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Conserved domains on  [gi|31543681|ref|NP_033178|]
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semaphorin-3A precursor [Mus musculus]

Protein Classification

semaphorin-3( domain architecture ID 10181338)

semaphorin-3 is a class III semaphorin that is secreted and contains a Sema domain, an Ig domain, and a short basic domain; may function as an axonal guidance cue and may have a role in the regulation of the cardiovascular, immune, and respiratory systems

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
26-518 0e+00

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: 1161.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  26 KNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKW 105
Cdd:cd11249   1 KNNVPRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 106 AGKDILKECANFIKVLEAYNQTHLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGE 185
Cdd:cd11249  81 AGKDILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEDNIFRLEDSHFENGRGKSPYDPKLLTASLLIDGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 186 LYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARI 265
Cdd:cd11249 161 LYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTGKATHARI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 266 GQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSM 345
Cdd:cd11249 241 GQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMYSM 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 346 SDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKT 425
Cdd:cd11249 321 TDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKT 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 426 DVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSVPKETWHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGS 505
Cdd:cd11249 401 DVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETWHDLEEVLLEEMTVFREPTAISAMELSTKQQQLYIGS 480
                       490
                ....*....|...
gi 31543681 506 TAGVAQLPLHRCD 518
Cdd:cd11249 481 AIGVSQLPLHRCD 493
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
580-671 5.70e-45

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


:

Pssm-ID: 409455  Cd Length: 92  Bit Score: 155.97  E-value: 5.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 580 SLEERIIYGVENSSTFLECSPKSQRALVYWQFQRRNEDRKEEIRMGDHIIRTEQGLLLRSLQKKDSGNYLCHAVEHGFMQ 659
Cdd:cd05871   1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                        90
                ....*....|..
gi 31543681 660 TLLKVTLEVIDT 671
Cdd:cd05871  81 TLVKIRLHVIEP 92
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
516-552 7.52e-07

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 46.38  E-value: 7.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 31543681    516 RCDIYgKACAECCLARDPYCAWD--GSSCSRYFPTAKRR 552
Cdd:smart00423   1 RCSKY-TSCSECLLARDPYCAWCssQGRCTSGERCDSRR 38
 
Name Accession Description Interval E-value
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
26-518 0e+00

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: 1161.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  26 KNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKW 105
Cdd:cd11249   1 KNNVPRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 106 AGKDILKECANFIKVLEAYNQTHLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGE 185
Cdd:cd11249  81 AGKDILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEDNIFRLEDSHFENGRGKSPYDPKLLTASLLIDGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 186 LYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARI 265
Cdd:cd11249 161 LYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTGKATHARI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 266 GQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSM 345
Cdd:cd11249 241 GQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMYSM 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 346 SDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKT 425
Cdd:cd11249 321 TDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKT 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 426 DVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSVPKETWHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGS 505
Cdd:cd11249 401 DVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETWHDLEEVLLEEMTVFREPTAISAMELSTKQQQLYIGS 480
                       490
                ....*....|...
gi 31543681 506 TAGVAQLPLHRCD 518
Cdd:cd11249 481 AIGVSQLPLHRCD 493
Sema smart00630
semaphorin domain;
57-490 7.45e-172

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 499.59  E-value: 7.45e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681     57 YHTFLLDEERSRLYVGAKDHIFSFNLVNIKD-FQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACGTG 135
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEaELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    136 AFHPICTYIEVGhhpednifklqdshfengrgkspydpklltasllidgELYSGTAADFMGRDFAIFRTLGHHH------ 209
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRlkgtsg 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    210 -PIRTEQHDSRWLNDPRFISAHLIpesdnpeDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLK 288
Cdd:smart00630 124 vSLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLK 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    289 ARLICSVPGPngIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVP 368
Cdd:smart00630 197 ARLECSVPGE--DPFYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    369 Y-QGRVPYPRPGTCPSKTFggfdSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVdAEDGQYD 447
Cdd:smart00630 275 YsRGKVPYPRPGTCPNKPP----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNYT 349
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 31543681    448 VMFIGTDVGTVLKVVSVPKETWHdlEEVLLEEMTVFREPTTIS 490
Cdd:smart00630 350 VLFLGTSDGRILKVVLSESSSSS--ESVVLEEISVFPDGSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
308-495 3.21e-81

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: 257.20  E-value: 3.21e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681   308 LQDVFLMN--SKDPKNPIVYGVFTTS-SNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSK 384
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681   385 TFGgfdstKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTdvNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSV 464
Cdd:pfam01403  81 PLR-----LDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRT--GVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLV 153
                         170       180       190
                  ....*....|....*....|....*....|.
gi 31543681   465 PKEtwhdlEEVLLEEMTVFREPTTISAMELS 495
Cdd:pfam01403 154 GSE-----ESHIIEEIQVFPEPQPVLNLLLS 179
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
580-671 5.70e-45

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 155.97  E-value: 5.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 580 SLEERIIYGVENSSTFLECSPKSQRALVYWQFQRRNEDRKEEIRMGDHIIRTEQGLLLRSLQKKDSGNYLCHAVEHGFMQ 659
Cdd:cd05871   1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                        90
                ....*....|..
gi 31543681 660 TLLKVTLEVIDT 671
Cdd:cd05871  81 TLVKIRLHVIEP 92
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
516-552 7.52e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 46.38  E-value: 7.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 31543681    516 RCDIYgKACAECCLARDPYCAWD--GSSCSRYFPTAKRR 552
Cdd:smart00423   1 RCSKY-TSCSECLLARDPYCAWCssQGRCTSGERCDSRR 38
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
586-664 6.85e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 36.33  E-value: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    586 IYGVENSSTFLECSPKSQR-ALVYWQFQRrnedrKEEIRMGDHIIRTEQG----LLLRSLQKKDSGNYLCHAV-EHG--F 657
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPpPEVTWYKQG-----GKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATnSSGsaS 78

                   ....*..
gi 31543681    658 MQTLLKV 664
Cdd:smart00410  79 SGTTLTV 85
 
Name Accession Description Interval E-value
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
26-518 0e+00

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: 1161.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  26 KNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKW 105
Cdd:cd11249   1 KNNVPRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIVWPVSPSRRDECKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 106 AGKDILKECANFIKVLEAYNQTHLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGE 185
Cdd:cd11249  81 AGKDILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEDNIFRLEDSHFENGRGKSPYDPKLLTASLLIDGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 186 LYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARI 265
Cdd:cd11249 161 LYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTGKATHARI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 266 GQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSM 345
Cdd:cd11249 241 GQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMYSM 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 346 SDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKT 425
Cdd:cd11249 321 TDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKT 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 426 DVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSVPKETWHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGS 505
Cdd:cd11249 401 DVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETWHDLEEVLLEEMTVFREPTAISAMELSTKQQQLYIGS 480
                       490
                ....*....|...
gi 31543681 506 TAGVAQLPLHRCD 518
Cdd:cd11249 481 AIGVSQLPLHRCD 493
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
48-517 0e+00

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: 951.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  48 FNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNI-KDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQ 126
Cdd:cd11239   1 FLGSMNSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNInQDPKKIYWPASPERIEECKMAGKDPNTECANFVRVLQPYNR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 127 THLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLG 206
Cdd:cd11239  81 THLYACGTGAFHPICAFINVGRRLEDPIFKLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 207 HHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTF 286
Cdd:cd11239 161 HRHYIRTEQYDSRWLNEPKFVGAYLIPDSDNPDDDKVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGGQRSLVNKWSTF 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 287 LKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQW 366
Cdd:cd11239 241 LKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQW 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 367 VPYQGRVPYPRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQ 445
Cdd:cd11239 321 VEYQGKVPYPRPGTCPSKTYGpLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPYRLTQIAVDRVEAEDGQ 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543681 446 YDVMFIGTDVGTVLKVVSVPKETWhDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRC 517
Cdd:cd11239 401 YDVLFIGTDSGTVLKVVSLPKENW-EMEEVILEELQVFKHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
51-517 0e+00

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: 777.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  51 LANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNI-KDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHL 129
Cdd:cd11250   4 LERSCCYDALLLDEERGRLFVGAKNYLASLSLDNIsKQEKKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 130 YACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHH 209
Cdd:cd11250  84 YACGTGAFHPTCAFVEVGQRMEDHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 210 PIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKA 289
Cdd:cd11250 164 SLRTEQHDSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 290 RLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPY 369
Cdd:cd11250 244 RLVCSVPGNEGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSY 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 370 QGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVM 449
Cdd:cd11250 324 QGKVPYPRPGMCPSKTFGSFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPYTFTQIAVDRVAAADGHYDVM 403
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543681 450 FIGTDVGTVLKVVSVPKETWHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRC 517
Cdd:cd11250 404 FIGTDVGSVLKVISVPKGSWPSNEELLLEELHVFKDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
48-517 0e+00

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: 695.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  48 FNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIV-WPVSYTRRDECKWAGKDILKECANFIKVLEAYNQ 126
Cdd:cd11254   1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIhWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 127 THLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLG 206
Cdd:cd11254  81 THLYVCGTGAYNPVCAYINRGRRAEDYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 207 HHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHsGKATHARIGQICKNDFGGHRSLVNKWTTF 286
Cdd:cd11254 161 KQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQ-SPAVLSRIGRVCLNDDGGHCCLVNKWSTF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 287 LKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQW 366
Cdd:cd11254 240 LKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQW 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 367 VPYQGRVPYPRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQ 445
Cdd:cd11254 320 MPYTGKIPYPRPGTCPGGTFTpSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGR 399
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543681 446 YDVMFIGTDVGTVLKVVSVPKETwHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRC 517
Cdd:cd11254 400 YEVLFLGTDRGTVQKVIVLPKDD-LETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
48-517 0e+00

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: 689.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  48 FNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNI-KDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQ 126
Cdd:cd11252   1 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIYLLDLVDLnKNPKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 127 THLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLG 206
Cdd:cd11252  81 THVYVCGTGAFHPTCGYIELGTHKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 207 ---HHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKW 283
Cdd:cd11252 161 ptpDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKW 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 284 TTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPN 363
Cdd:cd11252 241 TTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPD 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 364 YQWVPYQGRVPYPRPGTCPSKTFGG-FDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAE 442
Cdd:cd11252 321 HRWVQYEGRIPYPRPGTCPSKTYDPlIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVAAE 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543681 443 DGQYDVMFIGTDVGTVLKVVSVPKETWhDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRC 517
Cdd:cd11252 401 DGQYDVMFLGTDIGTVLKVVSITKEKW-TMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
55-515 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: 679.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  55 SSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDIlKECANFIKVLEAYNQTHLYACGT 134
Cdd:cd11235   1 LKYHTKLLHEDRSTLYVGARDRVYLVDLDSLYTEQKVAWPSSPDDVDTCYLKGKSK-DDCRNFIKVLEKNSDDSLLVCGT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 135 GAFHPICTYIEVGHHPEDnifklqdSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTE 214
Cdd:cd11235  80 NAFNPSCRNYNVETFELV-------GKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 215 QHDSRWLNDPRFISAHLIPesdnpedDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICS 294
Cdd:cd11235 153 YHDSKWLNEPQFVGAFDIG-------DYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCS 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 295 VPGpnGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQG-RV 373
Cdd:cd11235 226 VPG--EFPFYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDeRV 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 374 PYPRPGTCpsktfggFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQ-YDVMFIG 452
Cdd:cd11235 304 PEPRPGTC-------VDDSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDVNYRFTKIAVDRVQAKLGQtYDVLFVG 376
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543681 453 TDVGTVLKVVSVPKETwhDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLH 515
Cdd:cd11235 377 TDRGIILKVVSLPEQG--LQASNILEEMPVGPPPEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
48-517 0e+00

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: 635.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  48 FNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNI-KDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQ 126
Cdd:cd11255   1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQThPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 127 THLYACGTGAFHPICTYIEVGHHPEdNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLG 206
Cdd:cd11255  81 THLLACGTGAFQPVCALINVGHRGE-HVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 207 HHHPIRTEQhDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEH-SGKATHARIGQICKNDFGGHRSLVNKWTT 285
Cdd:cd11255 160 TRSPLRTET-DQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETAEdDDGAIHSRVGRLCANDAGGQRVLVNKWST 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 286 FLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQ 365
Cdd:cd11255 239 FIKARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQ 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 366 WVPYQGRVPYPRPGTCPSKTFG----GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDA 441
Cdd:cd11255 319 WGPYEGKVPYPRPGVCPSKITAqpgrAFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEA 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543681 442 EDGQYDVMFIGTDVGTVLKVVSVPKETWHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRC 517
Cdd:cd11255 399 EDGYYDVMFIGTDSGSVLKVIVLQKGNSAAGEEVTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
58-517 0e+00

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: 615.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  58 HTFLLDEERSRLYVGAKDHIFSFNLVNIKD-FQKIVWPVSYTRRDECKWAGKDIlKECANFIKVLEAYNQTHLYACGTGA 136
Cdd:cd11253  11 HTMLLDEYQERLFVGGRDLLYSLSLERISAnYKEIHWPSTQLQVEDCIMKGRDK-PECANYIRVLHHYNRTHLLACGTGA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 137 FHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQH 216
Cdd:cd11253  90 FDPVCAFIRVGRGSEDHLFQLESDKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMNHLAHIRTEHD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 217 DSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVP 296
Cdd:cd11253 170 DERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLICSVP 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 297 GPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPYP 376
Cdd:cd11253 250 GPNGIDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVYEGKVPYP 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 377 RPGTCPSKTFGG-FDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTDV 455
Cdd:cd11253 330 RPGSCASKVNGGhYGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNLKQIAVDRVEAEDGQYDVLFIGTDN 409
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543681 456 GTVLKVVSVPKETWHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRC 517
Cdd:cd11253 410 GIVLKVITIYNQETETMEEVILEELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
57-517 0e+00

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: 607.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  57 YHTFLLDEERSRLYVGAKDHIFSFNLVNI-KDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACGTG 135
Cdd:cd11251  10 YRILFMDEDQDRIYVGSKDHILSLNINNIsQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNRTHLYVCGSG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 136 AFHPICTYIEVGHHPEDNIFKLqDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQ 215
Cdd:cd11251  90 AFSPVCVYVNRGRRSEEQVFHI-DSKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQ 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 216 HDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSV 295
Cdd:cd11251 169 HNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFLKARLVCSV 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 296 PGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPY 375
Cdd:cd11251 249 MDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQGRIPY 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 376 PRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTD 454
Cdd:cd11251 329 PRPGTCPGGAFTpNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGRYHVLFLGTD 408
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543681 455 VGTVLKVVSVPKETWHDlEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRC 517
Cdd:cd11251 409 KGTVQKVVVLPTNGSLS-GELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema smart00630
semaphorin domain;
57-490 7.45e-172

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 499.59  E-value: 7.45e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681     57 YHTFLLDEERSRLYVGAKDHIFSFNLVNIKD-FQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACGTG 135
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEaELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    136 AFHPICTYIEVGhhpednifklqdshfengrgkspydpklltasllidgELYSGTAADFMGRDFAIFRTLGHHH------ 209
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRlkgtsg 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    210 -PIRTEQHDSRWLNDPRFISAHLIpesdnpeDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLK 288
Cdd:smart00630 124 vSLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLK 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    289 ARLICSVPGPngIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVP 368
Cdd:smart00630 197 ARLECSVPGE--DPFYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    369 Y-QGRVPYPRPGTCPSKTFggfdSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVdAEDGQYD 447
Cdd:smart00630 275 YsRGKVPYPRPGTCPNKPP----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNYT 349
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 31543681    448 VMFIGTDVGTVLKVVSVPKETWHdlEEVLLEEMTVFREPTTIS 490
Cdd:smart00630 350 VLFLGTSDGRILKVVLSESSSSS--ESVVLEEISVFPDGSPIS 390
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
54-514 7.72e-161

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: 473.82  E-value: 7.72e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  54 SSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQK--IVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYA 131
Cdd:cd11240   6 IQNYSTLLLSEDEGTLYVGAREALFALNVSDISTELKdkIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYNSTHLYV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 132 CGTGAFHPICTYIEVghhpEDniFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPI 211
Cdd:cd11240  86 CGTFAFSPRCTYINL----SD--FSLSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEGNVL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 212 RTEqHDSRWLNDPRFISAHLIPESDNP---EDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLK 288
Cdd:cd11240 160 KTE-NTLRWLNEPAFVGSAHIRESIDSpdgDDDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGGQRTLQKKWTTFLK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 289 ARLICSVPGPngiDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVP 368
Cdd:cd11240 239 AQLVCSQPDS---GLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSR 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 369 YQGRVPYPRPGTC--PSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPInNRPIMIKTDVNYqfTQIVVDRVDAEDGQ- 445
Cdd:cd11240 316 YTGPVPDPRPGACitNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPI-NRPLLVKSGVNY--TRIAVHRVQALDGQt 392
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543681 446 YDVMFIGTDVGTVLKVVSVPKETwhdleeVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11240 393 YTVLFLGTEDGFLHKAVSLDGGM------HIIEEIQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
53-514 2.01e-141

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: 424.17  E-value: 2.01e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  53 NSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDF--QKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLY 130
Cdd:cd11262   6 PAQNYSTLLLEDESGRLYVGARGAIFSLNASDISDSsaLTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRFNSTHLY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 131 ACGTGAFHPICTYIEVghhpedNIFKLQdSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFmgRDFAIFRTLGHHHP 210
Cdd:cd11262  86 TCGTHAFRPLCAYIDA------ERFTLS-SQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQYEF--RSFPDIRRNSPQPT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 211 IRTEQHDSRWLNDPRFISAHLIPESDNPE---DDKVYFFFRENAidGEHSGKATH---ARIGQICKNDFGGHRSLVNKWT 284
Cdd:cd11262 157 LRTEEAPTRWLNDADFVGSVLVRESMNSSvgdDDKIYFFFTERS--QEETAYFSQsrvARVARVCKGDRGGKKTLQRKWT 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 285 TFLKARLICSVPGpngIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNY 364
Cdd:cd11262 235 SFLKARLVCYIPE---YEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSS 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 365 QWVPYQGRVPYPRPGTCPSKTF--GGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYqfTQIVVDRVDAE 442
Cdd:cd11262 312 KWSRYTGKVPEPRPGSCITDEHrsQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIY--TKIAVQTVRGL 389
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543681 443 DGQ-YDVMFIGTDVGTVLKVVSVPKETwHdleevLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11262 390 DGRvYDVLFLGTDEGWLHKAVVIGSAV-H-----IIEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
55-514 1.10e-126

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: 386.52  E-value: 1.10e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  55 SSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQ-KIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACG 133
Cdd:cd11259  18 SNYSTLLLSEDKDVLYVGAREAVFALNALNISEKQhELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLNDTFLYVCG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 134 TGAFHPICTYIEVGHhpedniFKLQDSHfENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLgHHHPIRT 213
Cdd:cd11259  98 TNAFQPTCDYLNLTS------FRLLGKN-EDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRNS-SQSPLRT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 214 EqHDSRWLNDPRFISAHLI---PESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKAR 290
Cdd:cd11259 170 E-YAIPWLNEPSFVFADVIradPDSPDGEDDKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKAR 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 291 LICSVPGPNGIdthFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFL-GPYAHR---DGPNYQW 366
Cdd:cd11259 249 LICSIPDKNLV---FNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHTKW 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 367 VPYQGRVPYPRPGTCPSKTF--GGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYqfTQIVVDRVDAEDG 444
Cdd:cd11259 326 VRYNGEVPKPRPGACINNEAraANYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNY--TQIVVDRVQALDG 403
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543681 445 Q-YDVMFIGTDVGTVLKVVSVPKETwHDLEEVLLeemtvFREPTTISAMELSTKQQQ--LYIGSTAGVAQLPL 514
Cdd:cd11259 404 TiYDVMFISTDRGALHKAISLENEV-HIIEETQL-----FPDFEPVQTLLLSSKKGRrfLYAGSNSGVVQSPL 470
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
53-517 2.52e-121

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: 371.66  E-value: 2.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  53 NSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDILkECANFIKVLEAYNQTHLYAC 132
Cdd:cd11237   1 ETHSDHFKLLDQDGNSLLVGARNAVYNISLSDLTENQRIEWPSSDAHREMCLLKGKSED-DCQNYIRVLAKKSAGRLLVC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 133 GTGAFHPICTYIEVghhPEDNIFKLQDShfeNGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRtlghhHPIR 212
Cdd:cd11237  80 GTNAYKPLCREYTV---KDGGYRVEREF---DGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYR-----EPLR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 213 TEQHDSRWLNDPRFISAHlipesdnPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLI 292
Cdd:cd11237 149 TERYDLKQLNAPNFVSSF-------AYGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLN 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 293 CSVPGpngiDT--HFDELQ---DVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWV 367
Cdd:cd11237 222 CSVPG----EYpfYFNEIQstsDIVEGGYGGKSAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWL 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 368 PYQG-RVPYPRPGTCPSktfggfDSTKdLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVD-RVDAEDGQ 445
Cdd:cd11237 298 PVPSnKVPEPRPGQCVN------DSRT-LPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQYRFTQIAVDpQVKALDGK 370
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543681 446 -YDVMFIGTDVGTVLKVVSVPKETWHD-LEEVLLEEMTVFREPTTISAMELSTKQQQ--LYIGSTAGVAQLPLHRC 517
Cdd:cd11237 371 yYDVLFIGTDDGKVLKAVNIASADTVDkVSPVVIEETQVFPRGVPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
55-514 1.08e-119

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: 367.98  E-value: 1.08e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  55 SSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACGT 134
Cdd:cd11258  10 SNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPISWEAPAEKKTECAQKGKSNQTECFNYIRFLQPYNQSHLYTCGT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 135 GAFHPICTYIEVGHhpedniFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTE 214
Cdd:cd11258  90 YAFQPKCAYINMLT------FTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMKTE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 215 qHDSRWLNDPRFISAHLIPE---SDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARL 291
Cdd:cd11258 164 -YLAFWLNEPHFVGSAFVPEsvgSFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTFLKARL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 292 ICSVPgpnGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQG 371
Cdd:cd11258 243 LCSIP---EWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTD 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 372 RVPYPRPGTCPSK--TFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNyqFTQIVVDRVDAEDGQ-YDV 448
Cdd:cd11258 320 PVPSPRPGSCINNwhRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSN--FTHVVWTRVLGLDGEtYSV 397
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543681 449 MFIGTDVGTVLKVVSVPKETWhdleevLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11258 398 LFIGTLDGWLIKAVSLGSWVH------MIEELQVFDQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
55-514 2.29e-112

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: 349.16  E-value: 2.29e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  55 SSYHTFLLDEERSRLYVGAKDHIFSFNLVNI---KDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYA 131
Cdd:cd11257   8 SNYTALLLSKDGNMLYVGARETLFALSSNDIsptGEQQELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRLNSTHLFT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 132 CGTGAFHPICTYIEVghhpeDNIFKLQDSH----FENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGH 207
Cdd:cd11257  88 CGTYAFSPICTYIVM-----TNFSLERDEKgeplLEDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIYRSLGS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 208 HHPIRTEqHDSRWLNDPRFISAHLIPESDNP---EDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWT 284
Cdd:cd11257 163 GTPLKTE-NSLNWLQDPAFVGSAYIQESLPKlvgDDDKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGGERVLQKRWT 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 285 TFLKARLICSVPGpNGIDthFDELQDVFLM--NSKDPKNPIVYGVFTT--SSNIFKGSAVCMYSMSDVRRVFLGPYAHRD 360
Cdd:cd11257 242 TFLKAQLLCSLPD-DGFP--FNVLQDVFVLtpSPEDWKDTLFYGVFTSqwHKGTAGSSAVCVFTMDQVQRAFNGLYKEVN 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 361 GPNYQWVPYQGRVPYPRPGTCPSKTFG--GFDSTKDLPDDVITFARSHPAMYNpvfPINNRPIMIKTDVNYqfTQIVVDR 438
Cdd:cd11257 319 RETQQWYTYTHPVPEPRPGACITNSARerKINSSLHMPDRVLNFVKDHFLMDG---QVRSQPLLLQPQVRY--TQIAVHR 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543681 439 VDAEDGQYDVMFIGTDVGTVLKVVSVPKETWhdleevLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11257 394 VKGLHKTYDVLFLGTDDGRLHKAVSVGPMVH------IIEELQIFSEGQPVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
49-514 1.84e-111

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: 346.51  E-value: 1.84e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  49 NGLANsssYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQ-KIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQT 127
Cdd:cd11260   4 QGIWN---YSTMLLREDLGLLVLGAREAVFALDLNDISVKRaKVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMNDS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 128 HLYACGTGAFHPICTYIEVghhpEDNIFKLQDSHfENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTlgH 207
Cdd:cd11260  81 RMYVCGTNAFSPTCDYISY----DDGQLTLEGKQ-EDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRS--S 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 208 HHPIRTEqHDSRWLNDPRFISAHLIPES-DNPE--DDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWT 284
Cdd:cd11260 154 PITIRTE-FKSSWLNEPNFIYMAAVPESeDSPEgdDDKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQKKWT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 285 TFLKARLICSVPGPNGIDThfdeLQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFL-GPYAHR---D 360
Cdd:cd11260 233 SFLKARLDCSVPEPSLPYV----IQDVFHVCHQDWRKCVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrGKFKTPvavE 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 361 GPNYQWVPYQGRVPYPRPGTCPSKTF--GGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVnyQFTQIVVDR 438
Cdd:cd11260 309 TSFVKWVMYSGELPVPRPGACINNAArtSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGA--LFTRIVVDM 386
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543681 439 VDAEDGQ-YDVMFIGTDVGTVLKVVSvpketwHDLEEVLLEEMTVFREPTTISAMELStkQQQLYIGSTAGVAQLPL 514
Cdd:cd11260 387 VTAADGQsYPVMFIGTANGYVLKAVN------YDGEMHIIEEVQLFEPEEPIDILRLS--QNQLYAGSASGVVQMPV 455
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
69-514 1.04e-109

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: 342.19  E-value: 1.04e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  69 LYVGAKDHIFSFNL-----VNIKDFQKIVWPVSYTRRDECKWAGKDIlKECANFIKVLEAYNQTHLYACGTGAFHPICTY 143
Cdd:cd11242  21 LYIAARDHVYTVDLdashtEEIVPSKKLTWRSRQADVENCRMKGKHK-DECHNFIKVLVPRNDETLFVCGTNAFNPVCRN 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 144 IEVGhhpednifKLQDSHFE-NGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLN 222
Cdd:cd11242 100 YRID--------TLEQDGEEiSGMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYDSKWLK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 223 DPRFIsaHLIPESDNpeddkVYFFFRENAIDGEHSGKATHARIGQICKNDFGG-HRSLVNKWTTFLKARLICSVPGpngi 301
Cdd:cd11242 172 EPHFV--HAVEYGDY-----VYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPG---- 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 302 DTHF--DELQ---DVFLMNSKdpknPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPY-QGRVPY 375
Cdd:cd11242 241 DSHFyfDVLQavtDVIRINGR----PVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVpEDRVPK 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 376 PRPGTCP-SKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTD 454
Cdd:cd11242 317 PRPGCCAgSGSAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYRLTQIAVDNAAGPYQNYTVVFLGSE 396
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543681 455 VGTVLKVVSVPKETWHDlEEVLLEEMTVFR---------EPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11242 397 AGTVLKFLARIGPSGSN-GSVFLEEIDVYNpakcsydgeEDRRIIGLELDRASHALFVAFSGCVIRVPL 464
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
51-514 2.00e-103

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: 325.33  E-value: 2.00e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  51 LANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVN---IKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQT 127
Cdd:cd11256   4 QENVHNYDQLLLSPDETTLYVGARDNILALGIRTpgpIRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPVNGT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 128 HLYACGTGAFHPICTYIEVGHhpedniFKLQDSH----FENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFR 203
Cdd:cd11256  84 HLYTCGTYAFSPACTYIELDH------FSLPPPNgtiiTMDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 204 TLGHHHPIRTEQHdSRWLN-DPRFISAHLIPEsdnpeDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNK 282
Cdd:cd11256 158 NLGTKVSLKTDGF-LRWLNaDAVFVASFNPQG-----DSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKK 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 283 WTTFLKARLICSVPGpngiDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNI--FKGSAVCMYSMSDVRRVFLGPYAHRD 360
Cdd:cd11256 232 WTTFLKAQLTCSQQG----HFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLggRRSSAVCAYKLNDIEKVFNGKYKELN 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 361 GPNYQWVPYQGRVPYPRPGTCPsktfGGFDSTKDLpddviTFARSHPAMYNPVFPINNRPIMIKTDVNYqfTQIVVDRVD 440
Cdd:cd11256 308 KESSRWTRYMGPVSDPRPGSCS----GGKSSDKAL-----NFMKDHFLMDEVVLPGAGRPLLVKSNVQY--TRIAVDSVQ 376
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543681 441 AEDGQ-YDVMFIGTDVGTVLKVVSVPKETWHdleevLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11256 377 GVSGHnYTVMFLGTDKGFLHKAVLMGGSESH-----IIEEIELLTPPEPVENLLLAANEGVVYIGYSAGVWRVPL 446
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
51-514 2.93e-103

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: 324.51  E-value: 2.93e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  51 LANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDIlKECANFIKVLEAYNQThLY 130
Cdd:cd11241   3 IEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLSLLQAVPWNSDEDTKRQCQSKGKSV-EECQNYVRVLLVVGKN-LF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 131 ACGTGAFHPICTYIEVGhhpedNIFKLQDSHfeNGRGKSPYDPKL-LTASLLIDGELYSGTAADFMGRDFAIFRTLGHHH 209
Cdd:cd11241  81 TCGTYAFSPVCTIRKLS-----NLTQILDTI--SGVARCPYSPAHnSTALISASGELYAGTVYDFSGRDPAIYRSLGGKP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 210 PIRTEQHDSRWLNDPRFISAHLIpesdnpeDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKA 289
Cdd:cd11241 154 PLRTAQYNSKWLNEPNFVGSYEI-------GNHTYFFFRENAVEHQDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKA 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 290 RLICSVPGPngIDTHFDELQDVFLMnskdPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPY 369
Cdd:cd11241 227 RLNCSLPGE--FPFYYNEIQGTFYL----PETDLIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPT 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 370 QgrVPYPRPGTCPSKTFGGFDST--KDLPDdvitfARSHPAMYNPVFPINNRPIMIKTDVnyQFTQIVVDRVDAEDGQ-Y 446
Cdd:cd11241 301 P--NPHPNFQCTTSIDRGQPANTteRDLQD-----AQKYQLMAEVVQPVTKIPLVTMDDV--RFSKLAVDVVQGRGTQlV 371
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543681 447 DVMFIGTDVGTVLKVVSVPKEtwhdLEEVLLEEMTVF----REPttISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11241 372 HIFYVGTDYGTILKMYQPHRS----QKSCTLEEIKILpamkGEP--ITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
54-513 1.88e-99

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: 315.29  E-value: 1.88e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  54 SSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDF-QKIVWPVSYTRRDECKWAGKDiLKECANFIKVLEAYNQTHLYAC 132
Cdd:cd11261  11 TYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERpRRIDWMVPEAHRQNCRKKGKK-EAECHNFIRILAIANASHLLTC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 133 GTGAFHPICTYIEVGHhpedniFKlQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHP-I 211
Cdd:cd11261  90 GTFAFDPKCGVIDVSS------FQ-QVERLESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAVGRAEEwI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 212 RTEQHDSrWLNDPRFISAHLI---PESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLK 288
Cdd:cd11261 163 RTETLPS-WLNAPAFVAAVFLspaEWGDEDGDDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLK 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 289 ARLICsvPGPNGiDTHFDELQDVFLMNSKDPKN-PIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWV 367
Cdd:cd11261 242 ADLLC--PGPEH-GRASSILQDVTTLRPLPGAGtPIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGL 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 368 PY-QGRVPYPRPGTC--PSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQftQIVVDRVDAEDG 444
Cdd:cd11261 319 PVmDSDVPQPRPGECitNNMKLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYL--RVAAHRVTSLSG 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 445 Q-YDVMFIGTDVGTVLKVVSVPKETwhdleeVLLEEMTVFREPTTISAMELstKQQQLYIGSTAGVAQLP 513
Cdd:cd11261 397 KeYDVLYLGTEDGHLHRAVRIGAQL------SVLEDLALFPEPQPVENLQL--HHNWLLVGSDTEVTQIN 458
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
57-514 8.93e-99

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


Pssm-ID: 200499 [Multi-domain]  Cd Length: 452  Bit Score: 313.21  E-value: 8.93e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  57 YHTFLLDEERSRLYVGAKDHIFSFNLVNIKD----FQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQ-THLYA 131
Cdd:cd11238   3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINDtgnnCARDELTLSPSDVSECVSKGKDEEYECRNHVRVIQPMGDgQTLYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 132 CGTGAfhpictyievgHHPED---NIFKLQDSHF----ENGRGKSPYDPKLLTASLLIDG-------ELYSGTAADFMGR 197
Cdd:cd11238  83 CSTNA-----------MNPKDrvlDANLLHLPEYvpgpGNGIGKCPYDPDDNSTAVWVEWgnpgdlpALYSGTRTEFTKA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 198 DFAIFR------TLGHHHP-IRTEQHDSRWLNDPRFISAHLIpesdnpeDDKVYFFFRENAIDGEHSGKATHARIGQICK 270
Cdd:cd11238 152 NTVIYRpplynnTKGRHESfMRTLKYDSKWLDEPNFVGSFDI-------GDYVYFFFRETAVEYINCGKVVYSRVARVCK 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 271 NDFGGHRSLVNKWTTFLKARLICSVPG--PngidTHFDELQDVFLMNSKDpkNPIVYGVFTTSSNIFKGSAVCMYSMSDV 348
Cdd:cd11238 225 KDTGGKNVLRQNWTTFLKARLNCSISGefP----FYFNEIQSVYKVPGRD--DTLFYATFTTSENGFTGSAVCVFTLSDI 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 349 RRVFL-GPYAHRDGPNYQWVPY-QGRVPYPRPGTCPSktfggfdSTKDLPDDVITFARSHPAMYNPVfpINNRPIMIKTD 426
Cdd:cd11238 299 NAAFDtGKFKEQASSSSAWLPVlSSEVPEPRPGTCVN-------DSATLSDTVLHFARTHPLMDDAV--SHGPPLLYLRD 369
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 427 VnyQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSvpketWHDLEEVLLEEMTVF--REPTTISAMELStKQQQLYIG 504
Cdd:cd11238 370 V--VFTHLVVDKLRIDDQEYVVFYAGSNDGKVYKIVH-----WKDAGESKSNLLDVFelTPGEPIRAMELL-PGEFLYVA 441
                       490
                ....*....|
gi 31543681 505 STAGVAQLPL 514
Cdd:cd11238 442 SDHRVSQIDL 451
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
61-514 4.11e-98

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: 311.96  E-value: 4.11e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  61 LLDEERSRLYVGAKDHIFSFNL-----VNIKDFQKIVWPVSYTRRDECKWAGKDiLKECANFIKVLEAYNQTHLYACGTG 135
Cdd:cd11269  13 LMLKIRDTLYIAGRDQVYTVNLnevpkTEVTPSRKLTWRSRQQDRENCAMKGKH-KDECHNFIKVFVPRNDEMVFVCGTN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 136 AFHPICTYievghhpedniFKLQDSHFE----NGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPI 211
Cdd:cd11269  92 AFNPMCRY-----------YRLSTLEYDgeeiSGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 212 RTEQHDSRWLNDPRFIsaHLIPESdnpedDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGG-HRSLVNKWTTFLKAR 290
Cdd:cd11269 161 RTIKYDSKWIKEPHFL--HAIEYG-----NYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKAR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 291 LICSVPGPNGIdtHFDELQ---DVFLMNSKdpknPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWV 367
Cdd:cd11269 234 LNCSVPGDSFF--YFDVLQsitDIIEINGI----PTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWT 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 368 PY-QGRVPYPRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQ 445
Cdd:cd11269 308 AVpEDKVPKPRPGCCAKHGLAeAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTAIAVDHAAGPHQN 387
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543681 446 YDVMFIGTDVGTVLKVVSvpKETWHDL-EEVLLEEMTVF---------REPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11269 388 YTVIFVGSEAGVVLKILA--KTSPFSLnDSVLLEEIEAYnhakcsaenEEDRRVISLQLDRDHHALFVAFSSCVVRIPL 464
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
57-514 1.26e-96

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: 307.29  E-value: 1.26e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  57 YHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDILkECANFIKVLeAYNQTHLYACGTGA 136
Cdd:cd11264   9 FSQLALDLNRNQLIVGARNYLFRLSLHNVSLIQATEWGSDEDTRRSCQSKGKTEE-ECQNYVRVL-IVYGKKVFTCGTNA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 137 FHPICTYIEVGhhpedNIFKLQDShfENGRGKSPYDPKL-LTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQ 215
Cdd:cd11264  87 FSPVCTSRQVG-----NLSKVIER--INGVARCPYDPRHnSTAVITSRGELYAATVIDFSGRDPAIYRSLGSVPPLRTAQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 216 HDSRWLNDPRFISAHLIPESdnpeddkVYFFFRENAIdgEHS-GKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICS 294
Cdd:cd11264 160 YNSKWLNEPNFIAAYDIGLF-------TYFFFRENAV--EHDcGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCS 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 295 VPGPngIDTHFDELQDVFLMnskdPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVP 374
Cdd:cd11264 231 RPGE--IPFYYNELQSTFYL----PEQDLIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTANPIP 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 375 YPRPGTCPSKTfggfdSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVnyQFTQIVVDRVDAEDGQYDVMFIGTD 454
Cdd:cd11264 305 NFQCGTLSDDS-----PNENLTERSLQDAQRLFLMNDVVQPVTVDPLVTQDSV--RFSKLVVDIVQGKDTLYHVMYIGTE 377
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31543681 455 VGTVLKVVSVPKETwhdLEEVLLEEMTVF----REPttISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11264 378 YGTILKALSTTNRS---LRSCYLEEMQILppgqREP--IRSLQILHSDRSLFVGLNNGVLKIPL 436
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
69-514 1.27e-95

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: 305.42  E-value: 1.27e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  69 LYVGAKDHIFSFNL-----VNIKDFQKIVWPVSYTRRDECKWAGKDiLKECANFIKVLEAYNQTHLYACGTGAFHPICTY 143
Cdd:cd11266  21 LYIAARDHIYTVDIdtshtEEIYFSKKLTWKSRQADVDTCRMKGKH-KDECHNFIKVLLKRNDDTLFVCGTNAFNPSCRN 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 144 IEVghhpedNIFKLQDSHFeNGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLND 223
Cdd:cd11266 100 YKM------DTLEFFGDEF-SGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKE 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 224 PRFISAhlipesdNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGG-HRSLVNKWTTFLKARLICSVPGpngiD 302
Cdd:cd11266 173 PYFVQA-------VDYGDYIYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPG----D 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 303 THF-----DELQDVFLMNSKDpknpIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPY-QGRVPYP 376
Cdd:cd11266 242 SHFyfnilQAVTDVIHINGRD----VVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVpDERVPKP 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 377 RPGTCP-SKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTDV 455
Cdd:cd11266 318 RPGCCAgSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVDNAAGPYQNHTVVFLGSEK 397
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543681 456 GTVLKVVSVPKETWHDLEEVLLEEMTVFR---------EPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11266 398 GIILKFLARTGNSGFLNDSLFLEEMNVYNsekcsydgvEDKRIMGMQLDKASSALYVAFSTCVIKVPL 465
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
69-484 1.46e-89

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: 289.42  E-value: 1.46e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  69 LYVGAKDHIFSFNLVNIKD-----FQKIVWPVSYTRRDECKWAGKDiLKECANFIKVLEAYNQTHLYACGTGAFHPIC-- 141
Cdd:cd11267  21 LYIGDRDNLYRVELDPTAGtemryHKKLTWRSNKNDINVCRMKGKH-EGECRNFIKVLLLRDYGTLFVCGTNAFNPVCan 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 142 ----TYIEVGhhpeDNIfklqdshfeNGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHD 217
Cdd:cd11267 100 ysidTLEPVG----DNI---------SGMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 218 SRWLNDPRFISA-----HlipesdnpeddkVYFFFRENAIDGEHSGKATHARIGQICKNDFGG-HRSLVNKWTTFLKARL 291
Cdd:cd11267 167 SKWFKEPYFVHAvewgsH------------VYFFFREIAMEFNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 292 ICSVPGpngiDTHF-----DELQDVFLMNSKdpknPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQW 366
Cdd:cd11267 235 NCSVPG----DSHFyfnvlQAVSDILNLGGR----PVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIW 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 367 VPY-QGRVPYPRPGTCPSKTFGgFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQ 445
Cdd:cd11267 307 TPVpEELVPRPRPGCCAAPGMR-YNSSSTLPDEVLNFVKTHPLMDEAVPSLGHAPWIVRTMTRYQLTHMVVDTEAGPHGN 385
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 31543681 446 YDVMFIGTDVGTVLKVVSVPKETWHDL--EEVLLEEMTVFR 484
Cdd:cd11267 386 HTVVFLGSTRGTVLKFLIIPNASSSEIsnQSVFLEELETYN 426
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
53-514 4.70e-88

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: 284.62  E-value: 4.70e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  53 NSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDiLKECANFIKVLeAYNQTHLYAC 132
Cdd:cd11263   5 NAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLSLIQAVEWECDEATKKACYSKGKS-KEECQNYIRVL-LVGGDRLFTC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 133 GTGAFHPICTyievgHHPEDNIFKLQDShfENGRGKSPYDPKLLTASLLI-DGELYSGTAADFMGRDFAIFRTLGHHHPI 211
Cdd:cd11263  83 GTNAFTPICT-----NRTLNNLTEIHDQ--ISGMARCPYSPQHNSTALLTsSGELYAATAMDFPGRDPAIYRSLGILPPL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 212 RTEQHDSRWLNDPRFISAHLIpesdnpeDDKVYFFFRENAIdgEHS-GKATHARIGQICKNDFGGHRSLVNKWTTFLKAR 290
Cdd:cd11263 156 RTAQYNSKWLNEPNFVSSYDI-------GNFTYFFFRENAV--EHDcGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKAR 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 291 LICSVPGPngIDTHFDELQDVFLMnskdPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYq 370
Cdd:cd11263 227 LNCSRPGE--IPFYYNELQSTFFL----PELDLIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPY- 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 371 grvPYPRP----GTCPSKTFGGFdSTKDLPDdvitfARSHPAMYNPVFPINNRPIMIKTdvNYQFTQIVVDRVDAEDGQY 446
Cdd:cd11263 300 ---PNPNPnfqcGTMDQGLYVNL-TERNLQD-----AQKFILMHEVVQPVTPVPYFMED--NSRFSHVAVDVVQGKDMLF 368
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543681 447 DVMFIGTDVGTVLKVVSVPKETwhdLEEVLLEEMTVF----REPttISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11263 369 HIIYLATDYGTIKKVLAPLNQS---SSSCLLEEIELFpkrqREP--IRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
69-514 3.11e-84

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: 275.45  E-value: 3.11e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  69 LYVGAKDHIFSFNLVNIKDF----QKIVWPVSytRRDECKWAGKdILKECANFIKVLEAYNQTHLYACGTGAFHPICTYI 144
Cdd:cd11270  21 VYIAARDHVFAINLSASLERivpqQKLTWKTK--DVEKCTVRGK-NSDECYNYIKVLVPRNDETLFACGTNAFNPTCRNY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 145 EVghhpedNIFKLQDSHFeNGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPI-RTEQHDSRWLND 223
Cdd:cd11270  98 KM------SSLEQDGEEV-IGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLGESSPVlRTVKYDSKWLRE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 224 PRFISAhliPESDNpeddKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGH-RSLVNKWTTFLKARLICSVPGPNGId 302
Cdd:cd11270 171 PHFLHA---IEYGN----YVYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPGDSFF- 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 303 tHFDELQ---DVFLMNSKdpknPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPY-QGRVPYPRP 378
Cdd:cd11270 243 -YFDVLQsltNVMQINHR----PAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVpDEAVPKPRP 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 379 GTCPS-KTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGT 457
Cdd:cd11270 318 GSCAGdGPAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFKLTQIAVDTAAGPYKNYTVVFLGSENGH 397
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543681 458 VLKVVSVPKETwHDLEEVLLEEMTVF--------REPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11270 398 VLKVLASMHPN-SSYSTQVLEDIDVYnpnkcnvrGEDRRILGLELDKDHHALFVAFTGCVIRVPL 461
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
69-514 9.53e-83

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: 271.57  E-value: 9.53e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  69 LYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDE----CKWAGKdILKECANFIKVLEAYNQTHLYACGTGAFHPIC-TY 143
Cdd:cd11268  21 LLVAARDHVFSFDLQAEEEGEGLVPNKYLTWRSQdvenCAVRGK-LTDECYNYIRVLVPWDSQTLLACGTNSFSPVCrSY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 144 ievghhpedNIFKLQDSHFE-NGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLN 222
Cdd:cd11268 100 ---------GITSLQQEGEElSGQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 223 DPRFISAHlipesdnPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGH-RSLVNKWTTFLKARLICSVPGPNGI 301
Cdd:cd11268 171 EPHFVQAL-------EHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPGDSTF 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 302 dtHFDELQDVflmnsKDPKN----PIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPY-QGRVPYP 376
Cdd:cd11268 244 --YFDVLQAL-----TGPVNlhgrSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVsEDRVPSP 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 377 RPGTCPSktFGG---FDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDvNYQFTQIVVDRVDAEDGQYDVMFIGT 453
Cdd:cd11268 317 RPGSCAG--VGGaalFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLTLTS-RALLTQVAVDGMAGPHSNITVMFLGS 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31543681 454 DVGTVLKVVSvPKETWHDLEEVLLEEMTVF--------REPTT---ISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11268 394 NDGTVLKVLP-PGGRSGGPEPILLEEIDAYsparcsgkRTAQTarrIIGLELDTEGHRLFVAFSGCIVYLPL 464
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
308-495 3.21e-81

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: 257.20  E-value: 3.21e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681   308 LQDVFLMN--SKDPKNPIVYGVFTTS-SNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSK 384
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681   385 TFGgfdstKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTdvNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSV 464
Cdd:pfam01403  81 PLR-----LDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRT--GVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVLV 153
                         170       180       190
                  ....*....|....*....|....*....|.
gi 31543681   465 PKEtwhdlEEVLLEEMTVFREPTTISAMELS 495
Cdd:pfam01403 154 GSE-----ESHIIEEIQVFPEPQPVLNLLLS 179
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
53-513 3.89e-78

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: 258.17  E-value: 3.89e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  53 NSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDIlKECANFIKVLEAYNQtHLYAC 132
Cdd:cd11265   5 EVTSYSQMLFDVARNQVIVGARDNLYRLSLDGLELLERASWPAAESKVALCQNKGQSE-EDCHNYVKVLLSYGK-QLFAC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 133 GTGAFHPICTYIEVghhpeDNIFKLQDShfENGRGKSPYDPKL-LTASLLIDGELYSGTAADFMGRDFAIFRTLG--HHH 209
Cdd:cd11265  83 GTNAFSPRCSWREM-----ENLTSVTEW--DSGVAKCPYSPHAnITALLSSSGQLFVGSPTDFSGSDSAIYRTLGtsNKS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 210 PIRTEQHDSRWLNDPRFISAHlipESDNpeddKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLV-NKWTTFLK 288
Cdd:cd11265 156 FLRTKQYNSKWLNEPQFVGSF---ETGN----FVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLLkDNWTTFLK 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 289 ARLICSVPG--PngidTHFDELQDVFLMnskdPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQW 366
Cdd:cd11265 229 ARLNCSLPGeyP----FYFDEIQGMTYL----PDEGILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAW 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 367 vpyqGRVPYP---RPGTCPSKTFGGF-DSTKdlpddvitfarsHPAMYNPVFPINNRPiMIKTDVNyQFTQIVVDRVDAE 442
Cdd:cd11265 301 ----ERVNVNhrdHFNQCSSSSSSHLlESSR------------YQLMDEAVQPITLEP-LHHAKLE-RFSHIAVDVIPTK 362
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31543681 443 -DGQYDVMFIGTDVGTVLKVVSVPKETwhdlEEVLLEEMTVFREPTT-ISAMELSTKQQQLYIGSTAGVAQLP 513
Cdd:cd11265 363 iHQSVHVLYVATTGGLIKKISVLPRTQ----ETCLVEIWQPLPTPDSpIKTMQYLKVTDSLYVGTELALMRIP 431
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
56-514 1.64e-70

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: 237.05  E-value: 1.64e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  56 SYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVwPVSYTRRDeCKwaGKDILKECANFIKVLEAYNQThLYACGTG 135
Cdd:cd11243   3 SYPVFFHEAGSSSVYVGGQGALYLLDFTGSAVIVKKI-PDEKTEKD-CK--KRATLDDCENYITLIKKLDYR-LLVCGTN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 136 AFHPICTYIEvghhpEDNIFKLQDshfenGRGKSPYDPKLLTASLLIDGELYS---GTAADFMgrdfaIFRTLGHHHPIR 212
Cdd:cd11243  78 AGSPKCWFLV-----NQTLVTLSA-----DRGVAPFLPDENSLVLIEGNNVYStisGKKGNIP-----RFRRYGGKKELY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 213 TEqhDSrWLNDPRFISAHLIPEsDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSL-VNKWTTFLKARL 291
Cdd:cd11243 143 TS--DT-VMQKPQFVKATLLPE-DEQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLsTSKWSTFLKARL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 292 ICSVPGPNGidtHFDELQDVFLMNSKDPKNPIVYGVFTtssNIFKGSAVCMYSMSDVRRVFlgpyahrdgPNYQWVPYQG 371
Cdd:cd11243 219 VCGDPATPM---NFNRLQDVFLLPKEEWREAVVYGVFS---NTWGSSAVCSYSLGDIDKVF---------RTSSLKGYSG 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 372 RVPYPRPGTC-PSktfggfDSTkdLPDDVITFARSHPAMYNPVFPINNRPIMIKTDvNYQFTQIVVDRVDAEDG-QYDVM 449
Cdd:cd11243 284 SLPNPRPGTCvPP------EQT--HPSETFSFADEHPELDDRIEPDEPRKLPVFQN-KDHYQKVVVDEVRASDGvSYDVL 354
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543681 450 FIGTDVGTVLKVVSVPKETwhdleeVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd11243 355 YLATDKGKIHKVVESKGQT------HNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
57-514 2.41e-66

The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins and plexins have a Sema domain on their N-termini. Plexins function as receptors for the semaphorins. Evolutionarily, plexins may be the ancestor of semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems, and cancer. Semaphorins can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. Plexins are a large family of transmembrane proteins, which are divided into four types (A-D) according to sequence similarity. In vertebrates, type A plexins serve as co-receptors for neuropilins to mediate the signalling of class 3 semaphorins. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B plexins. This family also includes the MET and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves to recognize and bind receptors.


Pssm-ID: 200495 [Multi-domain]  Cd Length: 392  Bit Score: 225.16  E-value: 2.41e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681  57 YHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQ-----KIVWPVSYTRRDECKwAGKDILKECANFIKVLEA-YNQTHLY 130
Cdd:cd09295   2 DDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLscispELNFGFNEDQKAFCP-LRRGKWTECINYIKVLQQkGDLDILA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 131 ACGTGAFHPICtyievGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIF-RTLGHHH 209
Cdd:cd09295  81 VCGSNAAQPSC-----GSYRLDVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKDGDRPALsRRSSNVH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 210 PIRTEQHDSRWLNDPRFISAHLIPESDnpedDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKA 289
Cdd:cd09295 156 YLRIVVDSSTGLDEITFVYAFVSGDDD----DEVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKA 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 290 RLICSVPGPngiDTHFDELQDVFLMnSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFlgpyahrdgpnyqwvpy 369
Cdd:cd09295 232 DLNCSRPQS---GFAFNLLQDATGD-TKNLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVF----------------- 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 370 qgrvpyprpgtcpsktfggfdstkdlpDDvitfarshpamynPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVM 449
Cdd:cd09295 291 ---------------------------DD-------------PVEAINNRPLYAHQNQRSRLTSIAVDATKQKSVGYQVV 330
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543681 450 FIGTDVGTVLKVVSvpKETWHDLEevLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPL 514
Cdd:cd09295 331 FLGLKLGSLGKALA--FFFLYKGH--IIEEWKVFKDSSRITNLDLSRPPLYLYVGSESGVLGVPV 391
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
580-671 5.70e-45

Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed of the immunoglobulin (Ig)-like domain of Sema3 and similar proteins. Semaphorins are classified based on structural features additional to the Sema domain. Sema3 is a Class III semaphorin that is secreted. It is a vertebrate class having a Sema domain, an Ig domain, a short basic domain. They have been shown to be axonal guidance cues and have a part in the regulation of the cardiovascular, immune, and respiratory systems. Sema3A, the prototype member of this class III subfamily, induces growth cone collapse and is an inhibitor of axonal sprouting. In perinatal rat cortex, it acts as a chemoattractant and functions to direct the orientated extension of apical dendrites. It may play a role, prior to the development of apical dendrites, in signaling the radial migration of newborn cortical neurons towards the upper layers. Sema3A selectively inhibits vascular endothelial growth factor receptor (VEGF)-induced angiogenesis and induces microvascular permeability. This group also includes Sema3B, -C, -D, -E, -G.


Pssm-ID: 409455  Cd Length: 92  Bit Score: 155.97  E-value: 5.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 580 SLEERIIYGVENSSTFLECSPKSQRALVYWQFQRRNEDRKEEIRMGDHIIRTEQGLLLRSLQKKDSGNYLCHAVEHGFMQ 659
Cdd:cd05871   1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                        90
                ....*....|..
gi 31543681 660 TLLKVTLEVIDT 671
Cdd:cd05871  81 TLVKIRLHVIEP 92
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
580-671 1.57e-28

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 109.47  E-value: 1.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 580 SLEERIIYGvENSSTFLECSPKSQRALVYWQFQRRNEDRKeeiRMGDHIIRTEQGLLLRSLQKKDSGNYLCHAVEHGFMQ 659
Cdd:cd04979   1 TSFKQISVK-EGDTVILSCSVKSNNAPVTWIHNGKKVPRY---RSPRLVLKTERGLLIRSAQEADAGVYECHSGERVLGS 76
                        90
                ....*....|..
gi 31543681 660 TLLKVTLEVIDT 671
Cdd:cd04979  77 TLRSVTLHVLER 88
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
446-544 3.27e-08

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


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 56.86  E-value: 3.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 446 YDVMFIGTDVGTVLKV-VSVPKETwhdleEVLLEEMTVFREPTTI-SAMELSTKQQQLYIGSTAGVAQLPLHRCDIYgKA 523
Cdd:cd11272 406 YSVVFVGTKSGKLKKIrADGPPHG-----GVQYEMVSVFKDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQY-TT 479
                        90       100
                ....*....|....*....|...
gi 31543681 524 CAECCLARDPYCAWDG--SSCSR 544
Cdd:cd11272 480 CGECLSSGDPHCGWCAlhNMCSR 502
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
262-515 1.23e-07

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: 54.64  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 262 HARIGQICKNDfgghrslvNKWTTFLKARLICSVPGPngidTHFDELQDVFLMN---------SKDPKNPIVYGVFTTSS 332
Cdd:cd11236 212 ISRLVRVCQSD--------SNYYSYTEVPLQCTGGDG----TNYNLLQAAYVGKagsdlarslGISTDDDVLFGVFSKSK 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 333 NIFKG----SAVCMYSMSDVRRVFlgpyahrdgpnYQWVPYQGRVPYprpgtcpsktfggfdstkdlpddvitfarshpa 408
Cdd:cd11236 280 GPSAEpsskSALCVFSMKDIEAAF-----------NDNCPLGGGVPI--------------------------------- 315
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 409 mynpvfpinnrpIMIKTDVNYQFTQIVVDRVDaedgQYDVMFIGTDVGTVLKVVSVPKETwhdleEVLLEEMTVFREPTT 488
Cdd:cd11236 316 ------------TTSAVLSDSLLTSVAVTTTR----NHTVAFLGTSDGQLKKVVLESSSS-----ATQYETLLVDSGSPI 374
                       250       260
                ....*....|....*....|....*..
gi 31543681 489 ISAMELSTKQQQLYIGSTAGVAQLPLH 515
Cdd:cd11236 375 LPDMVFDPDGEHLYVMTPKKVTKVPVE 401
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
516-552 7.52e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 46.38  E-value: 7.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 31543681    516 RCDIYgKACAECCLARDPYCAWD--GSSCSRYFPTAKRR 552
Cdd:smart00423   1 RCSKY-TSCSECLLARDPYCAWCssQGRCTSGERCDSRR 38
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
240-541 4.92e-05

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: 46.43  E-value: 4.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 240 DDKVYFFFRENAIdgehsgkaTHARIGQICKNDFGGhrslvnkwTTFLKARLICSVpgpngiDTHFDELQDV-FLMNSKD 318
Cdd:cd09295   2 DDKILVSFRKDTI--------YVGAIARIYKVDGGG--------TRLLLSCISPEL------NFGFNEDQKAfCPLRRGK 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 319 PKNPIVYGVFTTSSNIFKGSAVCMYSMsdvrrvFLGPYAHRDGPNYQwvpYQGRVPYPRP-GTCPSKTFGGfdSTKDLPD 397
Cdd:cd09295  60 WTECINYIKVLQQKGDLDILAVCGSNA------AQPSCGSYRLDVLV---ELGKVRWPSGrPRCPIDNKHS--NMGVNVD 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 398 DVITFARSHPAMYNpvfpinNRPIMIKTDVNYQFTQIVVDRVDAEDGQ-YDVMFIGTDvgtvlkvvsvpketwhDLEEVL 476
Cdd:cd09295 129 SKLYSATDHDFKDG------DRPALSRRSSNVHYLRIVVDSSTGLDEItFVYAFVSGD----------------DDDEVY 186
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31543681 477 LeemtVFREPTTisameLSTKQQQLYIGSTAGVAQLPLHRCDIYGKaCAECCLARDPYCAWDGSS 541
Cdd:cd09295 187 F----FFRQEPV-----EYLKKGMVYVPRIARVCKLDVGGCHRLKK-KLTSFLKADLNCSRPQSG 241
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
596-668 9.49e-05

Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. Sema4D is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4D has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4D plays a part in the development of GABAergic synapses. Sema4D in addition is an immune semaphorin. It is abundant on resting T cells; its expression is weak on resting B cells and antigen presenting cells (APCs), but is upregulated by various stimuli. The receptor used by Sema4D in the immune system is CD72. Sem4D enhances the activation of B cells and DCs through binding CD72, perhaps by reducing CD72s inhibitory signals. The receptor used by Sema4D in the non-lymphatic tissues is plexin-B1. Sem4D is anchored to the cell surface but its extracellular domain can be released from the cell surface by a metalloprotease-dependent process. Sem4D may mediate its effects in its membrane-bound form and/or its cleaved form.


Pssm-ID: 409457  Cd Length: 87  Bit Score: 41.72  E-value: 9.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681 596 LECSPKSQRALVYWQFQR---RNEDRKEEIrMGDhiirteqGLLLRSLQKKDSGNYLCHAVEHG----FMQTLLKVTLEV 668
Cdd:cd05873  16 LKCSPKSNLARVVWKFQGkvlKAESPKYGL-YGD-------GLLIFNASEADAGRYQCLSVEKSkaktFFQTVAKYVLEV 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
586-664 6.85e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 36.33  E-value: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543681    586 IYGVENSSTFLECSPKSQR-ALVYWQFQRrnedrKEEIRMGDHIIRTEQG----LLLRSLQKKDSGNYLCHAV-EHG--F 657
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPpPEVTWYKQG-----GKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATnSSGsaS 78

                   ....*..
gi 31543681    658 MQTLLKV 664
Cdd:smart00410  79 SGTTLTV 85
 
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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