVDQGLYVNLT 369
Cdd:cd11263    241 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLYVNLT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  370 ERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTASSCLLEEIE 449
Cdd:cd11263    321 ERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRFSHVAVDVVQGKDMLFHIIYLATDYGTIKKVLAPLNQSSSSCLLEEIE 400

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1622942836  450 LFPERRREPIRSLQILHSQSVLLVGLWEHVVKIPLK 485
Cdd:cd11263    401 LFPKRQREPIRSLQILHSQSVLFVGLQEHVIKIPLK 436
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
 50-485 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: 778.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 129
Cdd:cd11241      1 FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSVEECQNYVRVLLVVGKNLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 209
Cdd:cd11241     81 TCGTYAFSPVCTIRKLSNLTQILDTISGVARCPYSPAHNSTALISASGELYAGTVYDFSGRDPAIYRSLGGKPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  210 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYY 288
Cdd:cd11241    161 NSKWLNEPNFVGSYEIGNHTYFFFRENAVEHqDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGEFPFYY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  289 NELQSTFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGT-VDQGLYVN 367
Cdd:cd11241    241 NEIQGTFYLPETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPTPNPHPNFQCTTsIDRGQPAN 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  368 LTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGRE-ALVHIIYLATDYGTIKKVRAPLnQTASSCLLE 446
Cdd:cd11241    321 TTERDLQDAQKYQLMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRGtQLVHIFYVGTDYGTILKMYQPH-RSQKSCTLE 399

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1622942836  447 EIELFPERRREPIRSLQILHSQSVLLVGLWEHVVKIPLK 485
Cdd:cd11241    400 EIKILPAMKGEPITSLQFLKSEKSLFVGLETGVLRIPLN 438
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
 50-485 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: 736.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 129
Cdd:cd11264      1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEEECQNYVRVLIVYGKKVF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQY 209
Cdd:cd11264     81 TCGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  210 NSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYN 289
Cdd:cd11264    161 NSKWLNEPNFIAAYDIGLFTYFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEIPFYYN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  290 ELQSTFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGTV-DQGLYVNL 368
Cdd:cd11264    241 ELQSTFYLPEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLsDDSPNENL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  369 TERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTASSCLLEEI 448
Cdd:cd11264    321 TERSLQDAQRLFLMNDVVQPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKALSTTNRSLRSCYLEEM 400

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1622942836  449 ELFPERRREPIRSLQILHSQSVLLVGLWEHVVKIPLK 485
Cdd:cd11264    401 QILPPGQREPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
 50-483 1.01e-158

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: 476.97  E-value: 1.01e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLF 129
Cdd:cd11265      1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSEEDCHNYVKVLLSYGKQLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLTAGGELYAATAMDFPGRDPAIYRSLGI--LPPLRTA 207
Cdd:cd11265     81 ACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSSSGQLFVGSPTDFSGSDSAIYRTLGTsnKSFLRTK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  208 QYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGR-FLLEDTWTTFMKARLNCSRPGEVP 285
Cdd:cd11265    161 QYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYmNCGKVIYSRIARVCKNDVGGGtMLLKDNWTTFLKARLNCSLPGEYP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  286 FYYNELQSTFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPN--FQCGTVDQG 363
Cdd:cd11265    241 FYFDEIQGMTYLPDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVNVNHRDhfNQCSSSSSS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  364 lyvnlterNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGR-EALVHIIYLATDYGTIKKVRApLNQTASS 442
Cdd:cd11265    321 --------HLLESSRYQLMDEAVQPITLEPLHHAKLERFSHIAVDVIPTKiHQSVHVLYVATTGGLIKKISV-LPRTQET 391

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1622942836  443 CLLEEIELFPERRRePIRSLQILHSQSVLLVGLWEHVVKIP 483
Cdd:cd11265    392 CLVEIWQPLPTPDS-PIKTMQYLKVTDSLYVGTELALMRIP 431
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
 70-484 5.90e-155

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: 467.27  E-value: 5.90e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   70 LVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLL-VGGDRLFTCGTNAFTPVCTNRSLSNL 148
Cdd:cd11235     15 LYVGARDRVYLVDLDSLYTEQKVAWPSSPDDVDTCYLKGKSKDDCRNFIKVLEkNSDDSLLVCGTNAFNPSCRNYNVETF 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  149 TEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNF 228
Cdd:cd11235     95 ELVGKEESGRGKCPYDPDHNSTALF-ADGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWLNEPQFVGAFDIGDY 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  229 TYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELD----LI 303
Cdd:cd11235    174 VYFFFREIAVEYiNCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFPFYFNELQDVFDLPSPSnkekIF 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  304 YGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNP----NFQCGTVDQglyvNLTERNLQDAQKF 379
Cdd:cd11235    254 YAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDERVpeprPGTCVDDSS----PLPDDTLNFIKSH 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  380 ILMHEVVQPVTTVPSFM--EDNSRFSHVVVDVVQGREA-LVHIIYLATDYGTIKKVRAPLNQTAS-SCLLEEIELFPErr 455
Cdd:cd11235    330 PLMDEAVTPILNRPLFIktDVNYRFTKIAVDRVQAKLGqTYDVLFVGTDRGIILKVVSLPEQGLQaSNILEEMPVGPP-- 407

                          410       420
                   ....*....|....*....|....*....
gi 1622942836  456 REPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11235    408 PEPIQTMQLSRKRRSLYVGSETGVLQVPL 436
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
 70-487 1.72e-129

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: 401.32  E-value: 1.72e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   70 LVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVL-LVGGDRLFTCGTNAFTPVCT--NRSLS 146
Cdd:cd11237     17 LLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLaKKSAGRLLVCGTNAYKPLCReyTVKDG 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  147 NLTEIHDQiSGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSlgilpPLRTAQYNSKWLNEPNFVSSYDIG 226
Cdd:cd11237     97 GYRVEREF-DGQGLCPYDPKHNSTAVY-ADGQLYSATVADFSGADPLIYRE-----PLRTERYDLKQLNAPNFVSSFAYG 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  227 NFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPE------ 299
Cdd:cd11237    170 DYVYFFFRETAVEYiNCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGEYPFYFNEIQSTSDIVEggyggk 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  300 -LDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPN-----PNPNfQCgtvdqglyVNlTERNL 373
Cdd:cd11237    250 sAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVPSnkvpePRPG-QC--------VN-DSRTL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  374 QD-AQKFI----LMHEVVQPVTTVPSFME--DNSRFSHVVVD--VVQGREALVHIIYLATDYGTIKKV----RAPLNQTA 440
Cdd:cd11237    320 PDvTVNFIkshpLMDEAVPSFFGRPILVRtsLQYRFTQIAVDpqVKALDGKYYDVLFIGTDDGKVLKAvniaSADTVDKV 399

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1622942836  441 SSCLLEEIELFPerRREPIRSLQILHS--QSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11237    400 SPVVIEETQVFP--RGVPIRNLLIVRGkdDGRLVVVSDDEIVSIPLHRC 446
Sema smart00630
semaphorin domain;
58-460 2.12e-128

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 396.35  E-value: 2.12e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836    58 FSQLTFDPGQKELVVGARNYLFRLQLEDLSLI-QAVEWECDEATKKACYSKGKSK-EECQNYIRVLL-VGGDRLFTCGTN 134
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAeLKTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLdYNEDRLLVCGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   135 AFTPVCTNRSLsnlteihdqisgmarcpyspqhnstalltagGELYAATAMDFPGRDPAIYRSLGILP-------PLRTA 207
Cdd:smart00630   81 AFQPVCRLRNL-------------------------------GELYVGTVADFSGSDPAIPRSLSVRRlkgtsgvSLRTV 129

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   208 QYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPF 286
Cdd:smart00630  130 LYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDnCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDPF 209

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   287 YYNELQSTFFLPEL----DLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPN-PNPNFQCGTVD 361
Cdd:smart00630  210 YFNELQAAFLLPPGsesdDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRgKVPYPRPGTCP 289

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   362 QGLY--VNLTERNLQDAQKFILMHEVVQPVTTVPSFME--DNSRFSHVVVDVVQGREAlVHIIYLATDYGTIKKVRAPLN 437
Cdd:smart00630  290 NKPPssKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKtdSNYLLTSIAVDRVATDGN-YTVLFLGTSDGRILKVVLSES 368

                           410       420
                    ....*....|....*....|....
gi 1622942836   438 QTAS-SCLLEEIELFPErrREPIR 460
Cdd:smart00630  369 SSSSeSVVLEEISVFPD--GSPIS 390
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
 70-484 8.65e-114

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: 360.68  E-value: 8.65e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   70 LVVGARNYLFRLQL-----EDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDR-LFTCGTNAFTPVCTNR 143
Cdd:cd11242     21 LYIAARDHVYTVDLdashtEEIVPSKKLTWRSRQADVENCRMKGKHKDECHNFIKVLVPRNDEtLFVCGTNAFNPVCRNY 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  144 SLSNLTEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSY 223
Cdd:cd11242    101 RIDTLEQDGEEISGMARCPFDAKQANVALF-ADGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYDSKWLKEPHFVHAV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  224 DIGNFTYFFFRENAVEHD-CGKTVFSRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPEL- 300
Cdd:cd11242    180 EYGDYVYFFFREIAVEYNtLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPGDSHFYFDVLQAVTDVIRIn 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  301 --DLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPN---PNPNFQCGTVDQGLYVNLTERNLQD 375
Cdd:cd11242    260 grPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPEdrvPKPRPGCCAGSGSAEKYKTSNDFPD 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  376 -AQKFI----LMHEVVQPVTTVPSFMEDNSRF--SHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTAS--SCLLE 446
Cdd:cd11242    340 dTLNFIkthpLMDEAVPSIINRPWFTRTMVRYrlTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARIGPSGSngSVFLE 419

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1622942836  447 EIELF-PER--------RRepIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11242    420 EIDVYnPAKcsydgeedRR--IIGLELDRASHALFVAFSGCVIRVPL 464
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
 50-484 4.05e-108

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: 345.16  E-value: 4.05e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLI--QAVEWECDEATKKACYSKGKSKE-ECQNYIRVLLVGGD 126
Cdd:cd11240      1 FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDISTElkDKIKWEASEDKKKECANKGKDNQtDCFNFIRILQFYNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  127 -RLFTCGTNAFTPVCTNRSLSNLTEIH-DQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPL 204
Cdd:cd11240     81 tHLYVCGTFAFSPRCTYINLSDFSLSSiKFEDGKGRCPFDPAQRYTAIM-VDGELYSATVNNFLGSEPVISRNHSEGNVL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  205 RTaQYNSKWLNEPNFVSSY----DIGNFT------YFFFRENAVEHDCG-KTVFSRAARVCKNDIGGRFLLEDTWTTFMK 273
Cdd:cd11240    160 KT-ENTLRWLNEPAFVGSAhireSIDSPDgdddkiYFFFTETAVEYDFYeKVTVSRVARVCKGDLGGQRTLQKKWTTFLK 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  274 ARLNCSRPGEvPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYP 349
Cdd:cd11240    239 AQLVCSQPDS-GLPFNVLRDVFVLSPDSwdatIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRYT 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  350 NPNPNFQ---CGT-----VDQGLYVNLTERNLQDAQKFILMHEVVQPVTTvPSFMEDNSRFSHVVVDVVQGREALVH-II 420
Cdd:cd11240    318 GPVPDPRpgaCITnsarsQGITSSLNLPDNVLTFVKDHPLMDEQVHPINR-PLLVKSGVNYTRIAVHRVQALDGQTYtVL 396

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942836  421 YLATDYGTIKKVrAPLNQTASscLLEEIELFPErrREPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11240    397 FLGTEDGFLHKA-VSLDGGMH--IIEEIQLFDQ--PQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
 54-487 1.71e-99

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: 322.77  E-value: 1.71e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   54 NAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSL-IQAVEWECDEATKKACYSKGKSKE-ECQNYIRVL-LVGGDRLFT 130
Cdd:cd11239      6 NSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQdPKKIYWPASPERIEECKMAGKDPNtECANFVRVLqPYNRTHLYA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  131 CGTNAFTPVCT----NRSLSNLT---EIHDQISGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPP 203
Cdd:cd11239     86 CGTGAFHPICAfinvGRRLEDPIfklDDSSLESGRGKCPFDPNQPFASVLI-DGELYSGTAIDFMGRDAAIFRSLGHRHY 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  204 LRTAQYNSKWLNEPNFVSSYDI-------GNFTYFFFRENAVEHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKAR 275
Cdd:cd11239    165 IRTEQYDSRWLNEPKFVGAYLIpdsdnpdDDKVYFFFREKAVEAEgSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLKAR 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  276 LNCSRPGE--VPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPY- 348
Cdd:cd11239    245 LVCSVPGPdgIDTYFDELEDVFLLPTRDpknpLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVEYq 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  349 ---PNPNPnfqcGTVDQGLYVNL---TERNLQDAQKFI----LMHEVVQPVTTVPSFMEDNS--RFSHVVVDVVQGREAL 416
Cdd:cd11239    325 gkvPYPRP----GTCPSKTYGPLyksTKDFPDDVISFArshpLMYNPVYPLHGRPLLIRTNVpyRLTQIAVDRVEAEDGQ 400

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942836  417 VHIIYLATDYGTIKKVRAPLNQTASS--CLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11239    401 YDVLFIGTDSGTVLKVVSLPKENWEMeeVILEELQVF--KHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
 58-472 2.42e-99

The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted semaphorin, signals through its receptor plexin B (PlexB) to regulate central and peripheral axon pathfinding. In the Drosophila embryo, Sema2A secreted by oenocytes interacts with PlexB to guide sensory axons. Sema2A is a member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200499 [Multi-domain]  Cd Length: 452  Bit Score: 321.68  E-value: 2.42e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   58 FSQLTFDPGQKELVVGARNYLFRLQLEDLS----LIQAVEWECDEATKKACYSKGKSKE-ECQNYIRVLLV--GGDRLFT 130
Cdd:cd11238      3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINdtgnNCARDELTLSPSDVSECVSKGKDEEyECRNHVRVIQPmgDGQTLYV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  131 CGTNAFTPvcTNRSL--SNLTEIHDQIS---GMARCPYSPQHNSTALLTAGGE------LYAATAMDFPGRDPAIYRslg 199
Cdd:cd11238     83 CSTNAMNP--KDRVLdaNLLHLPEYVPGpgnGIGKCPYDPDDNSTAVWVEWGNpgdlpaLYSGTRTEFTKANTVIYR--- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  200 ilPPL------------RTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGRFLLED 266
Cdd:cd11238    158 --PPLynntkgrhesfmRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETAVEYiNCGKVVYSRVARVCKKDTGGKNVLRQ 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  267 TWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELD--LIYGIFTTNVNSIAASAVCIFNLSAIAQAF-AGPFKYQENSRS 343
Cdd:cd11238    236 NWTTFLKARLNCSISGEFPFYFNEIQSVYKVPGRDdtLFYATFTTSENGFTGSAVCVFTLSDINAAFdTGKFKEQASSSS 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  344 AWLPYPNPN-PNFQCGTVDQGLYvNLTERNLQDAQKFILMHEVVQpvTTVPSFMEDNSRFSHVVVDVVQGREALVHIIYL 422
Cdd:cd11238    316 AWLPVLSSEvPEPRPGTCVNDSA-TLSDTVLHFARTHPLMDDAVS--HGPPLLYLRDVVFTHLVVDKLRIDDQEYVVFYA 392

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622942836  423 ATDYGTIKK-VRAPLNQTASSCLLEEIELFPErrrEPIRSLQILHSQSVLL 472
Cdd:cd11238    393 GSNDGKVYKiVHWKDAGESKSNLLDVFELTPG---EPIRAMELLPGEFLYV 440
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
 68-484 2.80e-98

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: 319.09  E-value: 2.80e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   68 KELVVGARNYLFRLQLE-----DLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDR-LFTCGTNAFTPVCT 141
Cdd:cd11267     19 RTLYIGDRDNLYRVELDptagtEMRYHKKLTWRSNKNDINVCRMKGKHEGECRNFIKVLLLRDYGtLFVCGTNAFNPVCA 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  142 NRSLSNLTEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVS 221
Cdd:cd11267     99 NYSIDTLEPVGDNISGMARCPYDPKHANVALF-ADGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEPYFVH 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  222 SYDIGNFTYFFFRENAVE-HDCGKTVFSRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPE 299
Cdd:cd11267    178 AVEWGSHVYFFFREIAMEfNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVSDILN 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  300 L---DLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPN---PNPNFQCGTVdQGLYVNLTERNL 373
Cdd:cd11267    258 LggrPVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEelvPRPRPGCCAA-PGMRYNSSSTLP 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  374 QDAQKFI----LMHEVVQPVTTVPSFMEDNSRF--SHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTAS-----S 442
Cdd:cd11267    337 DEVLNFVkthpLMDEAVPSLGHAPWIVRTMTRYqlTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLIIPNASSSeisnqS 416

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1622942836  443 CLLEEIELF-PERRREPIRSLQILHSQSV------LLVGLWEHVVKIPL 484
Cdd:cd11267    417 VFLEELETYnPERCGWDSPQAQKLLSLELdkgsggLLLAFPSCVVRVPV 465
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
 67-484 5.36e-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: 307.73  E-value: 5.36e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   67 QKELVVGARNYLFRLQL-----EDLSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLV-GGDRLFTCGTNAFTPVC 140
Cdd:cd11266     18 NRTLYIAARDHIYTVDIdtshtEEIYFSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKrNDDTLFVCGTNAFNPSC 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  141 TNRSLSNLTEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFV 220
Cdd:cd11266     98 RNYKMDTLEFFGDEFSGMARCPYDAKHANVALF-ADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFV 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  221 SSYDIGNFTYFFFRENAVE-HDCGKTVFSRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLP 298
Cdd:cd11266    177 QAVDYGDYIYFFFREIAVEyNSMGKVVFPRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQAVTDVI 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  299 EL---DLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPN-----PNPNFQCGTVDQGLYVNLTE 370
Cdd:cd11266    257 HIngrDVVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDervpkPRPGCCAGSSSLEKYATSNE 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  371 RNlQDAQKFI----LMHEVVQPVTTVPSFMEDNSRF--SHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTA---S 441
Cdd:cd11266    337 FP-DDTLNFIkthpLMDEAVPSIINRPWFLRTMVRYrlTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARTGNSGflnD 415

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622942836  442 SCLLEEIELF-PER------RREPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11266    416 SLFLEEMNVYnSEKcsydgvEDKRIMGMQLDKASSALYVAFSTCVIKVPL 465
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
 70-484 3.47e-93

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: 305.41  E-value: 3.47e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   70 LVVGARNYLFRLQLED-----LSLIQAVEWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRL-FTCGTNAFTPVCTNR 143
Cdd:cd11269     21 LYIAGRDQVYTVNLNEvpkteVTPSRKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEMvFVCGTNAFNPMCRYY 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  144 SLSNLTEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSY 223
Cdd:cd11269    101 RLSTLEYDGEEISGLARCPFDARQTNVALF-ADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLHAI 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  224 DIGNFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELD 301
Cdd:cd11269    180 EYGNYVYFFFREIAVEHnNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFFYFDVLQSITDIIEIN 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  302 ---LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPN---PNPNFQCgTVDQGL------YVNLT 369
Cdd:cd11269    260 gipTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEdkvPKPRPGC-CAKHGLaeayktSIDFP 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  370 ERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRF--SHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTA--SSCLL 445
Cdd:cd11269    339 DETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYrlTAIAVDHAAGPHQNYTVIFVGSEAGVVLKILAKTSPFSlnDSVLL 418

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1622942836  446 EEIELF---------PERRRepIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11269    419 EEIEAYnhakcsaenEEDRR--VISLQLDRDHHALFVAFSSCVVRIPL 464
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
 54-487 3.93e-84

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: 280.94  E-value: 3.93e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   54 NAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLS---LIqaVEWECDEATKKACYSKGK-SKEECQNYIRVLL-VGGDRL 128
Cdd:cd11254      6 NTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWPASPQRIEECILSGKgSNGECGNFIRLIQpWNRTHL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  129 FTCGTNAFTPVCT--NRSLSNLTEIHDQI-----SGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGIL 201
Cdd:cd11254     84 YVCGTGAYNPVCAyiNRGRRAEDYMFRLEpdkleSGKGKCPYDPKQDSVSALI-NGELYAGVYIDFMGTDAAIFRTMGKQ 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  202 PPLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKA 274
Cdd:cd11254    163 PAMRTDQYNSRWLNDPAFVHAHLIPDSSeknddklYFFFREKSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKA 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  275 RLNCSRPGE--VPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPY 348
Cdd:cd11254    243 RLVCSVPGAdgIETHFDELRDVFIQPTQDtknpVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPY 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  349 ----PNPNPnfqcGTVDQGLYV--NLTERNLQD-AQKFI----LMHEVVQPVTTVPSFMEDNS--RFSHVVVDVVQGREA 415
Cdd:cd11254    323 tgkiPYPRP----GTCPGGTFTpsMKSTKDYPDeVINFMrthpLMYNAVYPVHRRPLVVRTNVnyRFTTIAVDQVDAADG 398

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942836  416 LVHIIYLATDYGTIKKVRA-PLNQ-TASSCLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11254    399 RYEVLFLGTDRGTVQKVIVlPKDDlETEELTLEEVEVF--KVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
 38-487 1.41e-83

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: 280.35  E-value: 1.41e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   38 ISYKEIgpwlreFRAKNAVDFSQL-------TF--DPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKG 108
Cdd:cd11249      9 LSYKEM------LESNNLITFNGLansssyhTFllDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKWAG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  109 KS-KEECQNYIRVL-LVGGDRLFTCGTNAFTPVCT-----NRSLSNLTEIHDQI--SGMARCPYSPQHNSTALLTaGGEL 179
Cdd:cd11249     83 KDiLKECANFIKVLkAYNQTHLYACGTGAFHPVCTyievgHHPEDNIFRLEDSHfeNGRGKSPYDPKLLTASLLI-DGEL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  180 YAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDI-------GNFTYFFFRENAV--EHdCGKTVFSRA 250
Cdd:cd11249    162 YSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIpesdnpeDDKIYFFFRENAIdgEH-TGKATHARI 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  251 ARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--VPFYYNELQSTFFL----PELDLIYGIFTTNVNSIAASAVCIFNL 324
Cdd:cd11249    241 GQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPngIDTHFDELQDVFLMnskdPKNPIVYAVFTTSSNIFKGSAVCMYSM 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  325 SAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGTVDQGLYVNL-TERNLQD-----AQKFILMHEVVQPVTTVPSFM-- 396
Cdd:cd11249    321 TDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGGFdSTKDLPDdvitfARSHPAMYNPVFPINNRPIIIkt 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  397 EDNSRFSHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQT---ASSCLLEEIELFperrREP--IRSLQILHSQSVL 471
Cdd:cd11249    401 DVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETwhdLEEVLLEEMTVF----REPtaISAMELSTKQQQL 476

                          490
                   ....*....|....*.
gi 1622942836  472 LVGLWEHVVKIPLKRC 487
Cdd:cd11249    477 YIGSAIGVSQLPLHRC 492
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
 58-487 6.25e-82

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: 274.87  E-value: 6.25e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   58 FSQLTFDPGQKELVVGARNYLFRLQLEDLS-LIQAVEWECDEATKKACYSKGKS-KEECQNYIRVL-LVGGDRLFTCGTN 134
Cdd:cd11250     10 YDALLLDEERGRLFVGAKNYLASLSLDNISkQEKKIYWPAPVEWREECNWAGKDiNTDCMNYVKILhHYNRTHLYACGTG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  135 AFTPVCTNRSLSNLTEIH----DQIS---GMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPPLRTA 207
Cdd:cd11250     90 AFHPTCAFVEVGQRMEDHvfrlDPSRvedGKGKSPYDPRHTAASVL-VGDELYSGVATDLMGRDFTIFRSLGQRPSLRTE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  208 QYNSKWLNEPNFVSSYDI-------GNFTYFFFRENAVE-HDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCS 279
Cdd:cd11250    169 QHDSRWLNEPKFVKVFWIpesenpdDDKIYFFFRETAVEaAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCS 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  280 RPGE--VPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPY----P 349
Cdd:cd11250    249 VPGNegGDTHFDELRDVFLLQTRDkrnpLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYqgkvP 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  350 NPNPNFqCGTVDQGLYV---NLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNS--RFSHVVVDVVQGREALVHIIYLAT 424
Cdd:cd11250    329 YPRPGM-CPSKTFGSFEstkDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIpyTFTQIAVDRVAAADGHYDVMFIGT 407

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942836  425 DYGTIKKVRAPLNQT---ASSCLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11250    408 DVGSVLKVISVPKGSwpsNEELLLEELHVF--KDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
 68-484 2.32e-80

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: 270.44  E-value: 2.32e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   68 KELVVGARNYLFRLQL----EDLSLIQAVEWECDEAtkKACYSKGKSKEECQNYIRVLLVGGDR-LFTCGTNAFTPVCTN 142
Cdd:cd11270     19 HMVYIAARDHVFAINLsaslERIVPQQKLTWKTKDV--EKCTVRGKNSDECYNYIKVLVPRNDEtLFACGTNAFNPTCRN 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  143 RSLSNLTEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPP-LRTAQYNSKWLNEPNFVS 221
Cdd:cd11270     97 YKMSSLEQDGEEVIGQARCPFESRQSNVGLF-AGGDFYSATMTDFLASDAVIYRSLGESSPvLRTVKYDSKWLREPHFLH 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  222 SYDIGNFTYFFFRENAVEHDC-GKTVFSRAARVCKNDIGGR-FLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPE 299
Cdd:cd11270    176 AIEYGNYVYFFLSEIAVEYTTlGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPGDSFFYFDVLQSLTNVMQ 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  300 LD---LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLP-----YPNPNPNFQCGTVDQGLYVNLTE- 370
Cdd:cd11270    256 INhrpAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPvpdeaVPKPRPGSCAGDGPAAGYKSSTNf 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  371 --RNLQDAQKFILMHEVVQPVTTVPSFMEDNSRF--SHVVVDVVQGREALVHIIYLATDYGTIKKVRAPL--NQTASSCL 444
Cdd:cd11270    336 pdETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFklTQIAVDTAAGPYKNYTVVFLGSENGHVLKVLASMhpNSSYSTQV 415

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1622942836  445 LEEIELF--------PERRRepIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11270    416 LEDIDVYnpnkcnvrGEDRR--ILGLELDKDHHALFVAFTGCVIRVPL 461
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
 50-484 1.70e-79

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: 267.55  E-value: 1.70e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQA---VEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VG 124
Cdd:cd11256      2 FRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTPGPIRLkhqIPWPANDSKISECAFKKKSNEtECFNFIRVLVpVN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  125 GDRLFTCGTNAFTPVCTNRSLSNLT---EIHDQI--SGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLG 199
Cdd:cd11256     82 GTHLYTCGTYAFSPACTYIELDHFSlppPNGTIItmDGKGQSPFDPQHNYTAILV-DGELYTGTMNNFRGNEPIIFRNLG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  200 ILPPLRTAQYNsKWLN-EPNFVSSYDI--GNFTYFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKAR 275
Cdd:cd11256    161 TKVSLKTDGFL-RWLNaDAVFVASFNPqgDSKVYFFFEETAREFDFfEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  276 LNCSRPGEVPFyyNELQSTFFLPELD----LIYGIFTT--NVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYP 349
Cdd:cd11256    240 LTCSQQGHFPF--NVIHHVALLNQPDpnnsVFYAVFTSqwQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYM 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  350 NPNPNFQCGTVDQGLYvnlTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREALVH-IIYLATDYGT 428
Cdd:cd11256    318 GPVSDPRPGSCSGGKS---SDKALNFMKDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSGHNYtVMFLGTDKGF 394

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942836  429 IKKVRAPlnQTASSCLLEEIELFPErrREPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11256    395 LHKAVLM--GGSESHIIEEIELLTP--PEPVENLLLAANEGVVYIGYSAGVWRVPL 446
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
 52-463 2.22e-78

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: 265.03  E-value: 2.22e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   52 AKNAVDFSQ-LTFDpgqKELVVGARNYLFRLQL------EDLSLIQAVEWECDEAtkKACYSKGKSKEECQNYIRVLLV- 123
Cdd:cd11268      5 AELGLDFQRfLTLN---RTLLVAARDHVFSFDLqaeeegEGLVPNKYLTWRSQDV--ENCAVRGKLTDECYNYIRVLVPw 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  124 GGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILPP 203
Cdd:cd11268     80 DSQTLLACGTNSFSPVCRSYGITSLQQEGEELSGQARCPFDATQSNVAIF-AEGSLYSATAADFQASDAVVYRSLGPQPP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  204 LRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGGR-FLLEDTWTTFMKARLNCSRP 281
Cdd:cd11268    159 LRSAKYDSKWLREPHFVQALEHGDHVYFFFREVSVEDaRLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVP 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  282 GEVPFYYNELQS---TFFLPELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLP-----YPNPNP 353
Cdd:cd11268    239 GDSTFYFDVLQAltgPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPvsedrVPSPRP 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  354 NFQCGTVDQGLYVnlTERNL-QDAQKFILMHEV----VQPVTTVPSF-MEDNSRFSHVVVDVVQGREALVHIIYLATDYG 427
Cdd:cd11268    319 GSCAGVGGAALFS--SSRDLpDDVLTFIKAHPLldpaVPPVTHQPLLtLTSRALLTQVAVDGMAGPHSNITVMFLGSNDG 396

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1622942836  428 TIKKVRAPLNQTA--SSCLLEEIELFPERRREPIRSLQ 463
Cdd:cd11268    397 TVLKVLPPGGRSGgpEPILLEEIDAYSPARCSGKRTAQ 434
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
 56-487 1.51e-76

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


Pssm-ID: 200514 [Multi-domain]  Cd Length: 471  Bit Score: 260.17  E-value: 1.51e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   56 VDFSQLTFDPGQKELVVGARNYLFRLQLEDLSL-IQAVEWECDEATKKACYSKGKSKEECQNYIRVLL-VGGDRLFTCGT 133
Cdd:cd11253      8 LDLHTMLLDEYQERLFVGGRDLLYSLSLERISAnYKEIHWPSTQLQVEDCIMKGRDKPECANYIRVLHhYNRTHLLACGT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  134 NAFTPVCTNRSLSNLTEIH------DQI-SGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLRT 206
Cdd:cd11253     88 GAFDPVCAFIRVGRGSEDHlfqlesDKFeRGRGRCPFDPNSSFISTLI-GGELFVGLYSDYWGRDAAIFRTMNHLAHIRT 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  207 AQYNSKWLNEPNFVSSYDI-------GNFTYFFFRENAVEHDCG-KTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNC 278
Cdd:cd11253    167 EHDDERLLKEPKFVGSYMIpdnedpdDNKVYFFFTEKALEAEGGnHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLIC 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  279 SRPGE--VPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPY---- 348
Cdd:cd11253    247 SVPGPngIDTHFDELEDVFLLRTRDnknpEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVYegkv 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  349 PNPNPNFQCGTVDQGLYVNLTE---RNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFS--HVVVDVVQGREALVHIIYLA 423
Cdd:cd11253    327 PYPRPGSCASKVNGGHYGTTKDypdEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNlkQIAVDRVEAEDGQYDVLFIG 406

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942836  424 TDYGTIKKVRAPLNQTASS---CLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11253    407 TDNGIVLKVITIYNQETETmeeVILEELQVF--KVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
 57-487 3.40e-76

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: 259.07  E-value: 3.40e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   57 DFSQLTFDPGQKELVVGARNYLFRLQLEDLSL-IQAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VGGDRLFTCGT 133
Cdd:cd11252      9 DFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKnPKKIYWPAAKERVELCKLAGKDANtECANFIRVLHpYNRTHVYVCGT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  134 NAFTPVCTNRSLSNLTE-------IHDQISGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPP--- 203
Cdd:cd11252     89 GAFHPTCGYIELGTHKEdriflldTQNLESGRLKCPFDPQQPFASVMT-DEYLYAGTASDFLGKDTTFTRSLGPTPDhhy 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  204 LRTAQYNSKWLNEPNFVSSYDIGNF-------TYFFFRENAVEHDCG-KTVFSRAARVCKNDIGGRFLLEDTWTTFMKAR 275
Cdd:cd11252    168 IRTDISEHYWLNGAKFIGTFPIPDTynpdddkIYFFFREASQDGSTSdKSVLSRVGRVCKNDVGGQRSLINKWTTFLKAR 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  276 LNCSRPGE--VPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAW---- 345
Cdd:cd11252    248 LVCSIPGPdgADTHFDELQDIFLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWvqye 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  346 --LPYPNPnpnfqcGTVDQGLY---VNLTERNLQDAQKFI----LMHEVVQPVTTVPSFMEDNS--RFSHVVVDVVQGRE 414
Cdd:cd11252    328 grIPYPRP------GTCPSKTYdplIKSTKDFPDEVISFIkrhpLMYKSVYPLTGGPVFTRINVdyRLTQIVVDHVAAED 401

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622942836  415 ALVHIIYLATDYGTIKKVR--APLNQTASSCLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11252    402 GQYDVMFLGTDIGTVLKVVsiTKEKWTMEEVVLEELQIF--KHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
 47-484 6.92e-75

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: 255.11  E-value: 6.92e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   47 LREFRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VG 124
Cdd:cd11258      1 VRRFSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQtECFNYIRFLQpYN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  125 GDRLFTCGTNAFTPVCTNRSLSNLTEIHDQIS-GMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPP 203
Cdd:cd11258     81 QSHLYTCGTYAFQPKCAYINMLTFTLDRAEFEdGKGKCPYDPAKGHTGLIV-DGELYSATLNNFLGTEPVILRNLGQHYS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  204 LRTaQYNSKWLNEPNFVSSY----DIGNFT------YFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFM 272
Cdd:cd11258    160 MKT-EYLAFWLNEPHFVGSAfvpeSVGSFTgdddkiYFFFSERAVEYDCdSEQVVARVARVCKGDLGGARTLQKKWTTFL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  273 KARLNCSRPgEVPFYYNELQSTFFLPELDL----IYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPY 348
Cdd:cd11258    239 KARLLCSIP-EWQLYFNQLKAVFTLEGASWrnttFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRY 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  349 PNPNPNFQCGTV------DQGLY--VNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQG-REALVHI 419
Cdd:cd11258    318 TDPVPSPRPGSCinnwhrDHGYTssLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSNFTHVVWTRVLGlDGETYSV 397

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622942836  420 IYLATDYGTIKKVrapLNQTASSCLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11258    398 LFIGTLDGWLIKA---VSLGSWVHMIEELQVF--DQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
 50-484 1.18e-74

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: 254.45  E-value: 1.18e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQA-VEWECDEATKKACYSKGKSKE-ECQNYIRVL-LVGGD 126
Cdd:cd11260      1 FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAkVLWEVTEEKQKDCTNKGKHADiDCHNYIRILhKMNDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  127 RLFTCGTNAFTPVCTNRSLSN--LTEIHDQISGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGIlpPL 204
Cdd:cd11260     81 RMYVCGTNAFSPTCDYISYDDgqLTLEGKQEDGKGKCPFDPFQRYSSVMV-DQDLYSATSMNFLGSEPVIMRSSPI--TI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  205 RTaQYNSKWLNEPNFVSSYDI----------GNFTYFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMK 273
Cdd:cd11260    158 RT-EFKSSWLNEPNFIYMAAVpesedspegdDDKIYLFFSETAVEYDFyNKLVVSRVARVCKGDLGGQRTLQKKWTSFLK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  274 ARLNCSRP-GEVPFYyneLQSTFFLPELD----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFA-GPFKYQ---ENSRSA 344
Cdd:cd11260    237 ARLDCSVPePSLPYV---IQDVFHVCHQDwrkcVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrGKFKTPvavETSFVK 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  345 WLPY----PNPNP----NFQCGTVDQGLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREAL 416
Cdd:cd11260    314 WVMYsgelPVPRPgaciNNAARTSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGALFTRIVVDMVTAADGQ 393

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  417 VH-IIYLATDYGTIKKVrapLNQTASSCLLEEIELF-PErrrEPIRSLQIlhSQSVLLVGLWEHVVKIPL 484
Cdd:cd11260    394 SYpVMFIGTANGYVLKA---VNYDGEMHIIEEVQLFePE---EPIDILRL--SQNQLYAGSASGVVQMPV 455
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
 50-484 3.00e-74

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: 253.63  E-value: 3.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   50 FRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLS---LIQAVEWECDEATKKACYSKGKS-KEECQNYIRVLL-VG 124
Cdd:cd11257      2 FEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISptgEQQELTWSADEEKKQECSFKGKDpQRDCQNYIKILLrLN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  125 GDRLFTCGTNAFTPVCTNRSLSNLTEIHDQI------SGMARCPYSPQHNSTALlTAGGELYAATAMDFPGRDPAIYRSL 198
Cdd:cd11257     82 STHLFTCGTYAFSPICTYIVMTNFSLERDEKgeplleDGKGRCPFDPEYKSTAI-MVDGELYTGTVSNFQGNDPIIYRSL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  199 GILPPLRTAqyNS-KWLNEPNFVSSYDI----------GNFTYFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLED 266
Cdd:cd11257    161 GSGTPLKTE--NSlNWLQDPAFVGSAYIqeslpklvgdDDKIYFFFSETGKEFDFfENTIVSRIARVCKGDEGGERVLQK 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  267 TWTTFMKARLNCSRPGEvPFYYNELQSTFFLPELD------LIYGIFTTNVNSIAA--SAVCIFNLSAIAQAFAGPFKYQ 338
Cdd:cd11257    239 RWTTFLKAQLLCSLPDD-GFPFNVLQDVFVLTPSPedwkdtLFYGVFTSQWHKGTAgsSAVCVFTMDQVQRAFNGLYKEV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  339 ENSRSAWLPYPNPNPNFQCGT----------VDQGLyvNLTERNLQDAQKFILMHevvQPVTTVPSFMEDNSRFSHVVVD 408
Cdd:cd11257    318 NRETQQWYTYTHPVPEPRPGAcitnsarerkINSSL--HMPDRVLNFVKDHFLMD---GQVRSQPLLLQPQVRYTQIAVH 392

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942836  409 VVQGREALVHIIYLATDYGTIKKVrapLNQTASSCLLEEIELFPErrREPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11257    393 RVKGLHKTYDVLFLGTDDGRLHKA---VSVGPMVHIIEELQIFSE--GQPVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
 52-487 3.51e-72

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: 247.88  E-value: 3.51e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   52 AKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSL-IQAVEWECDEATKKACYSKGKSKEE-CQNYIRVLL-VGGDRL 128
Cdd:cd11251      4 SERPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQdALSIFWPASASKVEECKMAGKDPTHgCGNFVRVIQpYNRTHL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  129 FTCGTNAFTPVCT-----NRSLSNLTEIHDQI-SGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILP 202
Cdd:cd11251     84 YVCGSGAFSPVCVyvnrgRRSEEQVFHIDSKAeSGKGRCSFNPNVNTVSVMI-NEELFSGMYIDFMGTDAAIFRSLTKRN 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  203 PLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRENAVEHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKA 274
Cdd:cd11251    163 AVRTDQHNSKWLSEPIFVDAHLIPDGTdpndaklYFFLKERLTDNSgSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKA 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  275 RLNCSRPGE--VPFYYNELQSTFFL----PELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPY 348
Cdd:cd11251    243 RLVCSVMDEdgTETHFDELEDVFLLetdnPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAY 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  349 ----PNPNPnfqcGTVDQGLY---VNLTERNLQDAQKFI----LMHEVVQPVTTVPSFMEDNS--RFSHVVVDVVQGREA 415
Cdd:cd11251    323 qgriPYPRP----GTCPGGAFtpnMQSTKEFPDDVVTFIrnhpLMFNPIYPIGRRPLLVRTGTdyKYTKIAVDRVNAADG 398

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942836  416 LVHIIYLATDYGTIKKVRA-PLNQTASSCL-LEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11251    399 RYHVLFLGTDKGTVQKVVVlPTNGSLSGELiLEELEVF--KNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
 48-484 5.65e-72

The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex. Sema4G and Sema4C proteins specifically bind to Plexin B2 expressed in the cerebellar granule cells. Sema4G and Sema4C are involved in neural tube closure and cerebellar granule cell development through Plexin B2.Sema4G belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200523 [Multi-domain]  Cd Length: 457  Bit Score: 246.98  E-value: 5.65e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   48 REFRAkNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLS--LIQAVEWECDEATKKACYSKGK-SKEECQNYIRVLL-V 123
Cdd:cd11262      1 RRFRG-PAQNYSTLLLEDESGRLYVGARGAIFSLNASDISdsSALTIDWEASPEQKHQCLKKGKnNQTECFNHVRFLQrF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  124 GGDRLFTCGTNAFTPVCT-----NRSLSNLTEihdqiSGMARCPYSPQHNSTALLTaGGELYAATAMDFpgRD-PAIYRS 197
Cdd:cd11262     80 NSTHLYTCGTHAFRPLCAyidaeRFTLSSQFE-----EGKEKCPYDPAKGYTGLIV-DGQLYTASQYEF--RSfPDIRRN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  198 LGiLPPLRTAQYNSKWLNEPNFVSSY----DIGNFT------YFFFRENAVEHDC--GKTVFSRAARVCKNDIGGRFLLE 265
Cdd:cd11262    152 SP-QPTLRTEEAPTRWLNDADFVGSVlvreSMNSSVgdddkiYFFFTERSQEETAyfSQSRVARVARVCKGDRGGKKTLQ 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  266 DTWTTFMKARLNCSRPgEVPFYYNELQSTFFL----PELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENS 341
Cdd:cd11262    231 RKWTSFLKARLVCYIP-EYEFLFNVLRSVFVLwgstPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDS 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  342 RSAWLPY----PNPNPNfQCGTVD---QGLYvnlTERNLQD-----AQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDV 409
Cdd:cd11262    310 SSKWSRYtgkvPEPRPG-SCITDEhrsQGIN---SSQDLPDnvldfVRRHPLMAEQVLPVEGRPLLFKRNVIYTKIAVQT 385

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942836  410 VQGREALV-HIIYLATDYGTIKKvraPLNQTASSCLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11262    386 VRGLDGRVyDVLFLGTDEGWLHK---AVVIGSAVHIIEELQVF--REPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
 47-484 1.80e-71

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: 245.92  E-value: 1.80e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   47 LREFRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLSLIQ-AVEWECDEATKKACYSKGKSKE-ECQNYIRVLLVG 124
Cdd:cd11259      9 LVHFHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNALNISEKQhELYWKVSEDKRTKCAVKGKSKQtECRNYIRVLQPL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  125 GDR-LFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGiLPP 203
Cdd:cd11259     89 NDTfLYVCGTNAFQPTCDYLNLTSFRLLGKNEDGKGRCPFDPAQSYTSVMV-DGELYSGTSYNFLGSEPIISRNSS-QSP 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  204 LRTaQYNSKWLNEPNFVSSYDI----------GNFTYFFFRENAVEHD-CGKTVFSRAARVCKNDIGGRFLLEDTWTTFM 272
Cdd:cd11259    167 LRT-EYAIPWLNEPSFVFADVIradpdspdgeDDKIYFFFTEVSVEYEfVGKLLIPRIARVCKGDQGGLRTLQKKWTSFL 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  273 KARLNCSRPgEVPFYYNELQSTFFLPELDL----IYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPfKYQ-----ENSRS 343
Cdd:cd11259    246 KARLICSIP-DKNLVFNVVNDVFILKSPTLkepvIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSKG-KYMqsatvEQSHT 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  344 AWLPY----PNPNP----NFQCGTVDQGLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREA 415
Cdd:cd11259    324 KWVRYngevPKPRPgaciNNEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNYTQIVVDRVQALDG 403

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622942836  416 LVH-IIYLATDYGTIKKVrapLNQTASSCLLEEIELFPErrREPIRSLQILHSQS--VLLVGLWEHVVKIPL 484
Cdd:cd11259    404 TIYdVMFISTDRGALHKA---ISLENEVHIIEETQLFPD--FEPVQTLLLSSKKGrrFLYAGSNSGVVQSPL 470
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
 56-487 2.08e-66

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: 231.72  E-value: 2.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   56 VDFSQLTFDPGQKELVVGARNYLFRLQLEDLSL-IQAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VGGDRLFTCG 132
Cdd:cd11255      8 LHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPdAKEIHWPPLPGQREECIRKGKDPEtECANFVRVLQpFNRTHLLACG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  133 TNAFTPVCTNRSLSNLTEiH----DQI---SGMARCPYSPQHNSTALLTaGGELYAATAMDFPGRDPAIYRSLGILPPLR 205
Cdd:cd11255     88 TGAFQPVCALINVGHRGE-HvfslDPTtveSGRGRCPHEPKRPFASTFT-GGELYTGLTADFLGRDSVIFRGFGTRSPLR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  206 TaQYNSKWLNEPNFVSSYDI-------GNFTYFFFRENAVEHDCGK--TVFSRAARVCKNDIGGRFLLEDTWTTFMKARL 276
Cdd:cd11255    166 T-ETDQRLLHEPRFVAAHLIpdnadrdNDKVYFFFTERATETAEDDdgAIHSRVGRLCANDAGGQRVLVNKWSTFIKARL 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  277 NCSRPGE--VPFYYNELQSTFFL-------PEldlIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLP 347
Cdd:cd11255    245 VCSVPGPhgIQTHFDQLEDVFLLrtkdgksPE---IYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGP 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  348 Y----PNPNPNFqC--GTVDQ-----GLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNS--RFSHVVVDVVQGRE 414
Cdd:cd11255    322 YegkvPYPRPGV-CpsKITAQpgrafRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLpyRLTQIVVDRVEAED 400

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942836  415 ALVHIIYLATDYGTIKKV---RAPLNQTASSCLLEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPLKRC 487
Cdd:cd11255    401 GYYDVMFIGTDSGSVLKVivlQKGNSAAGEEVTLEELQVF--KVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
 45-483 2.73e-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: 2.73e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   45 PWLREFRAKNAVDFSQLTFDPGQKELVVGARNYLFRLQLEDLS-LIQAVEWECDEATKKACYSKGKSKEECQNYIRVL-L 122
Cdd:cd11261      1 SALTRFSAPHTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGeRPRRIDWMVPEAHRQNCRKKGKKEAECHNFIRILaI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  123 VGGDRLFTCGTNAFTPVCTNRSLSNLTEIHDQISGMARCPYSPQHNSTALLtAGGELYAATAMDFPGRDPAIYRSLGILP 202
Cdd:cd11261     81 ANASHLLTCGTFAFDPKCGVIDVSSFQQVERLESGRGKCPFEPAQRSAAIM-AGGVLYAATVKNFLGTEPIISRAVGRAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  203 PLRTAQYNSKWLNEPNFVSSY----------DIGNFTYFFFRENAVEHDCGKTV-FSRAARVCKNDIGGRFLLEDTWTTF 271
Cdd:cd11261    160 EWIRTETLPSWLNAPAFVAAVflspaewgdeDGDDEIYFFFTETAREYDSYERIkVPRVARVCAGDLGGRKTLQQRWTTF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  272 MKARLNCSRP--GEVpfyYNELQSTFFLPELD-----LIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSA 344
Cdd:cd11261    240 LKADLLCPGPehGRA---SSILQDVTTLRPLPgagtpIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  345 WLPY-----PNPNPNfQCGTVDQ-----GLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVV---VDVVQ 411
Cdd:cd11261    317 GLPVmdsdvPQPRPG-ECITNNMkllgfGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYLRVAahrVTSLS 395

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942836  412 GREalVHIIYLATDYGTIKK-VRAplnqTASSCLLEEIELFPErrREPIRSLQILHSQsvLLVGLWEHVVKIP 483
Cdd:cd11261    396 GKE--YDVLYLGTEDGHLHRaVRI----GAQLSVLEDLALFPE--PQPVENLQLHHNW--LLVGSDTEVTQIN 458
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
 57-374 1.02e-57

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: 204.36  E-value: 1.02e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   57 DFSQLTFDPGQKELVVGARNYLFRLQL----EDLSLIQ-AVEWECDEATKKACYSKGKSKEECQNYIRVLLVGG--DRLF 129
Cdd:cd09295      1 DDDKILVSFRKDTIYVGAIARIYKVDGggtrLLLSCISpELNFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGdlDILA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTNAFTPVCTNRSLsNLTEIHDQI---SGMARCPYSPQHNSTALLTAGgELYAATAMDF-PGRDPAIYRSLGILPPLR 205
Cdd:cd09295     81 VCGSNAAQPSCGSYRL-DVLVELGKVrwpSGRPRCPIDNKHSNMGVNVDS-KLYSATDHDFkDGDRPALSRRSSNVHYLR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  206 TAQYNSKWLNEPNFVSSYDIG---NFTYFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRP 281
Cdd:cd09295    159 IVVDSSTGLDEITFVYAFVSGdddDEVYFFFRQEPVEYLKkGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSRP 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  282 GEvPFYYNELQSTFFL---PELDLIYGIFTTNVNSIAASAVCIFNLSAIAQAFAGPFKYQENsrSAWLPYPNPNPNFQCG 358
Cdd:cd09295    239 QS-GFAFNLLQDATGDtknLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVFDDPVEAINN--RPLYAHQNQRSRLTSI 315

                          330
                   ....*....|....*...
gi 1622942836  359 TVD--QGLYVNLTERNLQ 374
Cdd:cd09295    316 AVDatKQKSVGYQVVFLG 333
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
 64-484 9.27e-51

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: 185.05  E-value: 9.27e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   64 DPGQKELVVGARNYLFRLQLEDLSLIQavEWECDEATKKACYSKGkSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTNr 143
Cdd:cd11243     10 EAGSSSVYVGGQGALYLLDFTGSAVIV--KKIPDEKTEKDCKKRA-TLDDCENYITLIKKLDYRLLVCGTNAGSPKCWF- 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  144 sLSNLTEIHDQiSGMARCPYSPQHNStALLTAGGELYAATAmdfpGRDPAI--YRSLGILPPLRTAqynSKWLNEPNFVS 221
Cdd:cd11243     86 -LVNQTLVTLS-ADRGVAPFLPDENS-LVLIEGNNVYSTIS----GKKGNIprFRRYGGKKELYTS---DTVMQKPQFVK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  222 S--------YDigNFTYFFFREN--AVEHDCGKTVfSRAARVCKNDIGGRFLLE-DTWTTFMKARLNCSRPGEvPFYYNE 290
Cdd:cd11243    156 AtllpedeqYQ--DKIYYFFREDneDKGPEAEPNI-SRVARLCKEDQGGTSSLStSKWSTFLKARLVCGDPAT-PMNFNR 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  291 LQSTFFLP----ELDLIYGIFTTNVNSiaaSAVCIFNLSAIAQAFagpfkyqenSRSAWLPYPNPNPNFQCGTVDQGLYV 366
Cdd:cd11243    232 LQDVFLLPkeewREAVVYGVFSNTWGS---SAVCSYSLGDIDKVF---------RTSSLKGYSGSLPNPRPGTCVPPEQT 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  367 NLTErNLQDAQKFILMHEVVQPVTTVPSFM-EDNSRFSHVVVDVVQGREAL-VHIIYLATDYGTIKKVRAPLNQTASscl 444
Cdd:cd11243    300 HPSE-TFSFADEHPELDDRIEPDEPRKLPVfQNKDHYQKVVVDEVRASDGVsYDVLYLATDKGKIHKVVESKGQTHN--- 375

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1622942836  445 LEEIELFpeRRREPIRSLQILHSQSVLLVGLWEHVVKIPL 484
Cdd:cd11243    376 IMEIQPF--KEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
 291-466 2.57e-50

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: 175.54  E-value: 2.57e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  291 LQSTFFLPEL------DLIYGIFTTN-VNSIAASAVCIFNLSAIAQAFAGPFKYQENSRSAWLPYPNPNPNFQCGT-VDQ 362
Cdd:pfam01403    1 LQDVFVLKPGagdaldTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTcIND 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  363 GLYVNLTERNLQDAQKFILMHEVVQPVTTVPSFMEDNSRFSHVVVDVVQGREALVHIIYLATDYGTIKKVRAPLNQTasS 442
Cdd:pfam01403   81 PLRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLVGSEE--S 158

                          170       180
                   ....*....|....*....|....
gi 1622942836  443 CLLEEIELFPErrREPIRSLQILH 466
Cdd:pfam01403  159 HIIEEIQVFPE--PQPVLNLLLSS 180
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 850-902 2.23e-17

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 76.86  E-value: 2.23e-17
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   850 WSCWSPWTKCSATCGGGHYMRTRSCSNPAPAYGGDICLGLHTEEALCNTQPCP 902
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 793-845 1.64e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 1.64e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   793 WSAWTSWSQCSRDCSRGIRNRKRVCNNPEPKYGGMPCLGPSLEYQECNILPCP 845
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 598-657 1.25e-13

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 66.07  E-value: 1.25e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   598 WTPWTSWSPCSTTCGIGFQVRQRSCSNPTPRHGGRVCVGQNREERKihpalyCNEHlLCP 657
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRA------CNEQ-PCP 53
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
 61-331 1.22e-12

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


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 71.21  E-value: 1.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   61 LTFDPGQKELVVGARNYLFRLQlEDLSLIQAVE-------WECdeaTKKACYSKGKSKEECQNYIRVLLV--GGDRLFTC 131
Cdd:cd11236      5 LAVDNSTGRVYVGAVNRLYQLD-SSLLLEAEVStgpvldsPLC---LPPGCCSCDHPRSPTDNYNKILLIdySSGRLITC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  132 GTnAFTPVCTNRSLSNLTEIHdQISGMARCPYSPQHNSTALLTAGGE-----LYAATAMD---FPGRDPAI-YRSLGILP 202
Cdd:cd11236     81 GS-LYQGVCQLRNLSNISVVV-ERSSTPVAANDPNASTVGFVGPGPYnnenvLYVGATYTnngYRDYRPAVsSRSLPPDD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  203 PLRTAQYN--SKWLNEPNFVSSYDI--------GNFTYFFFRENAVeHDCGKTVFSRAARVCKNDIGgrflledtWTTFM 272
Cdd:cd11236    159 DFNAGSLTggSAISIDDEYRDRYSIkyvygfssGGFSYFVTVQRKS-VDDESPYISRLVRVCQSDSN--------YYSYT 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942836  273 KARLNC-SRPGEVpfyYNELQSTF-------------FLPELDLIYGIFTTNVNSIAA----SAVCIFNLSAIAQAF 331
Cdd:cd11236    230 EVPLQCtGGDGTN---YNLLQAAYvgkagsdlarslgISTDDDVLFGVFSKSKGPSAEpsskSALCVFSMKDIEAAF 303
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 662-708 2.02e-12

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.60  E-value: 2.02e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836   662 WTGWGPWERCTAQCGGGIQARRRTCENGP------DCAGCNVEYQPCNTNPCP 708
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
851-901 2.44e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 2.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622942836  851 SCWSPWTKCSATCGGGHYMRTRSCSNPAPayGGDICLGLHTEEALCNTQPC 901
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
794-844 5.90e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.81  E-value: 5.90e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622942836  794 SAWTSWSQCSRDCSRGIRNRKRVCNNPEPkyGGMPCLGPSLEYQECNILPC 844
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
599-643 2.37e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 2.37e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622942836  599 TPWTSWSPCSTTCGIGFQVRQRSCSNPTPrhGGRVCVGQNREERK 643
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQA 43
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 599-634 3.63e-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: 50.74  E-value: 3.63e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1622942836  599 TPWTSWSPCSTTCGIGFQVRQRSCSNPtPRHGGRVC 634
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC 38
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 486-533 6.08e-08

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 50.01  E-value: 6.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622942836  486 RCQFYRTHSTCIGAQDPYCGWDVVMKKCTS----LEESLSMTQWEQSISACP 533
Cdd:pfam01437    1 RCSQYTSCSSCLAARDPYCGWCSSEGRCVRrsacGAPEGNCEEWEQASSKCP 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 546-595 7.05e-08

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.89  E-value: 7.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1622942836   546 WSPWTPCTHTDGSAVgscLCRTRSCDSPAPQCGGWQCEGPSMEIANCSRN 595
Cdd:smart00209    4 WSEWSPCSVTCGGGV---QTRTRSCCSPPPQNGGGPCTGEDVETRACNEQ 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
665-707 1.93e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 48.57  E-value: 1.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622942836  665 WGPWERCTAQCGGGIQARRRTC----ENGPDCAGCNVEYQPCNTNPC 707
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
 58-514 2.39e-07

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


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 54.55  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   58 FSQLTFDPGQKELVVGARNYLFRLQlEDLSLIQAVEwECDEATKKACYSK------GKSKEECQNYIRVLLV--GGDRLF 129
Cdd:cd11272     13 FNHLTVHQSTGAVYVGAINRVYKLS-GNLTILVAHK-TGPEEDNKSCYPPlivqpcSEVLTLTNNVNKLLIIdySENRLL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  130 TCGTnAFTPVCTNRSLSNLTEIHDqiSGMARCPYSPQHNSTALL------TAG--GELYAATAMD-----FPG------- 189
Cdd:cd11272     91 ACGS-LYQGVCKLLRLDDLFILVE--PSHKKEHYLSSVNKTGTMygvivrSEGedGKLFIGTAVDgkqdyFPTlssrklp 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  190 RDPaiyRSLGILPPLRTAQYNSKWLNEPN----FVSSYDI--------GNFTYFFF-----RENAVEHDCGKTVF-SRAA 251
Cdd:cd11272    168 RDP---ESSAMLDYELHSDFVSSLIKIPSdtlaLVSHFDIfyiygfasGNFVYFLTvqpetPEGVSINSAGDLFYtSRIV 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  252 RVCKNDiggrflleDTWTTFMKARLNCSRPGEvpfYYNELQSTFF-------------LPELDLIYGIFTTNVNSIAA-- 316
Cdd:cd11272    245 RLCKDD--------PKFHSYVSLPFGCVRGGV---EYRLLQAAYLskpgevlarslniTAQEDVLFAIFSKGQKQYHHpp 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  317 --SAVCIFNLSA----IAQAFAGPFKYQENSRSAWL----------PYPnPNPNFqCG-TVDQGLYVNlternlqdaqkf 379
Cdd:cd11272    314 ddSALCAFPIRAinaqIKERLQSCYQGEGNLELNWLlgkdvqctkaPVP-IDDNF-CGlDINQPLGGS------------ 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  380 ilmhevvQPVTTVPSFMEDNSRFSHVVVDVVQGREalvhIIYLATDYGTIKKVRA--PLNqtaSSCLLEEIELFpeRRRE 457
Cdd:cd11272    380 -------TPVEGVTLYTSSRDRLTSVASYVYNGYS----VVFVGTKSGKLKKIRAdgPPH---GGVQYEMVSVF--KDGS 443

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942836  458 PI-RSLQILHSQSVLLVGLWEHVVKIPLKRCQFYRTHSTCIGAQDPYCGWDVVMKKCT 514
Cdd:cd11272    444 PIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDPHCGWCALHNMCS 501
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 853-901 2.81e-07

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 48.04  E-value: 2.81e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1622942836  853 WSPWTKCSATCGGGHYMRTRSCSNPaPAYGGDIClGLHTEEALCNTQPC 901
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
906-949 9.18e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.64  E-value: 9.18e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622942836  906 SEWSDWSECEAS---GVQVRARQCILLFPVGSQCSGNTTESRPCVFD 949
Cdd:pfam00090    1 SPWSPWSPCSVTcgkGIQVRQRTCKSPFPGGEPCTGDDIETQACKMD 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 905-946 9.29e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.81  E-value: 9.29e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1622942836   905 WSEWSDWSECEAS---GVQVRARQCIL--LFPVGSQCSGNTTESRPC 946
Cdd:smart00209    1 WSEWSEWSPCSVTcggGVQTRTRSCCSppPQNGGGPCTGEDVETRAC 47
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 794-844 1.22e-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: 1.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622942836  794 SAWTSWSQCSRDCSRGIRNRKR---VcnnpEPKYGGMPClGPSLEYQECNILPC 844
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRtviV----EPQNGGRPC-PELLERRPCNLPPC 52
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
 49-363 2.26e-05

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


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 48.23  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836   49 EFRAKNAVdfSQLTFDPGQKELVVGARNYLFRLQlEDLSLIQAVEWECDEATKKaC-----YSKGKSKEECQNYIRVLLV 123
Cdd:cd11276      1 FFQSATEL--NHLVVDPQTGRVYLGAVNALYQLD-ADLQLESRVETGPKKDNKK-CtppieENQCTEAKMTDNYNKLLLL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  124 --GGDRLFTCGTnAFTPVCTNRSLSNLTEI----------------HDQISGMARCPYSPQHNSTALLTAGGE------L 179
Cdd:cd11276     77 dsANKTLVVCGS-LFKGICSLRNLSNISEViyysdtsgeksfvasnDEGVSTVGLISSLKPGNDRVFFVGKGNgsndngK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  180 YAATAMDFPGRDPAIYRSLGILPPLRTAqYNSKWLNepNFVSSYDIGNFTYFFFRENAVEHDCGKTVFsraARVCKNDIG 259
Cdd:cd11276    156 IISTRLLQNYDDREVFENYIDAATVKSA-YVSRYTQ--QFRYAFEDNNYVYFLFNQQLGHPDKNRTLI---ARLCENDHH 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942836  260 grflledtWTTFMKARLNC---------------SRPGEVPfyyneLQSTFFLPELD-LIYGIFTTNVNSIAASAVCIFN 323
Cdd:cd11276    230 --------YYSYTEMDLNCrdganaynkcqaayvSTPGKEL-----AQNYGNSILSDkVLFAVFSRDEKDSGESALCMFP 296

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1622942836  324 LSAIAQAF-----AGPFKYQENSRSAWLPYPNPNPNfQCGTVDQG 363
Cdd:cd11276    297 LKSINAKMeanreACYTGTIDDRDVFYKPFHSQKDI-ICGSHQQK 340
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
486-524 3.76e-05

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 42.15  E-value: 3.76e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1622942836   486 RCQFYRTHSTCIGAQDPYCGWDVVMKKCTSLEESLSMTQ 524
Cdd:smart00423    1 RCSKYTSCSECLLARDPYCAWCSSQGRCTSGERCDSRRQ 39
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 663-707 1.61e-04

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 40.34  E-value: 1.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622942836  663 TGWGPWERCTAQCGGGIQARRRTC-----ENGPDCAGcNVEYQPCNTNPC 707
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVivepqNGGRPCPE-LLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 906-946 1.93e-04

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.96  E-value: 1.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1622942836  906 SEWSDWSECEAS---GVQVRARQcILLFPV--GSQCsGNTTESRPC 946
Cdd:pfam19028    4 SEWSEWSECSVTcggGVQTRTRT-VIVEPQngGRPC-PELLERRPC 47
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 905-947 9.26e-04

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 42.63  E-value: 9.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622942836  905 WSEWSDWSEC-----EASGVQVRARQCIllFPVGSQCSGNTTESRPCV 947
Cdd:PTZ00087   233 YTEWGEWSNCsmecdHPDNVQIRERKCA--HPSGDCFKGDLKETRPCQ 278
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 602-653 1.12e-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: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622942836  602 TSWSPCSTTCGIGFQVRQRSCSNPTPR--HGGRVCVGQNREERKIHpalyCNEH 653
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKPPETQS----CNLK 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 855-901 2.74e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.05  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622942836  855 PWTKCSATCGGGhyMRTRS--CSNPAP--AYGGDICLGLH--TEEALCNTQPC 901
Cdd:pfam19030    5 PWGECSVTCGGG--VQTRLvqCVQKGGgsIVPDSECSAQKkpPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
546-593 3.34e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.63  E-value: 3.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622942836  546 WSPWTPCTHTDGSAVGSclcRTRSCDSPAPqcGGWQCEGPSMEIANCS 593
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQV---RQRTCKSPFP--GGEPCTGDDIETQACK 45
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 666-707 4.39e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 36.28  E-value: 4.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622942836  666 GPWERCTAQCGGGIQARRRTC--------ENGPDCAGCN--VEYQPCNTNPC 707
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCvqkgggsiVPDSECSAQKkpPETQSCNLKPC 55
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 660-710 6.25e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 39.93  E-value: 6.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942836  660 MFWTGWGPWERCTAQCG--GGIQARRRTCEN-GPDC-AGCNVEYQPCNT--NPCPEL 710
Cdd:PTZ00087   231 MFYTEWGEWSNCSMECDhpDNVQIRERKCAHpSGDCfKGDLKETRPCQVplPPCNSL 287
 
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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