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Conserved domains on  [gi|1907137465|ref|XP_036016203|]
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semaphorin-6D isoform X6 [Mus musculus]

Protein Classification

semaphorin( domain architecture ID 10336503)

semaphorin, containing Sema and PSI domains, is a regulatory molecule that functions in the development of the nervous system and in axonal guidance; may lack the Ig domain typically present in semaphorins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema super family cl15693
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
49-513 0e+00

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.


The actual alignment was detected with superfamily member cd11269:

Pssm-ID: 472829 [Multi-domain]  Cd Length: 465  Bit Score: 1028.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   49 SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPR 128
Cdd:cd11269      1 SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEVPKTEVTPSRKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  129 NDEMVFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 208
Cdd:cd11269     81 NDEMVFVCGTNAFNPMCRYYRLSTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPG 288
Cdd:cd11269    161 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  289 DSFFYFDVLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPG 368
Cdd:cd11269    241 DSFFYFDVLQSITDIIEINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  369 CCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVV 448
Cdd:cd11269    321 CCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTAIAVDHAAGPHQNYTVIFVGSEAGVV 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907137465  449 LKVLAKTSPFSLNDSVLLEEIEAYNPAKCSAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11269    401 LKILAKTSPFSLNDSVLLEEIEAYNHAKCSAENEEDRRVISLQLDRDHHALFVAFSSCVVRIPLS 465
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
514-543 1.30e-07

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: 49.24  E-value: 1.30e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907137465  514 RCERYGSCKkSCIASRDPYCGWLS-QGVCER 543
Cdd:pfam01437    1 RCSQYTSCS-SCLAARDPYCGWCSsEGRCVR 30
PHA03247 super family cl33720
large tegument protein UL36; Provisional
899-1046 2.61e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  899 LDPVGPMAEVPPKVPNREASLYSPPSTLPRNSPTKRVDVPTTPGVPMTslerqRGYHKNSSQRHSISAVPKNLNSPNGVL 978
Cdd:PHA03247  2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT-----RPAVASLSESRESLPSPWDPADPPAAV 2811
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907137465  979 LSRQPSMNR----GGYMPTPTGAKVdyIQGTPVSVHLQPSLSRQSSYTSNGTLPRTGLKRTPSLKPDVPPKP 1046
Cdd:PHA03247  2812 LAPAAALPPaaspAGPLPPPTSAQP--TAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP 2881
 
Name Accession Description Interval E-value
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
49-513 0e+00

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: 1028.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   49 SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPR 128
Cdd:cd11269      1 SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEVPKTEVTPSRKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  129 NDEMVFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 208
Cdd:cd11269     81 NDEMVFVCGTNAFNPMCRYYRLSTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPG 288
Cdd:cd11269    161 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  289 DSFFYFDVLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPG 368
Cdd:cd11269    241 DSFFYFDVLQSITDIIEINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  369 CCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVV 448
Cdd:cd11269    321 CCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTAIAVDHAAGPHQNYTVIFVGSEAGVV 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907137465  449 LKVLAKTSPFSLNDSVLLEEIEAYNPAKCSAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11269    401 LKILAKTSPFSLNDSVLLEEIEAYNHAKCSAENEEDRRVISLQLDRDHHALFVAFSSCVVRIPLS 465
Sema smart00630
semaphorin domain;
57-470 6.18e-140

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 426.01  E-value: 6.18e-140
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465    57 LDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVipskKLTWRSRQQDRENCAMKGKHK-DECHNFIKVFVPRNDEMVFV 135
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAEL----KTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLDYNEDRLLV 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   136 CGTNAFNPMCRYYRLrtleydgeeisglarcpfdarqtnvalfadGKLYSATVADFLASDAVIYRSMG-------DGSAL 208
Cdd:smart00630   77 CGTNAFQPVCRLRNL------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSL 126
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPG 288
Cdd:smart00630  127 RTVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGG-PRSLDKKWTSFLKARLECSVPG 205
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   289 DSFFYFDVLQSITDIIQINGIPTVV-GVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRP 367
Cdd:smart00630  206 EDPFYFNELQAAFLLPPGSESDDVLyGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRGKVPYPRP 285
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   368 GCCAKHGLaeaykTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYqNYTVIFVGSEAGV 447
Cdd:smart00630  286 GTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRVATDG-NYTVLFLGTSDGR 359
                           410       420
                    ....*....|....*....|...
gi 1907137465   448 VLKVLAKTSPfSLNDSVLLEEIE 470
Cdd:smart00630  360 ILKVVLSESS-SSSESVVLEEIS 381
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
297-474 1.68e-52

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: 181.70  E-value: 1.68e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  297 LQSITDIIQINGIP--TVV-GVFTTQL-NSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPeDKVPKPRPGCCAK 372
Cdd:pfam01403    1 LQDVFVLKPGAGDAldTVLyGVFTTQWsNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYT-GKVPYPRPGTCIN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  373 HGLaeayktSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYrlTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVL 452
Cdd:pfam01403   80 DPL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRL--TSIAVDRVQALDGNYTVLFLGTDDGRLHKVV 151
                          170       180
                   ....*....|....*....|..
gi 1907137465  453 AKTSpfslNDSVLLEEIEAYNP 474
Cdd:pfam01403  152 LVGS----EESHIIEEIQVFPE 169
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
514-543 1.30e-07

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: 49.24  E-value: 1.30e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907137465  514 RCERYGSCKkSCIASRDPYCGWLS-QGVCER 543
Cdd:pfam01437    1 RCSQYTSCS-SCLAARDPYCGWCSsEGRCVR 30
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
514-541 3.77e-05

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 42.15  E-value: 3.77e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907137465   514 RCERYGSCKkSCIASRDPYCGW-LSQGVC 541
Cdd:smart00423    1 RCSKYTSCS-ECLLARDPYCAWcSSQGRC 28
PHA03247 PHA03247
large tegument protein UL36; Provisional
899-1046 2.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  899 LDPVGPMAEVPPKVPNREASLYSPPSTLPRNSPTKRVDVPTTPGVPMTslerqRGYHKNSSQRHSISAVPKNLNSPNGVL 978
Cdd:PHA03247  2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT-----RPAVASLSESRESLPSPWDPADPPAAV 2811
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907137465  979 LSRQPSMNR----GGYMPTPTGAKVdyIQGTPVSVHLQPSLSRQSSYTSNGTLPRTGLKRTPSLKPDVPPKP 1046
Cdd:PHA03247  2812 LAPAAALPPaaspAGPLPPPTSAQP--TAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP 2881
 
Name Accession Description Interval E-value
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
49-513 0e+00

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: 1028.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   49 SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPR 128
Cdd:cd11269      1 SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEVPKTEVTPSRKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  129 NDEMVFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 208
Cdd:cd11269     81 NDEMVFVCGTNAFNPMCRYYRLSTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPG 288
Cdd:cd11269    161 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  289 DSFFYFDVLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPG 368
Cdd:cd11269    241 DSFFYFDVLQSITDIIEINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  369 CCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVV 448
Cdd:cd11269    321 CCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTAIAVDHAAGPHQNYTVIFVGSEAGVV 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907137465  449 LKVLAKTSPFSLNDSVLLEEIEAYNPAKCSAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11269    401 LKILAKTSPFSLNDSVLLEEIEAYNHAKCSAENEEDRRVISLQLDRDHHALFVAFSSCVVRIPLS 465
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
49-513 0e+00

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: 953.50  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   49 SGNESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPR 128
Cdd:cd11242      1 DNTTARHRLDFQRMLRINRTLYIAARDHVYTVDLDASHTEEIVPSKKLTWRSRQADVENCRMKGKHKDECHNFIKVLVPR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  129 NDEMVFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 208
Cdd:cd11242     81 NDETLFVCGTNAFNPVCRNYRIDTLEQDGEEISGMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSLGDSPTL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPG 288
Cdd:cd11242    161 RTVKYDSKWLKEPHFVHAVEYGDYVYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGSPRVLEKQWTSFLKARLNCSVPG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  289 DSFFYFDVLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPG 368
Cdd:cd11242    241 DSHFYFDVLQAVTDVIRINGRPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPEDRVPKPRPG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  369 CCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVV 448
Cdd:cd11242    321 CCAGSGSAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYRLTQIAVDNAAGPYQNYTVVFLGSEAGTV 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907137465  449 LKVLAKTSPFSLNDSVLLEEIEAYNPAKCSAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11242    401 LKFLARIGPSGSNGSVFLEEIDVYNPAKCSYDGEEDRRIIGLELDRASHALFVAFSGCVIRVPLS 465
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
54-512 0e+00

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: 735.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   54 QHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEMV 133
Cdd:cd11266      6 RHRLDIQMIMIMNRTLYIAARDHIYTVDIDTSHTEEIYFSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKRNDDTL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  134 FVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKY 213
Cdd:cd11266     86 FVCGTNAFNPSCRNYKMDTLEFFGDEFSGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKH 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  214 DSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPGDSFFY 293
Cdd:cd11266    166 DSKWLKEPYFVQAVDYGDYIYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGSQRVLEKQWTSFLKARLNCSVPGDSHFY 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  294 FDVLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCAKH 373
Cdd:cd11266    246 FNILQAVTDVIHINGRDVVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDERVPKPRPGCCAGS 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  374 GLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVLA 453
Cdd:cd11266    326 SSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLA 405
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907137465  454 KT--SPFsLNDSVLLEEIEAYNPAKCSAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPL 512
Cdd:cd11266    406 RTgnSGF-LNDSLFLEEMNVYNSEKCSYDGVEDKRIMGMQLDKASSALYVAFSTCVIKVPL 465
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
57-513 0e+00

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: 670.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   57 LDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTeVIPSKKLTWRSrqQDRENCAMKGKHKDECHNFIKVFVPRNDEMVFVC 136
Cdd:cd11270      9 LDFQRMLRINHMVYIAARDHVFAINLSASLER-IVPQQKLTWKT--KDVEKCTVRGKNSDECYNYIKVLVPRNDETLFAC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  137 GTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGS-ALRTIKYDS 215
Cdd:cd11270     86 GTNAFNPTCRNYKMSSLEQDGEEVIGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLGESSpVLRTVKYDS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  216 KWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPGDSFFYFD 295
Cdd:cd11270    166 KWLREPHFLHAIEYGNYVYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSPRVLERYWTSFLKARLNCSVPGDSFFYFD 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  296 VLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCAKHGL 375
Cdd:cd11270    246 VLQSLTNVMQINHRPAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVPDEAVPKPRPGSCAGDGP 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  376 AEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVLAKT 455
Cdd:cd11270    326 AAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFKLTQIAVDTAAGPYKNYTVVFLGSENGHVLKVLASM 405
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137465  456 SPFSLNDSVLLEEIEAYNPAKCSAEsEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11270    406 HPNSSYSTQVLEDIDVYNPNKCNVR-GEDRRILGLELDKDHHALFVAFTGCVIRVPLS 462
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
52-513 0e+00

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: 668.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   52 ESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDE 131
Cdd:cd11267      4 RGRDRLNIQRVLRVNRTLYIGDRDNLYRVELDPTAGTEMRYHKKLTWRSNKNDINVCRMKGKHEGECRNFIKVLLLRDYG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  132 MVFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTI 211
Cdd:cd11267     84 TLFVCGTNAFNPVCANYSIDTLEPVGDNISGMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRTV 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  212 KYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPGDSF 291
Cdd:cd11267    164 KHDSKWFKEPYFVHAVEWGSHVYFFFREIAMEFNYLEKVVVSRVARVCKNDMGGSQRVLEKQWTSFLKARLNCSVPGDSH 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  292 FYFDVLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCA 371
Cdd:cd11267    244 FYFNVLQAVSDILNLGGRPVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEELVPRPRPGCCA 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  372 KHGLaeAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVVLKV 451
Cdd:cd11267    324 APGM--RYNSSSTLPDEVLNFVKTHPLMDEAVPSLGHAPWIVRTMTRYQLTHMVVDTEAGPHGNHTVVFLGSTRGTVLKF 401
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907137465  452 L----AKTSPFSlNDSVLLEEIEAYNPAKCSAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11267    402 LiipnASSSEIS-NQSVFLEELETYNPERCGWDSPQAQKLLSLELDKGSGGLLLAFPSCVVRVPVA 466
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
57-513 0e+00

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: 558.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   57 LDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTE-VIPSKKLTWRSrqQDRENCAMKGKHKDECHNFIKVFVPRNDEMVFV 135
Cdd:cd11268      9 LDFQRFLTLNRTLLVAARDHVFSFDLQAEEEGEgLVPNKYLTWRS--QDVENCAVRGKLTDECYNYIRVLVPWDSQTLLA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  136 CGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDS 215
Cdd:cd11268     87 CGTNSFSPVCRSYGITSLQQEGEELSGQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  216 KWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPGDSFFYFD 295
Cdd:cd11268    167 KWLREPHFVQALEHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSPRALDRHWTSFLKLRLNCSVPGDSTFYFD 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  296 VLQSITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCAKHGL 375
Cdd:cd11268    247 VLQALTGPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVSEDRVPSPRPGSCAGVGG 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  376 AEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRvRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVLAKT 455
Cdd:cd11268    327 AALFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLTLTS-RALLTQVAVDGMAGPHSNITVMFLGSNDGTVLKVLPPG 405
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  456 SPFSLNDSVLLEEIEAYNPAKCSAE--SEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11268    406 GRSGGPEPILLEEIDAYSPARCSGKrtAQTARRIIGLELDTEGHRLFVAFSGCIVYLPLS 465
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
61-512 0e+00

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


Pssm-ID: 200496 [Multi-domain]  Cd Length: 437  Bit Score: 549.70  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   61 LMLKIRDTLYIAGRDQVYTVNLNEIPQtevipSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEMVFVCGTNA 140
Cdd:cd11235      7 LLHEDRSTLYVGARDRVYLVDLDSLYT-----EQKVAWPSSPDDVDTCYLKGKSKDDCRNFIKVLEKNSDDSLLVCGTNA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  141 FNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKE 220
Cdd:cd11235     82 FNPSCRNYNVETFELVGKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWLNE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  221 PHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRvLEKHWTSFLKARLNCSVPGDSFFYFDVLQSI 300
Cdd:cd11235    162 PQFVGAFDIGDYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRS-LEKKWTTFLKARLNCSVPGEFPFYFNELQDV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  301 TDIIQINGIPTVV-GVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCakhglaeaY 379
Cdd:cd11235    241 FDLPSPSNKEKIFyAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDERVPEPRPGTC--------V 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  380 KTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRS-AGPYQNYTVIFVGSEAGVVLKVLAKTSpF 458
Cdd:cd11235    313 DDSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDVNYRFTKIAVDRVqAKLGQTYDVLFVGTDRGIILKVVSLPE-Q 391
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907137465  459 SLNDSVLLEEIEAYNPAKcsaeseedrKVVSLQLDKDHHALYVAFSSCVVRIPL 512
Cdd:cd11235    392 GLQASNILEEMPVGPPPE---------PIQTMQLSRKRRSLYVGSETGVLQVPL 436
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
50-515 3.40e-164

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: 491.08  E-value: 3.40e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   50 GNESQHrldFQLMLKIRDTLYIAGRDQVYTVNLNEIpqTEVipsKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRN 129
Cdd:cd11237      1 ETHSDH---FKLLDQDGNSLLVGARNAVYNISLSDL--TEN---QRIEWPSSDAHREMCLLKGKSEDDCQNYIRVLAKKS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  130 DEMVFVCGTNAFNPMCRYYRLRTLEYDGE-EISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSmgdgsAL 208
Cdd:cd11237     73 AGRLLVCGTNAYKPLCREYTVKDGGYRVErEFDGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYRE-----PL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRvLEKHWTSFLKARLNCSVPG 288
Cdd:cd11237    148 RTERYDLKQLNAPNFVSSFAYGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHP-FRDRWTSFLKARLNCSVPG 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  289 DSFFYFDVLQSITDII--QINGI--PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPK 364
Cdd:cd11237    227 EYPFYFNEIQSTSDIVegGYGGKsaKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVPSNKVPE 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  365 PRPGCCAkhglaeayKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVD---RSAGPyQNYTVIFV 441
Cdd:cd11237    307 PRPGQCV--------NDSRTLPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQYRFTQIAVDpqvKALDG-KYYDVLFI 377
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137465  442 GSEAGVVLKVL--AKTSPFSLNDSVLLEEIEAYNPAKcsaeseedrKVVSLQL--DKDHHALYVAFSSCVVRIPLSRC 515
Cdd:cd11237    378 GTDDGKVLKAVniASADTVDKVSPVVIEETQVFPRGV---------PIRNLLIvrGKDDGRLVVVSDDEIVSIPLHRC 446
Sema smart00630
semaphorin domain;
57-470 6.18e-140

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 426.01  E-value: 6.18e-140
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465    57 LDFQLMLKIRDTLYIAGRDQVYTVNLNEIPQTEVipskKLTWRSRQQDRENCAMKGKHK-DECHNFIKVFVPRNDEMVFV 135
Cdd:smart00630    1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAEL----KTGPVLSSPDCEECVSKGKDPpTDCVNYIRLLLDYNEDRLLV 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   136 CGTNAFNPMCRYYRLrtleydgeeisglarcpfdarqtnvalfadGKLYSATVADFLASDAVIYRSMG-------DGSAL 208
Cdd:smart00630   77 CGTNAFQPVCRLRNL------------------------------GELYVGTVADFSGSDPAIPRSLSvrrlkgtSGVSL 126
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPG 288
Cdd:smart00630  127 RTVLYDSKWLNEPNFVYAFESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGG-PRSLDKKWTSFLKARLECSVPG 205
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   289 DSFFYFDVLQSITDIIQINGIPTVV-GVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRP 367
Cdd:smart00630  206 EDPFYFNELQAAFLLPPGSESDDVLyGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYSRGKVPYPRP 285
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   368 GCCAKHGLaeaykTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYqNYTVIFVGSEAGV 447
Cdd:smart00630  286 GTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRVATDG-NYTVLFLGTSDGR 359
                           410       420
                    ....*....|....*....|...
gi 1907137465   448 VLKVLAKTSPfSLNDSVLLEEIE 470
Cdd:smart00630  360 ILKVVLSESS-SSSESVVLEEIS 381
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
51-515 6.85e-128

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: 397.50  E-value: 6.85e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   51 NESQHRLDFQLMLK--IRDTLYIAGRDQVYTVNLNEIPQteviPSKKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVP 127
Cdd:cd11239      2 LGSMNSLDYRSLLLdeDRDRLYVGGKDHILSLSLDNINQ----DPKKIYWPASPERIEECKMAGKDPNtECANFVRVLQP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  128 RNDEMVFVCGTNAFNPMCRY----YRLR----TLEYDGEEiSGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIY 199
Cdd:cd11239     78 YNRTHLYACGTGAFHPICAFinvgRRLEdpifKLDDSSLE-SGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  200 RSMGDGSALRTIKYDSKWIKEPHFLHAI-------EYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEK 272
Cdd:cd11239    157 RSLGHRHYIRTEQYDSRWLNEPKFVGAYlipdsdnPDDDKVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGG-QRSLVN 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  273 HWTSFLKARLNCSVPG----DSffYFDVLQSITdIIQINGI--PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKE 346
Cdd:cd11239    236 KWSTFLKARLVCSVPGpdgiDT--YFDELEDVF-LLPTRDPknPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAH 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  347 QKTPDSVWTAVpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEV 426
Cdd:cd11239    313 KEGPNYQWVEY-QGKVPYPRPGTCPSKTYGPLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPYRLTQIAV 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  427 DRSAGPYQNYTVIFVGSEAGVVLKVLAKTSPFSLNDSVLLEEIEAYnpakcsaesEEDRKVVSLQLDKDHHALYVAFSSC 506
Cdd:cd11239    392 DRVEAEDGQYDVLFIGTDSGTVLKVVSLPKENWEMEEVILEELQVF---------KHPSPITSMEISSKRQQLYVGSAEG 462

                   ....*....
gi 1907137465  507 VVRIPLSRC 515
Cdd:cd11239    463 VVQLPLHRC 471
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
67-513 3.07e-118

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: 371.74  E-value: 3.07e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   67 DTLYIAGRDQVYTVNLNEIPQTEvipSKKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDEMVFVCGTNAFNPMC 145
Cdd:cd11240     19 GTLYVGAREALFALNVSDISTEL---KDKIKWEASEDKKKECANKGKDNQtDCFNFIRILQFYNSTHLYVCGTFAFSPRC 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  146 RYYRLRTLEYDGEEI-SGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTiKYDSKWIKEPHFL 224
Cdd:cd11240     96 TYINLSDFSLSSIKFeDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEGNVLKT-ENTLRWLNEPAFV 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  225 HA----------IEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFfYF 294
Cdd:cd11240    175 GSahiresidspDGDDDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGG-QRTLQKKWTTFLKAQLVCSQPDSGL-PF 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  295 DVLQsitDIIQING----IPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVpEDKVPKPRPGCC 370
Cdd:cd11240    253 NVLR---DVFVLSPdswdATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRY-TGPVPDPRPGAC 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  371 AKHGLAEA-YKTSIDFPDDTLAFIKSHPLMDSAVPPIaDEPWFTKTRVRYrlTAIEVDRSAGPY-QNYTVIFVGSEAGVV 448
Cdd:cd11240    329 ITNSARSQgITSSLNLPDNVLTFVKDHPLMDEQVHPI-NRPLLVKSGVNY--TRIAVHRVQALDgQTYTVLFLGTEDGFL 405
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907137465  449 LKVLaktspfSLNDSV-LLEEIEAYNPAKcsaeseedrKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11240    406 HKAV------SLDGGMhIIEEIQLFDQPQ---------PVKNLLLSSSKGVLYVGSSSGVVQVPLS 456
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
66-512 2.66e-104

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: 332.25  E-value: 2.66e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   66 RDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDE-MVFVCGTNAFNPM 144
Cdd:cd09295     11 KDTIYVGAIARIYKVDGGGTRLLLSCISPELNFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGDLdILAVCGSNAAQPS 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  145 CRYYRLRTLEYDGEE--ISGLARCPFDARQTNVALFADGKLYSATVADFL-ASDAVIYRSMGDGSALRTIKYDSKWIKEP 221
Cdd:cd09295     91 CGSYRLDVLVELGKVrwPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNVHYLRIVVDSSTGLDEI 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  222 HFLHAIEYG---NYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRvLEKHWTSFLKARLNCSVPGDSfFYFDVLQ 298
Cdd:cd09295    171 TFVYAFVSGdddDEVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHR-LKKKLTSFLKADLNCSRPQSG-FAFNLLQ 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  299 SITDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFkgrfkeqktpdsvwtavpedkvpkprpgccakhglaea 378
Cdd:cd09295    249 DATGDTKNLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVF-------------------------------------- 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  379 yktsidfpddtlafikshplmDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVLAKtspF 458
Cdd:cd09295    291 ---------------------DDPVEAINNRPLYAHQNQRSRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKALAF---F 346
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907137465  459 SLNDSVLLEEIEAYNPakcsaeseeDRKVVSLQLDKDHHALYVAFSSCVVRIPL 512
Cdd:cd09295    347 FLYKGHIIEEWKVFKD---------SSRITNLDLSRPPLYLYVGSESGVLGVPV 391
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
58-515 1.17e-102

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: 330.63  E-value: 1.17e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   58 DFQLMLKIRDT--LYIAGRDQVYTVNLNEIPQTEVIpskkLTWRSRQQDRENCAMKGK-HKDECHNFIKVFVPRNDEMVF 134
Cdd:cd11254      9 DYRILLKDEDHdrMYVGSKDYVLSLDLHDINREPLI----IHWPASPQRIEECILSGKgSNGECGNFIRLIQPWNRTHLY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  135 VCGTNAFNPMCRY-YRLRT-------LEYDGEEiSGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGS 206
Cdd:cd11254     85 VCGTGAYNPVCAYiNRGRRaedymfrLEPDKLE-SGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMGKQP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  207 ALRTIKYDSKWIKEPHFLHAI-------EYGNYVYFFFREIAVEHNNlGKAVYSRVARICKNDMGGsQRVLEKHWTSFLK 279
Cdd:cd11254    164 AMRTDQYNSRWLNDPAFVHAHlipdsseKNDDKLYFFFREKSLEAPQ-SPAVLSRIGRVCLNDDGG-HCCLVNKWSTFLK 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  280 ARLNCSVPGDSFF--YFDVLQSI-TDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTA 356
Cdd:cd11254    242 ARLVCSVPGADGIetHFDELRDVfIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  357 VpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNY 436
Cdd:cd11254    322 Y-TGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGRY 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  437 TVIFVGSEAGVVLKVLAKTSPFSLNDSVLLEEIEAYN-PAkcsaeseedrKVVSLQLDKDHHALYVAFSSCVVRIPLSRC 515
Cdd:cd11254    401 EVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKvPA----------PIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
58-513 1.26e-101

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: 326.94  E-value: 1.26e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   58 DF-QLMLKI-RDTLYIAGRDQVYTVNLNEIPQTEVIpskklTWRSRQQDRENCAMKGKHKDECHNFIKVFVPrNDEMVFV 135
Cdd:cd11264      8 DFsQLALDLnRNQLIVGARNYLFRLSLHNVSLIQAT-----EWGSDEDTRRSCQSKGKTEEECQNYVRVLIV-YGKKVFT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  136 CGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFAD-GKLYSATVADFLASDAVIYRSMGDGSALRTIKYD 214
Cdd:cd11264     82 CGTNAFSPVCTSRQVGNLSKVIERINGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQYN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  215 SKWIKEPHFLHAIEYGNYVYFFFREIAVEHnNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGDSFFYF 294
Cdd:cd11264    162 SKWLNEPNFIAAYDIGLFTYFFFRENAVEH-DCGKTVYSRVARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPGEIPFYY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  295 DVLQSITDIIQINgipTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPeDKVPKPRPGCCAKHG 374
Cdd:cd11264    240 NELQSTFYLPEQD---LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTA-NPIPNFQCGTLSDDS 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  375 LAEAYkTSIDFPDDTLAFikshpLMDSAVPPIADEPWFTKTRVRYrlTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVLAK 454
Cdd:cd11264    316 PNENL-TERSLQDAQRLF-----LMNDVVQPVTVDPLVTQDSVRF--SKLVVDIVQGKDTLYHVMYIGTEYGTILKALST 387
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907137465  455 TSPfSLNdSVLLEEIEAYNPAKcsaeseeDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11264    388 TNR-SLR-SCYLEEMQILPPGQ-------REPIRSLQILHSDRSLFVGLNNGVLKIPLE 437
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
44-512 3.49e-101

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: 325.66  E-value: 3.49e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   44 FRGRPSGNESQHRLDfqlmlKIRDTLYIAGRDQVYTVNLNEIPQTEVIPskkltWRSRQQDRENCAMKGKHKDECHNFIK 123
Cdd:cd11241      1 FEIEYVSDFSRLVLD-----PTHDQLIVGARNYLFRLRLQSLSLLQAVP-----WNSDEDTKRQCQSKGKSVEECQNYVR 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  124 VFVPrNDEMVFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALF-ADGKLYSATVADFLASDAVIYRSM 202
Cdd:cd11241     71 VLLV-VGKNLFTCGTYAFSPVCTIRKLSNLTQILDTISGVARCPYSPAHNSTALIsASGELYAGTVYDFSGRDPAIYRSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  203 GDGSALRTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARL 282
Cdd:cd11241    150 GGKPPLRTAQYNSKWLNEPNFVGSYEIGNHTYFFFRENAVEHQDCGKTVYSRIARVCKNDIGG-RFLLEDTWTTFMKARL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  283 NCSVPGDSFFYFDVLQsitDIIQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPedkV 362
Cdd:cd11241    229 NCSLPGEFPFYYNEIQ---GTFYLPETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPTP---N 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  363 PKPRPGCCAKHGLAEAYKTSIDFPDDTLAFIkshpLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGpYQNYTVIFVG 442
Cdd:cd11241    303 PHPNFQCTTSIDRGQPANTTERDLQDAQKYQ----LMAEVVQPVTKIPLVTMDDVRFSKLAVDVVQGRG-TQLVHIFYVG 377
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  443 SEAGVVLKVLaktSPFSLNDSVLLEEIEAYNPAKCSaeseedrKVVSLQLDKDHHALYVAFSSCVVRIPL 512
Cdd:cd11241    378 TDYGTILKMY---QPHRSQKSCTLEEIKILPAMKGE-------PITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
66-451 8.78e-101

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: 325.15  E-value: 8.78e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   66 RDTLYIAGRDQVYTVNLNEIPQTEVIPSKKLTWRSRQqDRENCAMKGKHKD-ECHNFIKVFVPRND-EMVFVCGTNAFNP 143
Cdd:cd11238     12 RNALYVGAMDRVFRLNLYNINDTGNNCARDELTLSPS-DVSECVSKGKDEEyECRNHVRVIQPMGDgQTLYVCSTNAMNP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  144 MCRYY---RLRTLEYDGEEISGLARCPFDARQTNVALFADG-------KLYSATVADFLASDAVIYRS----MGDG---S 206
Cdd:cd11238     91 KDRVLdanLLHLPEYVPGPGNGIGKCPYDPDDNSTAVWVEWgnpgdlpALYSGTRTEFTKANTVIYRPplynNTKGrheS 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  207 ALRTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSV 286
Cdd:cd11238    171 FMRTLKYDSKWLDEPNFVGSFDIGDYVYFFFRETAVEYINCGKVVYSRVARVCKKDTGG-KNVLRQNWTTFLKARLNCSI 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  287 PGDSFFYFDVLQSITdiiQINGI--PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVF-KGRFKEQKTPDSVWTAVPEDKVP 363
Cdd:cd11238    250 SGEFPFYFNEIQSVY---KVPGRddTLFYATFTTSENGFTGSAVCVFTLSDINAAFdTGKFKEQASSSSAWLPVLSSEVP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  364 KPRPGCCAkhglaeayKTSIDFPDDTLAFIKSHPLMDSAVPpiADEPWFTKTRVryRLTAIEVDRSAGPYQNYTVIFVGS 443
Cdd:cd11238    327 EPRPGTCV--------NDSATLSDTVLHFARTHPLMDDAVS--HGPPLLYLRDV--VFTHLVVDKLRIDDQEYVVFYAGS 394

                   ....*...
gi 1907137465  444 EAGVVLKV 451
Cdd:cd11238    395 NDGKVYKI 402
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
66-516 4.57e-100

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: 324.65  E-value: 4.57e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   66 RDTLYIAGRDQVYTVNLNEIPQTEvipskKLTWRSRQQDRENCAMKGKH-KDECHNFIKVFVPRNDEMVFVCGTNAFNPM 144
Cdd:cd11249     41 RGRLYVGAKDHIFSFNLVNIKDFQ-----KIVWPVSPSRRDECKWAGKDiLKECANFIKVLKAYNQTHLYACGTGAFHPV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  145 CRY-----------YRLRTLEYDgeeiSGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKY 213
Cdd:cd11249    116 CTYievghhpedniFRLEDSHFE----NGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQH 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  214 DSKWIKEPHFL--HAI-EYGN----YVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKhWTSFLKARLNCSV 286
Cdd:cd11249    192 DSRWLNDPRFIsaHLIpESDNpeddKIYFFFRENAIDGEHTGKATHARIGQLCKNDFGGHRSLVNK-WTTFLKARLICSV 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  287 PGDSFF--YFDVLQsitDIIQINGI----PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWtaVP-E 359
Cdd:cd11249    271 PGPNGIdtHFDELQ---DVFLMNSKdpknPIVYAVFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQW--VPfQ 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  360 DKVPKPRPGCCAKHGLAeAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVI 439
Cdd:cd11249    346 GRVPYPRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKTDVDYQFTQIVVDRVEAEDGQYDVM 424
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907137465  440 FVGSEAGVVLKVLA--KTSPFSLnDSVLLEEIEAYnpakcsaesEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLSRCE 516
Cdd:cd11249    425 FIGTDMGTVLKVVSipKETWHDL-EEVLLEEMTVF---------REPTAISAMELSTKQQQLYIGSAIGVSQLPLHRCD 493
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
53-511 2.25e-99

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: 320.57  E-value: 2.25e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   53 SQHRLDFQlmlkiRDTLYIAGRDQVYTVNLNEIPQTEVIPskkltWRSRQQDRENCAMKGKHKDECHNFIKVFVPrNDEM 132
Cdd:cd11265     10 SQMLFDVA-----RNQVIVGARDNLYRLSLDGLELLERAS-----WPAAESKVALCQNKGQSEEDCHNYVKVLLS-YGKQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  133 VFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALFA-DGKLYSATVADFLASDAVIYRSMG--DGSALR 209
Cdd:cd11265     79 LFACGTNAFSPRCSWREMENLTSVTEWDSGVAKCPYSPHANITALLSsSGQLFVGSPTDFSGSDSAIYRTLGtsNKSFLR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  210 TIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPGD 289
Cdd:cd11265    159 TKQYNSKWLNEPQFVGSFETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLLKDNWTTFLKARLNCSLPGE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  290 SFFYFDVLQSITdIIQINGIptVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKvpKPRPGC 369
Cdd:cd11265    239 YPFYFDEIQGMT-YLPDEGI--LYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVNVNH--RDHFNQ 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  370 C---AKHGLAEAYKtsidfpddtlafiksHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVdRSAGPYQNYTVIFVGSEAG 446
Cdd:cd11265    314 CsssSSSHLLESSR---------------YQLMDEAVQPITLEPLHHAKLERFSHIAVDV-IPTKIHQSVHVLYVATTGG 377
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907137465  447 VVLK--VLAKTSpfslnDSVLLEEIEaynpakcsAESEEDRKVVSLQLDKDHHALYVAFSSCVVRIP 511
Cdd:cd11265    378 LIKKisVLPRTQ-----ETCLVEIWQ--------PLPTPDSPIKTMQYLKVTDSLYVGTELALMRIP 431
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
53-515 4.69e-99

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: 321.09  E-value: 4.69e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   53 SQHRLDFQLML--KIRDTLYIAGRDQVYTVNLNEIPQTevipSKKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRN 129
Cdd:cd11252      4 SSEGLDFQTLLldEERGRLLLGAKDHIYLLDLVDLNKN----PKKIYWPAAKERVELCKLAGKDANtECANFIRVLHPYN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  130 DEMVFVCGTNAFNPMCRYYRLRT------LEYDGEEI-SGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSM 202
Cdd:cd11252     80 RTHVYVCGTGAFHPTCGYIELGThkedriFLLDTQNLeSGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  203 G---DGSALRTIKYDSKWIKEPHFL--HAIE--YG---NYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEK 272
Cdd:cd11252    160 GptpDHHYIRTDISEHYWLNGAKFIgtFPIPdtYNpddDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGG-QRSLIN 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  273 HWTSFLKARLNCSVPG----DSffYFDVLQSITDI-IQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQ 347
Cdd:cd11252    239 KWTTFLKARLVCSIPGpdgaDT--HFDELQDIFLLpTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHK 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  348 KTPDSVWTAVpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVD 427
Cdd:cd11252    317 ESPDHRWVQY-EGRIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVD 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  428 RSAGPYQNYTVIFVGSEAGVVLKVLAKTSPFSLNDSVLLEEIEAY-NPAkcsaeseedrKVVSLQLDKDHHALYVAFSSC 506
Cdd:cd11252    396 HVAAEDGQYDVMFLGTDIGTVLKVVSITKEKWTMEEVVLEELQIFkHPS----------PILNMELSLKQQQLYIGSRDG 465

                   ....*....
gi 1907137465  507 VVRIPLSRC 515
Cdd:cd11252    466 LVQLSLHRC 474
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
66-515 9.67e-99

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: 320.32  E-value: 9.67e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   66 RDTLYIAGRDQVYTVNLNEIPQTEvipsKKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDEMVFVCGTNAFNPM 144
Cdd:cd11250     19 RGRLFVGAKNYLASLSLDNISKQE----KKIYWPAPVEWREECNWAGKDINtDCMNYVKILHHYNRTHLYACGTGAFHPT 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  145 CRYYRL------RTLEYDGEEIS-GLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKW 217
Cdd:cd11250     95 CAFVEVgqrmedHVFRLDPSRVEdGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRPSLRTEQHDSRW 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  218 IKEPHFLHAI---EYGN----YVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPGD- 289
Cdd:cd11250    175 LNEPKFVKVFwipESENpdddKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGG-QRSLVNKWTTFLKARLVCSVPGNe 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  290 -SFFYFDVLQSITdIIQING--IPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVpEDKVPKPR 366
Cdd:cd11250    254 gGDTHFDELRDVF-LLQTRDkrNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSY-QGKVPYPR 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  367 PGCCAKHGLAeAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQNYTVIFVGSEAG 446
Cdd:cd11250    332 PGMCPSKTFG-SFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPYTFTQIAVDRVAAADGHYDVMFIGTDVG 410
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907137465  447 VVLKVLA--KTSPFSlNDSVLLEEIEAYnpakcsaesEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLSRC 515
Cdd:cd11250    411 SVLKVISvpKGSWPS-NEELLLEELHVF---------KDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
52-512 9.50e-97

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: 313.89  E-value: 9.50e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   52 ESQHRLDF-QLMLKIRDTLYIAG-RDQVYTVNLNEIPQTEVIpskklTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRN 129
Cdd:cd11263      2 RAENAVDFsQLTFDPGQKELIVGaRNYLFRLQLEDLSLIQAV-----EWECDEATKKACYSKGKSKEECQNYIRVLLVGG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  130 DEMvFVCGTNAFNPMCRYYRLRTLEYDGEEISGLARCPFDARQTNVALF-ADGKLYSATVADFLASDAVIYRSMGDGSAL 208
Cdd:cd11263     77 DRL-FTCGTNAFTPICTNRTLNNLTEIHDQISGMARCPYSPQHNSTALLtSSGELYAATAMDFPGRDPAIYRSLGILPPL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  209 RTIKYDSKWIKEPHFLHAIEYGNYVYFFFREIAVEHnNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPG 288
Cdd:cd11263    156 RTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEH-DCGKTVFSRAARVCKNDIGG-RFLLEDTWTTFMKARLNCSRPG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  289 DSFFYFDVLQSITDIIQINgipTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEdkvPKPRPG 368
Cdd:cd11263    234 EIPFYYNELQSTFFLPELD---LIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPN---PNPNFQ 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  369 C-CAKHGLaeayktSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYrlTAIEVDRSAGPYQNYTVIFVGSEAGV 447
Cdd:cd11263    308 CgTMDQGL------YVNLTERNLQDAQKFILMHEVVQPVTPVPYFMEDNSRF--SHVAVDVVQGKDMLFHIIYLATDYGT 379
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907137465  448 VLKVLAKTSPFSlnDSVLLEEIEAYNPAKcsaeseeDRKVVSLQLDKDHHALYVAFSSCVVRIPL 512
Cdd:cd11263    380 IKKVLAPLNQSS--SSCLLEEIELFPKRQ-------REPIRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
56-515 4.04e-93

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: 305.24  E-value: 4.04e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   56 RLDFQLML--KIRDTLYIAGRDQVYTVNLNEIPQteviPSKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEMV 133
Cdd:cd11253      7 FLDLHTMLldEYQERLFVGGRDLLYSLSLERISA----NYKEIHWPSTQLQVEDCIMKGRDKPECANYIRVLHHYNRTHL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  134 FVCGTNAFNPMCRYYR--------LRTLEYDGEEiSGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDG 205
Cdd:cd11253     83 LACGTGAFDPVCAFIRvgrgsedhLFQLESDKFE-RGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMNHL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  206 SALRTIKYDSKWIKEPHFLHAI-------EYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFL 278
Cdd:cd11253    162 AHIRTEHDDERLLKEPKFVGSYmipdnedPDDNKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGG-QRMLVNKWSTFL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  279 KARLNCSVPGDSFF--YFDVLQSITDI-IQINGIPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWt 355
Cdd:cd11253    241 KTRLICSVPGPNGIdtHFDELEDVFLLrTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHW- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  356 AVPEDKVPKPRPGCCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYQN 435
Cdd:cd11253    320 SVYEGKVPYPRPGSCASKVNGGHYGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNLKQIAVDRVEAEDGQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  436 YTVIFVGSEAGVVLKVLA-KTSPFSLNDSVLLEEIEAYnpakcsaesEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLSR 514
Cdd:cd11253    400 YDVLFIGTDNGIVLKVITiYNQETETMEEVILEELQVF---------KVPVPIISMEISSKRQQLYIGSESGVAQIRFHQ 470

                   .
gi 1907137465  515 C 515
Cdd:cd11253    471 C 471
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
57-515 1.40e-91

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: 301.06  E-value: 1.40e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   57 LDFQLML--KIRDTLYIAGRDQVYTVNLNeipQTEVIPsKKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDEMV 133
Cdd:cd11255      8 LHLSAVYldEYRDRLFLGGKDVLYSLRLD---QTHPDA-KEIHWPPLPGQREECIRKGKDPEtECANFVRVLQPFNRTHL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  134 FVCGTNAFNPMCRYYrlrTLEYDGEEI---------SGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGD 204
Cdd:cd11255     84 LACGTGAFQPVCALI---NVGHRGEHVfsldpttveSGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  205 GSALRTiKYDSKWIKEPHFLHAI-------EYGNYVYFFFREIAVE-HNNLGKAVYSRVARICKNDMGGsQRVLEKHWTS 276
Cdd:cd11255    161 RSPLRT-ETDQRLLHEPRFVAAHlipdnadRDNDKVYFFFTERATEtAEDDDGAIHSRVGRLCANDAGG-QRVLVNKWST 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  277 FLKARLNCSVPGDSFF--YFDVLQSITDIIQINGI-PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSV 353
Cdd:cd11255    239 FIKARLVCSVPGPHGIqtHFDQLEDVFLLRTKDGKsPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  354 WTAVpEDKVPKPRPGCCAKHGLAE---AYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSA 430
Cdd:cd11255    319 WGPY-EGKVPYPRPGVCPSKITAQpgrAFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  431 GPYQNYTVIFVGSEAGVVLKVLA-KTSPFSLNDSVLLEEIEAYNPAKcsaeseedrKVVSLQLDKDHHALYVAFSSCVVR 509
Cdd:cd11255    398 AEDGYYDVMFIGTDSGSVLKVIVlQKGNSAAGEEVTLEELQVFKVPT---------PITEMEISVKRQMLYVGSRTGVAQ 468

                   ....*.
gi 1907137465  510 IPLSRC 515
Cdd:cd11255    469 VPLHRC 474
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
53-515 5.73e-89

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: 294.10  E-value: 5.73e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   53 SQHRLDFQLML--KIRDTLYIAGRDQVYTVNLNEIPQTevipSKKLTWRSRQQDRENCAMKGKHKDE-CHNFIKVFVPRN 129
Cdd:cd11251      4 SERPLDYRILFmdEDQDRIYVGSKDHILSLNINNISQD----ALSIFWPASASKVEECKMAGKDPTHgCGNFVRVIQPYN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  130 DEMVFVCGTNAFNPMCRYYRL------RTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMG 203
Cdd:cd11251     80 RTHLYVCGSGAFSPVCVYVNRgrrseeQVFHIDSKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  204 DGSALRTIKYDSKWIKEPHFL--HAIEYGNY-----VYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTS 276
Cdd:cd11251    160 KRNAVRTDQHNSKWLSEPIFVdaHLIPDGTDpndakLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGG-QRSLVNKWTT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  277 FLKARLNCSVPGD--SFFYFDVLQSITDIIQINGIPTVV-GVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSV 353
Cdd:cd11251    239 FLKARLVCSVMDEdgTETHFDELEDVFLLETDNPRTTLVyGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  354 WTAVpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPY 433
Cdd:cd11251    319 LIAY-QGRIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAAD 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  434 QNYTVIFVGSEAGVVLKVLAKTSPFSLNDSVLLEEIEAYnpakcsaesEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11251    398 GRYHVLFLGTDKGTVQKVVVLPTNGSLSGELILEELEVF---------KNHAPITNMKISSKKQQLYVSSEEGISQVSLH 468

                   ..
gi 1907137465  514 RC 515
Cdd:cd11251    469 RC 470
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
66-513 7.71e-89

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: 293.69  E-value: 7.71e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   66 RDTLYIAGRDQVYTVNLNEIPQTEvipsKKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDEMVFVCGTNAFNPM 144
Cdd:cd11259     29 KDVLYVGAREAVFALNALNISEKQ----HELYWKVSEDKRTKCAVKGKSKQtECRNYIRVLQPLNDTFLYVCGTNAFQPT 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  145 CRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDgSALRTiKYDSKWIKEPHFL 224
Cdd:cd11259    105 CDYLNLTSFRLLGKNEDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRNSSQ-SPLRT-EYAIPWLNEPSFV 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  225 HA--IEYG--------NYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPgDSFFYF 294
Cdd:cd11259    183 FAdvIRADpdspdgedDKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGG-LRTLQKKWTSFLKARLICSIP-DKNLVF 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  295 DVLQSITdIIQINGI--PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVF-KGRFKEQKTPDSVWTAVPE--DKVPKPRPGC 369
Cdd:cd11259    261 NVVNDVF-ILKSPTLkePVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFsKGKYMQSATVEQSHTKWVRynGEVPKPRPGA 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  370 CAKH-GLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYrlTAIEVDRSAGPYQN-YTVIFVGSEAGV 447
Cdd:cd11259    340 CINNeARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNY--TQIVVDRVQALDGTiYDVMFISTDRGA 417
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907137465  448 VLKVLAKTspfslNDSVLLEEIEAYnpakcsaESEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11259    418 LHKAISLE-----NEVHIIEETQLF-------PDFEPVQTLLLSSKKGRRFLYAGSNSGVVQSPLA 471
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
58-513 9.58e-86

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: 284.49  E-value: 9.58e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   58 DFQLMLKIRDT--LYIAGRDQVYTVNLNEIPQTEvipsKKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDEMVF 134
Cdd:cd11260      8 NYSTMLLREDLglLVLGAREAVFALDLNDISVKR----AKVLWEVTEEKQKDCTNKGKHADiDCHNYIRILHKMNDSRMY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  135 VCGTNAFNPMCRY--YRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSmgDGSALRTiK 212
Cdd:cd11260     84 VCGTNAFSPTCDYisYDDGQLTLEGKQEDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRS--SPITIRT-E 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  213 YDSKWIKEPHFLH--AIEYG--------NYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARL 282
Cdd:cd11260    161 FKSSWLNEPNFIYmaAVPESedspegddDKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGG-QRTLQKKWTSFLKARL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  283 NCSVPGDSFFYfdVLQSITDIIQINGIPTVV-GVFTTQLNSIPGSAVCAFSMDDIEKVF-KGRFKEQ---KTPDSVWTAV 357
Cdd:cd11260    240 DCSVPEPSLPY--VIQDVFHVCHQDWRKCVFyAVFTSQSDSSQSSAVCAYNVTDISNVFsRGKFKTPvavETSFVKWVMY 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  358 PEDkVPKPRPGCCA-KHGLAEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVryRLTAIEVDR-SAGPYQN 435
Cdd:cd11260    318 SGE-LPVPRPGACInNAARTSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGA--LFTRIVVDMvTAADGQS 394
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137465  436 YTVIFVGSEAGVVLKVLAKTSpfslnDSVLLEEIEAYNPakcsaesEEDRKVVSLQldkdHHALYVAFSSCVVRIPLS 513
Cdd:cd11260    395 YPVMFIGTANGYVLKAVNYDG-----EMHIIEEVQLFEP-------EEPIDILRLS----QNQLYAGSASGVVQMPVS 456
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
61-513 7.45e-84

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: 279.82  E-value: 7.45e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   61 LMLKIRDTLYIAGRDQVYTVNLNEIPQTEVipSKKLTWRSRQQDRENCAMKGKH-KDECHNFIKVFVPRNDEMVFVCGTN 139
Cdd:cd11257     14 LLSKDGNMLYVGARETLFALSSNDISPTGE--QQELTWSADEEKKQECSFKGKDpQRDCQNYIKILLRLNSTHLFTCGTY 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  140 AFNPMCRYYRLR--TLEYD--GEEI--SGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTiKY 213
Cdd:cd11257     92 AFSPICTYIVMTnfSLERDekGEPLleDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIYRSLGSGTPLKT-EN 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  214 DSKWIKEPHFL----------HAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLN 283
Cdd:cd11257    171 SLNWLQDPAFVgsayiqeslpKLVGDDDKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGG-ERVLQKRWTTFLKAQLL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  284 CSVPGDSfFYFDVLQsitDIIQINGIPT------VVGVFTTQLN--SIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWT 355
Cdd:cd11257    250 CSLPDDG-FPFNVLQ---DVFVLTPSPEdwkdtlFYGVFTSQWHkgTAGSSAVCVFTMDQVQRAFNGLYKEVNRETQQWY 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  356 AVPEdKVPKPRPGCC----AKHglaEAYKTSIDFPDDTLAFIKSHPLMDSavpPIADEPWFTKTRVRYrlTAIEVDRSAG 431
Cdd:cd11257    326 TYTH-PVPEPRPGACitnsARE---RKINSSLHMPDRVLNFVKDHFLMDG---QVRSQPLLLQPQVRY--TQIAVHRVKG 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  432 PYQNYTVIFVGSEAGVVLKVLaktspfSLNDSV-LLEEIEAYnpakcsaesEEDRKVVSLQLDKDHHALYVAFSSCVVRI 510
Cdd:cd11257    397 LHKTYDVLFLGTDDGRLHKAV------SVGPMVhIIEELQIF---------SEGQPVQNLLLDTHKGLLYASSHSGVVQV 461

                   ...
gi 1907137465  511 PLS 513
Cdd:cd11257    462 PVA 464
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
68-513 4.19e-76

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: 258.28  E-value: 4.19e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   68 TLYIAGRDQVYTVNLneiPQTEVIPsKKLTWRSRQQDRENCAMKGKHKDECHNFIKVFVPRNDEMVFVCGTNAFNPMCRY 147
Cdd:cd11261     25 TLYVGARDAIFALTL---PFSGERP-RRIDWMVPEAHRQNCRKKGKKEAECHNFIRILAIANASHLLTCGTFAFDPKCGV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  148 YRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLHAI 227
Cdd:cd11261    101 IDVSSFQQVERLESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAVGRAEEWIRTETLPSWLNAPAFVAAV 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  228 -----EYG-----NYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPgDSFFYFDVL 297
Cdd:cd11261    181 flspaEWGdedgdDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGG-RKTLQQRWTTFLKADLLCPGP-EHGRASSIL 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  298 QSITDIIQING--IPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPEDKVPKPRPGCCAKHGL 375
Cdd:cd11261    259 QDVTTLRPLPGagTPIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGLPVMDSDVPQPRPGECITNNM 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  376 A-EAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRY-RLTAIEVDRSAGpyQNYTVIFVGSEAGVVLKVLA 453
Cdd:cd11261    339 KlLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYlRVAAHRVTSLSG--KEYDVLYLGTEDGHLHRAVR 416
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907137465  454 KTSPFSlndsvLLEEIEAYnpakcsaesEEDRKVVSLQLdkdHHA-LYVAFSSCVVRIPLS 513
Cdd:cd11261    417 IGAQLS-----VLEDLALF---------PEPQPVENLQL---HHNwLLVGSDTEVTQINTS 460
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
52-513 1.12e-75

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: 256.76  E-value: 1.12e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   52 ESQHRLDFQLMLKIRDTLYIAGRDQVYTVNLneipQTEVIPSKK--LTWRSRQQDRENCAMKGK-HKDECHNFIKVFVPR 128
Cdd:cd11256      5 ENVHNYDQLLLSPDETTLYVGARDNILALGI----RTPGPIRLKhqIPWPANDSKISECAFKKKsNETECFNFIRVLVPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  129 NDEMVFVCGTNAFNPMCRYYRLR--TLEYDGEEI---SGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMG 203
Cdd:cd11256     81 NGTHLYTCGTYAFSPACTYIELDhfSLPPPNGTIitmDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  204 DGSALRTIKYdSKWIK-EPHFLHAI--EYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKA 280
Cdd:cd11256    161 TKVSLKTDGF-LRWLNaDAVFVASFnpQGDSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGG-EKLLQKKWTTFLKA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  281 RLNCSVPGDsfFYFDVLQSITDIIQ-INGIPTVVGVFTT--QLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTaV 357
Cdd:cd11256    239 QLTCSQQGH--FPFNVIHHVALLNQpDPNNSVFYAVFTSqwQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWT-R 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  358 PEDKVPKPRPGCCAKHGlaeayktsidFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYRLTAIEVDRSAGPYqNYT 437
Cdd:cd11256    316 YMGPVSDPRPGSCSGGK----------SSDKALNFMKDHFLMDEVVLPGAGRPLLVKSNVQYTRIAVDSVQGVSGH-NYT 384
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137465  438 VIFVGSEAGVVLKVLAktspfsLNDSV--LLEEIEAYNPakcsaeseeDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11256    385 VMFLGTDKGFLHKAVL------MGGSEshIIEEIELLTP---------PEPVENLLLAANEGVVYIGYSAGVWRVPLA 447
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
66-513 1.37e-73

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: 251.22  E-value: 1.37e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   66 RDTLYIAGRDQVYTVNLNEIPQTEvipSKKLTWRSRQQDRENCAMKGK-HKDECHNFIKVFVPRNDEMVFVCGTNAFNPM 144
Cdd:cd11262     19 SGRLYVGARGAIFSLNASDISDSS---ALTIDWEASPEQKHQCLKKGKnNQTECFNHVRFLQRFNSTHLYTCGTHAFRPL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  145 CRYYRLRTLEYDGEEISGLARCPFDARQTNVALFADGKLYSATVADFlASDAVIYRSMGDGSaLRTIKYDSKWIKEPHFL 224
Cdd:cd11262     96 CAYIDAERFTLSSQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQYEF-RSFPDIRRNSPQPT-LRTEEAPTRWLNDADFV 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  225 HAI--------EYG--NYVYFFFREIAVEHNN--LGKAVySRVARICKNDMGGsQRVLEKHWTSFLKARLNCSVPgDSFF 292
Cdd:cd11262    174 GSVlvresmnsSVGddDKIYFFFTERSQEETAyfSQSRV-ARVARVCKGDRGG-KKTLQRKWTSFLKARLVCYIP-EYEF 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  293 YFDVLQSITDIIQINGIPTVV-GVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVpEDKVPKPRPGCCA 371
Cdd:cd11262    251 LFNVLRSVFVLWGSTPQDTVFyGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRY-TGKVPEPRPGSCI 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  372 KHGL-AEAYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYrlTAIEVDRSAGPYQN-YTVIFVGSEAGVVL 449
Cdd:cd11262    330 TDEHrSQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIY--TKIAVQTVRGLDGRvYDVLFLGTDEGWLH 407
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907137465  450 KvlaktsPFSLNDSV-LLEEIEAYnpakcsaesEEDRKVVSLQLDKDHHALYVAFSSCVVRIPLS 513
Cdd:cd11262    408 K------AVVIGSAVhIIEELQVF---------REPQPVENLVISKKQNSLYVGARSGVVQVPLS 457
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
66-473 9.09e-73

The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a Plexin B2 ligand to regulate the development of cerebellar granule cells and to modulate ureteric branching in the developing kidney. The binding of Sema4C to Plexin B2 results the phosphorylation of downstream regulator ErbB-2 and the plexin protein itself. The cytoplasmic region of Sema4C binds a neurite-outgrowth-related protein SFAP75, suggesting that Sema4C may also play a role in neural function. Sema4C belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200519 [Multi-domain]  Cd Length: 458  Bit Score: 248.95  E-value: 9.09e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   66 RDTLYIAGRDQVYTVNLNEIpqtEVIPSkkLTWRSRQQDRENCAMKGK-HKDECHNFIKVFVPRNDEMVFVCGTNAFNPM 144
Cdd:cd11258     21 RGLLYVGAREAIFALSLSNI---ELQPP--ISWEAPAEKKTECAQKGKsNQTECFNYIRFLQPYNQSHLYTCGTYAFQPK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  145 CRYYRLRTLEYDGEEIS-GLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSALRTiKYDSKWIKEPHF 223
Cdd:cd11258     96 CAYINMLTFTLDRAEFEdGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMKT-EYLAFWLNEPHF 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  224 L---HAIEYGNY-------VYFFFREIAVEHNNLGKAVYSRVARICKNDMGGSqRVLEKHWTSFLKARLNCSVPgDSFFY 293
Cdd:cd11258    175 VgsaFVPESVGSftgdddkIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGA-RTLQKKWTTFLKARLLCSIP-EWQLY 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  294 FDVLQSitdIIQINGI----PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPeDKVPKPRPGC 369
Cdd:cd11258    253 FNQLKA---VFTLEGAswrnTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYT-DPVPSPRPGS 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  370 CAKHGLAE-AYKTSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKtrVRYRLTAIEVDRSAG-PYQNYTVIFVGSEAGV 447
Cdd:cd11258    329 CINNWHRDhGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVP--CNSNFTHVVWTRVLGlDGETYSVLFIGTLDGW 406
                          410       420
                   ....*....|....*....|....*..
gi 1907137465  448 VLKVLaktspfSLNDSV-LLEEIEAYN 473
Cdd:cd11258    407 LIKAV------SLGSWVhMIEELQVFD 427
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
297-474 1.68e-52

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: 181.70  E-value: 1.68e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  297 LQSITDIIQINGIP--TVV-GVFTTQL-NSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVPeDKVPKPRPGCCAK 372
Cdd:pfam01403    1 LQDVFVLKPGAGDAldTVLyGVFTTQWsNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYT-GKVPYPRPGTCIN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  373 HGLaeayktSIDFPDDTLAFIKSHPLMDSAVPPIADEPWFTKTRVRYrlTAIEVDRSAGPYQNYTVIFVGSEAGVVLKVL 452
Cdd:pfam01403   80 DPL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGVRL--TSIAVDRVQALDGNYTVLFLGTDDGRLHKVV 151
                          170       180
                   ....*....|....*....|..
gi 1907137465  453 AKTSpfslNDSVLLEEIEAYNP 474
Cdd:pfam01403  152 LVGS----EESHIIEEIQVFPE 169
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
67-512 6.77e-41

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: 156.16  E-value: 6.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   67 DTLYIAGRDQVYTVNLneiPQTEVIpSKKLTWRSRQQDRENCAMKgkhkDECHNFIKVfVPRNDEMVFVCGTNAFNPMCR 146
Cdd:cd11243     14 SSVYVGGQGALYLLDF---TGSAVI-VKKIPDEKTEKDCKKRATL----DDCENYITL-IKKLDYRLLVCGTNAGSPKCW 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  147 YYRLRTLEYDGEEiSGLArcPFDARQTNVALFADGKLYSATVADflASDAVIYRSMGDGSALRTikyDSKWIKEPHFLHA 226
Cdd:cd11243     85 FLVNQTLVTLSAD-RGVA--PFLPDENSLVLIEGNNVYSTISGK--KGNIPRFRRYGGKKELYT---SDTVMQKPQFVKA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  227 I------EYGNYVYFFFREIAvEHNNLGKAVY-SRVARICKNDMGGSQRVLEKHWTSFLKARLNCSVPGDSfFYFDVLQS 299
Cdd:cd11243    157 TllpedeQYQDKIYYFFREDN-EDKGPEAEPNiSRVARLCKEDQGGTSSLSTSKWSTFLKARLVCGDPATP-MNFNRLQD 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  300 ITDIIQINGIPTVV-GVFTTQLNSipgSAVCAFSMDDIEKVFKgrfkeqktPDSVWTAvpEDKVPKPRPGCCAKHGLAEa 378
Cdd:cd11243    235 VFLLPKEEWREAVVyGVFSNTWGS---SAVCSYSLGDIDKVFR--------TSSLKGY--SGSLPNPRPGTCVPPEQTH- 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  379 yktsidfPDDTLAFIKSHPLMDSAVPPiaDEPwfTKTRV---RYRLTAIEVDR-SAGPYQNYTVIFVGSEAGVVLKVLAk 454
Cdd:cd11243    301 -------PSETFSFADEHPELDDRIEP--DEP--RKLPVfqnKDHYQKVVVDEvRASDGVSYDVLYLATDKGKIHKVVE- 368
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137465  455 tspfSLNDSVLLEEIEAYNPAKcsaeseedrKVVSLQLDKDHHALYVAFSSCVVRIPL 512
Cdd:cd11243    369 ----SKGQTHNIMEIQPFKEQE---------PIQSMILDAERSHLYVGTKAEVTRLPL 413
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
195-511 3.21e-15

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: 79.44  E-value: 3.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  195 DAVIYRSMGDGSALRTiKYDSKWIKEphFLHAIEYGNYVYFFFREiavehnNLGKAVYSR--VARICKNDmggsqrvleK 272
Cdd:cd11276    167 DREVFENYIDAATVKS-AYVSRYTQQ--FRYAFEDNNYVYFLFNQ------QLGHPDKNRtlIARLCEND---------H 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  273 HWTSFLKARLNCSVPGDSF-----FYF-----DVLQSITDIIQINGIptVVGVFTTQLNSIPGSAVCAFSMDDIEKvfkg 342
Cdd:cd11276    229 HYYSYTEMDLNCRDGANAYnkcqaAYVstpgkELAQNYGNSILSDKV--LFAVFSRDEKDSGESALCMFPLKSINA---- 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  343 rfKEQKTPDSVWTAVPEDK--VPKP----RPGCCAKH--GLAEAYKTSIDFPDDTLAfikSHPLMDSAVPPIadepwftk 414
Cdd:cd11276    303 --KMEANREACYTGTIDDRdvFYKPfhsqKDIICGSHqqKNSKSFPCGSEHLPYPLG---SRDELALTAPVL-------- 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  415 TRVRYRLTAIEVDRSagpyQNYTVIFVGSEAGVVLKVLAKTSPfslndsvlleeiEAYNPAkcsaeSEEDRKVVS--LQL 492
Cdd:cd11276    370 QRGGLNLTAVTVAVE----NGHTVAFLGTSDGRILKVHLSPDP------------EEYNSI-----LIEKNKPVNkdLVL 428
                          330
                   ....*....|....*....
gi 1907137465  493 DKDHHALYVAFSSCVVRIP 511
Cdd:cd11276    429 DKTLEHLYIMTEDKVFRLP 447
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
64-513 6.15e-12

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


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 68.90  E-value: 6.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465   64 KIRDTLYIAGRDQVYTVNLNEIPQTEVI--PskkltwrsrQQDRENCAMKG-----KHKDECHNFIKVFVP-RNDEMVFV 135
Cdd:cd11236      9 NSTGRVYVGAVNRLYQLDSSLLLEAEVStgP---------VLDSPLCLPPGccscdHPRSPTDNYNKILLIdYSSGRLIT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  136 CGTnAFNPMCRYYRLRTLEYDGEEISgLARCPFDARQTNVALFADG------KLYSATVADFLASD----AVIYRSM--- 202
Cdd:cd11236     80 CGS-LYQGVCQLRNLSNISVVVERSS-TPVAANDPNASTVGFVGPGpynnenVLYVGATYTNNGYRdyrpAVSSRSLppd 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  203 -----GDGSALRTIKYDSKWIKE--PHFLHAIEYGNYVYFFFREiaVEHNNLGKAVYSRVARICKNDmggsqrvleKHWT 275
Cdd:cd11236    158 ddfnaGSLTGGSAISIDDEYRDRysIKYVYGFSSGGFSYFVTVQ--RKSVDDESPYISRLVRVCQSD---------SNYY 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  276 SFLKARLNCSVPGDSFFyfDVLQSI------TDIIQINGIPT----VVGVFTTQLNS--IPG--SAVCAFSMDDIEKvfk 341
Cdd:cd11236    227 SYTEVPLQCTGGDGTNY--NLLQAAyvgkagSDLARSLGISTdddvLFGVFSKSKGPsaEPSskSALCVFSMKDIEA--- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  342 grfkeqktpdsvwtavpedkvpkprpgccakhglaeayktsidfpddtlAFIKSHPLmdSAVPPIADEPWFTKTrvryRL 421
Cdd:cd11236    302 -------------------------------------------------AFNDNCPL--GGGVPITTSAVLSDS----LL 326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  422 TAIEVDRsagpYQNYTVIFVGSEAGVVLKVLAKTSpfslndsvlleeieaynpakCSAESEEDRKVVS-------LQLDK 494
Cdd:cd11236    327 TSVAVTT----TRNHTVAFLGTSDGQLKKVVLESS--------------------SSATQYETLLVDSgspilpdMVFDP 382
                          490
                   ....*....|....*....
gi 1907137465  495 DHHALYVAFSSCVVRIPLS 513
Cdd:cd11236    383 DGEHLYVMTPKKVTKVPVE 401
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
221-543 9.28e-11

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: 65.72  E-value: 9.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  221 PHF----LHAIEYGNYVYFFFREI----AVEHNNLGKAVY-SRVARICKNDmggsqrvleKHWTSFLKARLNCSVPGDSF 291
Cdd:cd11272    200 SHFdifyIYGFASGNFVYFLTVQPetpeGVSINSAGDLFYtSRIVRLCKDD---------PKFHSYVSLPFGCVRGGVEY 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  292 FYF---------DVLQSITDIIQINGIptVVGVFTT---QLNSIPG-SAVCAFSMDDIEKVFKGR----FKEQKTPDSVW 354
Cdd:cd11272    271 RLLqaaylskpgEVLARSLNITAQEDV--LFAIFSKgqkQYHHPPDdSALCAFPIRAINAQIKERlqscYQGEGNLELNW 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  355 ---TAVPEDKVPKPrpgccakhglaeayktsIDfpDDTLAFIKSHPLMDSAvpPIADEPWFTKTRvrYRLTAIevdrSAG 431
Cdd:cd11272    349 llgKDVQCTKAPVP-----------------ID--DNFCGLDINQPLGGST--PVEGVTLYTSSR--DRLTSV----ASY 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  432 PYQNYTVIFVGSEAGVVLKVLAKTSPfslNDSVLLEEIEAYNpakcsaesEEDRKVVSLQLDKDHHALYVAFSSCVVRIP 511
Cdd:cd11272    402 VYNGYSVVFVGTKSGKLKKIRADGPP---HGGVQYEMVSVFK--------DGSPILRDMAFSIDHKYLYVMSERQVSRVP 470
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1907137465  512 LSRCERYGSCKKsCIASRDPYCGWLS-QGVCER 543
Cdd:cd11272    471 VESCEQYTTCGE-CLSSGDPHCGWCAlHNMCSR 502
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
514-543 1.30e-07

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: 49.24  E-value: 1.30e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907137465  514 RCERYGSCKkSCIASRDPYCGWLS-QGVCER 543
Cdd:pfam01437    1 RCSQYTSCS-SCLAARDPYCGWCSsEGRCVR 30
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
222-451 3.42e-05

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


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 47.62  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  222 HFLHAIEYGNYVYFFFREIAVEHNnlgKAVYSRVARICKNDmggsqrvleKHWTSFLKARLNCSVPGDSFFyfDVLQSI- 300
Cdd:cd11245    185 DFVYAFADNGYIYFLFSRRPGTAD---STKRTYISRLCEND---------HHYYSYVELPLNCTVNQENTY--NLVQAAy 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  301 --TDIIQINGiPTVVGVFTTQLNSIPG----SAVCAFSMDDIEKVFkgrfkeQKTPDSVWT-AVPEDKVPKprpgccakh 373
Cdd:cd11245    251 laKPGKVLNG-KVLFGVFSADEASTAApdgrSALCMYPLSSVDARF------ERTRESCYTgEGLEDDKPE--------- 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  374 glaEAY----KTSI--DFPDDTLafiKSHPLMDSAVP-PIADEPWFTKTRVRYR---LTAIEVDRSAGpyqnYTVIFVGS 443
Cdd:cd11245    315 ---TAYieynVKSIckTLPDKNV---KAYPCGAEHTPsPLASRYPLAAKPILTRndmLTAVAVAVENG----HTIAFLGD 384

                   ....*...
gi 1907137465  444 EAGVVLKV 451
Cdd:cd11245    385 SGGQLHKV 392
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
514-541 3.77e-05

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 42.15  E-value: 3.77e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907137465   514 RCERYGSCKkSCIASRDPYCGW-LSQGVC 541
Cdd:smart00423    1 RCSKYTSCS-ECLLARDPYCAWcSSQGRC 28
PHA03247 PHA03247
large tegument protein UL36; Provisional
899-1046 2.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137465  899 LDPVGPMAEVPPKVPNREASLYSPPSTLPRNSPTKRVDVPTTPGVPMTslerqRGYHKNSSQRHSISAVPKNLNSPNGVL 978
Cdd:PHA03247  2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT-----RPAVASLSESRESLPSPWDPADPPAAV 2811
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907137465  979 LSRQPSMNR----GGYMPTPTGAKVdyIQGTPVSVHLQPSLSRQSSYTSNGTLPRTGLKRTPSLKPDVPPKP 1046
Cdd:PHA03247  2812 LAPAAALPPaaspAGPLPPPTSAQP--TAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP 2881
 
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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