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Conserved domains on  [gi|2462591854|ref|XP_054203484|]
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semaphorin-3F isoform X2 [Homo sapiens]

Protein Classification

semaphorin-3( domain architecture ID 10181359)

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_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: 1022.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNR 127
Cdd:cd11254     1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 128 THLYVCGTGAYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11254    81 THLYVCGTGAYNPVCAYINRGRRAEDYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAVYARIGRICLNDDGGHCCLVNKWSTFL 287
Cdd:cd11254   161 KQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 288 KARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 367
Cdd:cd11254   241 KARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 368 PFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRY 447
Cdd:cd11254   321 PYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGRY 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 448 EVLFLGTDRGTVQKVIVLPKDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11254   401 EVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
577-666 2.28e-38

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: 137.48  E-value: 2.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 577 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKH 656
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|
gi 2462591854 657 VVTRVQLHVL 666
Cdd:cd05871    81 TLVKIRLHVI 90
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
516-553 3.42e-07

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 3.42e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462591854  516 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 553
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
 
Name Accession Description Interval E-value
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: 1022.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNR 127
Cdd:cd11254     1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 128 THLYVCGTGAYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11254    81 THLYVCGTGAYNPVCAYINRGRRAEDYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAVYARIGRICLNDDGGHCCLVNKWSTFL 287
Cdd:cd11254   161 KQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 288 KARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 367
Cdd:cd11254   241 KARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 368 PFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRY 447
Cdd:cd11254   321 PYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGRY 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 448 EVLFLGTDRGTVQKVIVLPKDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11254   401 EVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema smart00630
semaphorin domain;
57-490 1.08e-153

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 452.21  E-value: 1.08e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854   57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVCGTG 136
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  137 AYNPMCTYVNRGrraqdyifyleperlesgkgkcpydpkldtasalineELYAGVYIDFMGTDAAIFRTLG----KQTA- 211
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------ELYVGTVADFSGSDPAIPRSLSvrrlKGTSg 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  212 --MRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEA-PQSPAVYARIGRICLNDDGGHCCLVNKWSTFLK 288
Cdd:smart00630 124 vsLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDdNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLK 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  289 ARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMP 368
Cdd:smart00630 197 ARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  369 FS-GKMPYPRPGTCPGGTFtpsmkSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVdAADGRY 447
Cdd:smart00630 275 YSrGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNY 348
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2462591854  448 EVLFLGTDRGTVQKVIVLPKDDQeMEELMLEEVEVFKDPAPVK 490
Cdd:smart00630 349 TVLFLGTSDGRILKVVLSESSSS-SESVVLEEISVFPDGSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
308-496 1.54e-73

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: 236.40  E-value: 1.54e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 308 LQDVFVQQ--TQDVRNPVIYAVFTSS-GSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG 384
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 385 TFtpsmksTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGapYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIV 464
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTG--VRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462591854 465 LPKDD-------QemeelmleeveVFKDPAPVKTMTISS 496
Cdd:pfam01403 153 VGSEEshiieeiQ-----------VFPEPQPVLNLLLSS 180
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
577-666 2.28e-38

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: 137.48  E-value: 2.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 577 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKH 656
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|
gi 2462591854 657 VVTRVQLHVL 666
Cdd:cd05871    81 TLVKIRLHVI 90
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
516-553 3.42e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 3.42e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462591854  516 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 553
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
581-665 6.84e-07

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: 47.50  E-value: 6.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  581 SVQYGVAGSAAFLECQPRS-PQATVKWLFQRDpgdrrREIRAEDRFLRTEQG----LLLRALQLSDRGLYSCTATeNNFK 655
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGsPPPEVTWYKQGG-----KLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAAT-NSSG 75
                           90
                   ....*....|
gi 2462591854  656 HVVTRVQLHV 665
Cdd:smart00410  76 SASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
581-650 1.20e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.01  E-value: 1.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591854 581 SVQYGVAGSAAFLECQPR-SPQATVKWLFqrdPGDRRREIRAEDRFLRTEQGLL-LRALQLSDRGLYSCTAT 650
Cdd:pfam13927   9 SSVTVREGETVTLTCEATgSPPPTITWYK---NGEPISSGSTRSRSLSGSNSTLtISNVTRSDAGTYTCVAS 77
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
516-557 1.16e-03

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 37.69  E-value: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462591854 516 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRSRRQD 557
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRRSACGAPEGNCEE 43
 
Name Accession Description Interval E-value
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: 1022.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNR 127
Cdd:cd11254     1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 128 THLYVCGTGAYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11254    81 THLYVCGTGAYNPVCAYINRGRRAEDYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAVYARIGRICLNDDGGHCCLVNKWSTFL 287
Cdd:cd11254   161 KQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 288 KARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 367
Cdd:cd11254   241 KARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 368 PFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRY 447
Cdd:cd11254   321 PYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGRY 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 448 EVLFLGTDRGTVQKVIVLPKDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11254   401 EVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
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: 879.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNR 127
Cdd:cd11239     1 FLGSMNSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPKKIYWPASPERIEECKMAGKDPNTECANFVRVLQPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 128 THLYVCGTGAYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11239    81 THLYACGTGAFHPICAFINVGRRLEDPIFKLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQS-PAVYARIGRICLNDDGGHCCLVNKWSTF 286
Cdd:cd11239   161 HRHYIRTEQYDSRWLNEPKFVGAYLIPDSDNPDDDKVYFFFREKAVEAEGSgKAIYSRVGRICKNDVGGQRSLVNKWSTF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 287 LKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQW 366
Cdd:cd11239   241 LKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNYQW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 367 MPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGR 446
Cdd:cd11239   321 VEYQGKVPYPRPGTCPSKTYGPLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPYRLTQIAVDRVEAEDGQ 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591854 447 YEVLFLGTDRGTVQKVIVLPKDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11239   401 YDVLFIGTDSGTVLKVVSLPKENWEMEEVILEELQVFKHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
53-517 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: 702.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYV 132
Cdd:cd11251     6 RPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNRTHLYV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 133 CGTGAYNPMCTYVNRGRRAQDYIFYLEpERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAM 212
Cdd:cd11251    86 CGSGAFSPVCVYVNRGRRSEEQVFHID-SKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 213 RTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSP-AVYARIGRICLNDDGGHCCLVNKWSTFLKARL 291
Cdd:cd11251   165 RTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTkQIHSMIARVCPNDTGGQRSLVNKWTTFLKARL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG 371
Cdd:cd11251   245 VCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQG 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 372 KMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLF 451
Cdd:cd11251   325 RIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGRYHVLF 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591854 452 LGTDRGTVQKVIVLPKDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11251   405 LGTDKGTVQKVVVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
30-517 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: 648.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  30 PRVRLSFKELKATGTAHFFNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIhWAASPQRIEECVLSGK 109
Cdd:cd11249     5 PRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIV-WPVSPSRRDECKWAGK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 110 DVNGECGNFVRLIQPWNRTHLYVCGTGAYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYA 189
Cdd:cd11249    84 DILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEDNIFRLEDSHFENGRGKSPYDPKLLTASLLIDGELYS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 190 GVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQS-PAVYARIGRI 268
Cdd:cd11249   164 GTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTgKATHARIGQL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 269 CLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADI 348
Cdd:cd11249   244 CKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMYSMTDI 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 349 RMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTpSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGA 428
Cdd:cd11249   324 RRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFG-GFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIIIKTDV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 429 PYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDD-QEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAV 507
Cdd:cd11249   403 DYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETwHDLEEVLLEEMTVFREPTAISAMELSTKQQQLYIGSAI 482
                         490
                  ....*....|
gi 2462591854 508 GVTHLSLHRC 517
Cdd:cd11249   483 GVSQLPLHRC 492
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
57-517 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: 625.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVCGTG 136
Cdd:cd11250    10 YDALLLDEERGRLFVGAKNYLASLSLDNISKQEKKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHLYACGTG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 137 AYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQ 216
Cdd:cd11250    90 AFHPTCAFVEVGQRMEDHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRPSLRTEQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 217 YNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSPAV-YARIGRICLNDDGGHCCLVNKWSTFLKARLVCSV 295
Cdd:cd11250   170 HDSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAGLGKQsYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCSV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 296 PGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPY 375
Cdd:cd11250   250 PGNEGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGKVPY 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 376 PRPGTCPGGTFTpSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTD 455
Cdd:cd11250   330 PRPGMCPSKTFG-SFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPYTFTQIAVDRVAAADGHYDVMFIGTD 408
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591854 456 RGTVQKVIVLPKDD-QEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11250   409 VGSVLKVISVPKGSwPSNEELLLEELHVFKDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
56-517 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: 590.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11252     9 DFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNRTHVYVCGT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 136 GAYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLG---KQTAM 212
Cdd:cd11252    89 GAFHPTCGYIELGTHKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLGptpDHHYI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 213 RTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQS-PAVYARIGRICLNDDGGHCCLVNKWSTFLKARL 291
Cdd:cd11252   169 RTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGSTSdKSVLSRVGRVCKNDVGGQRSLINKWTTFLKARL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG 371
Cdd:cd11252   249 VCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPDHRWVQYEG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 372 KMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLF 451
Cdd:cd11252   329 RIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVAAEDGQYDVMF 408
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591854 452 LGTDRGTVQKVIVLPKDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11252   409 LGTDIGTVLKVVSITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
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: 578.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNR 127
Cdd:cd11255     1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 128 THLYVCGTGAYNPMCTYVNRGRRAQdYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11255    81 THLLACGTGAFQPVCALINVGHRGE-HVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDQyNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSP--AVYARIGRICLNDDGGHCCLVNKWST 285
Cdd:cd11255   160 TRSPLRTET-DQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETAEDDdgAIHSRVGRLCANDAGGQRVLVNKWST 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 286 FLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQ 365
Cdd:cd11255   239 FIKARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 366 WMPFSGKMPYPRPGTCPGG-TFTPS--MKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDA 442
Cdd:cd11255   319 WGPYEGKVPYPRPGVCPSKiTAQPGraFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEA 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591854 443 ADGRYEVLFLGTDRGTVQKVIVLPKDDQEMEELML-EEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11255   399 EDGYYDVMFIGTDSGSVLKVIVLQKGNSAAGEEVTlEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
56-517 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: 554.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDvNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11253     9 DLHTMLLDEYQERLFVGGRDLLYSLSLERISANYKEIHWPSTQLQVEDCIMKGRD-KPECANYIRVLHHYNRTHLLACGT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 136 GAYNPMCTYVNRGRRAQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTD 215
Cdd:cd11253    88 GAFDPVCAFIRVGRGSEDHLFQLESDKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMNHLAHIRTE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 216 QYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQSP-AVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCS 294
Cdd:cd11253   168 HDDERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGGNhAIYTRVGRVCANDQGGQRMLVNKWSTFLKTRLICS 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 295 VPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMP 374
Cdd:cd11253   248 VPGPNGIDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVYEGKVP 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 375 YPRPGTCP----GGTFTpsmkSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVL 450
Cdd:cd11253   328 YPRPGSCAskvnGGHYG----TTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNLKQIAVDRVEAEDGQYDVL 403
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591854 451 FLGTDRGTVQKVI-VLPKDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 517
Cdd:cd11253   404 FIGTDNGIVLKVItIYNQETETMEEVILEELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
55-515 6.28e-161

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: 472.66  E-value: 6.28e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  55 TDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREpLIIHWAASPQRIEECVLSGKDVNgECGNFVRLIQPWNRTHLYVCG 134
Cdd:cd11235     1 LKYHTKLLHEDRSTLYVGARDRVYLVDLDSLYTE-QKVAWPSSPDDVDTCYLKGKSKD-DCRNFIKVLEKNSDDSLLVCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 135 TGAYNPMCTYvnrgrRAQDYIFYLEPErlESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRT 214
Cdd:cd11235    79 TNAFNPSCRN-----YNVETFELVGKE--ESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 215 DQYNSRWLNDPSFIHAELIPdsaerndDKLYFFFRERSAE-APQSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVC 293
Cdd:cd11235   152 EYHDSKWLNEPQFVGAFDIG-------DYVYFFFREIAVEyINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNC 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 294 SVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG-K 372
Cdd:cd11235   225 SVPGEFP--FYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVPDeR 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 373 MPYPRPGTCPGgtftpsmkSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGR-YEVLF 451
Cdd:cd11235   303 VPEPRPGTCVD--------DSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDVNYRFTKIAVDRVQAKLGQtYDVLF 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591854 452 LGTDRGTVQKVIVLPKDDQeMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSLH 515
Cdd:cd11235   375 VGTDRGIILKVVSLPEQGL-QASNILEEMPVGPPPEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema smart00630
semaphorin domain;
57-490 1.08e-153

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 452.21  E-value: 1.08e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854   57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVCGTG 136
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  137 AYNPMCTYVNRGrraqdyifyleperlesgkgkcpydpkldtasalineELYAGVYIDFMGTDAAIFRTLG----KQTA- 211
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------ELYVGTVADFSGSDPAIPRSLSvrrlKGTSg 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  212 --MRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEA-PQSPAVYARIGRICLNDDGGHCCLVNKWSTFLK 288
Cdd:smart00630 124 vsLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDdNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLK 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  289 ARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMP 368
Cdd:smart00630 197 ARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  369 FS-GKMPYPRPGTCPGGTFtpsmkSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVdAADGRY 447
Cdd:smart00630 275 YSrGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNY 348
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2462591854  448 EVLFLGTDRGTVQKVIVLPKDDQeMEELMLEEVEVFKDPAPVK 490
Cdd:smart00630 349 TVLFLGTSDGRILKVVLSESSSS-SESVVLEEISVFPDGSPIS 390
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
55-514 9.81e-137

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: 411.42  E-value: 9.81e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  55 TDYRILLKDEDHDRMYVGSKDYVLSLDLHDINRE-PLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVC 133
Cdd:cd11240     7 QNYSTLLLSEDEGTLYVGAREALFALNVSDISTElKDKIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYNSTHLYVC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 134 GTGAYNPMCTYVNrgrrAQDyiFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMR 213
Cdd:cd11240    87 GTFAFSPRCTYIN----LSD--FSLSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEGNVLK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 214 TDqYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAE-APQSPAVYARIGRICLNDDGGHCCLVNKWSTFLKA 289
Cdd:cd11240   161 TE-NTLRWLNEPAFVGSAHIResiDSPDGDDDKIYFFFTETAVEyDFYEKVTVSRVARVCKGDLGGQRTLQKKWTTFLKA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 290 RLVCSVPGEdgiETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPF 369
Cdd:cd11240   240 QLVCSQPDS---GLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSRY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 370 SGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQrRPLVVRTGAPYrlTTIAVDQVDAADGR-Y 447
Cdd:cd11240   317 TGPVPDPRPGACiTNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPIN-RPLLVKSGVNY--TRIAVHRVQALDGQtY 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591854 448 EVLFLGTDRGTVQKVIVLPKddqemEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 514
Cdd:cd11240   394 TVLFLGTEDGFLHKAVSLDG-----GMHIIEEIQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
50-514 6.38e-123

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: 375.64  E-value: 6.38e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  50 FLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDI-NREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRT 128
Cdd:cd11262     3 FRGPAQNYSTLLLEDESGRLYVGARGAIFSLNASDIsDSSALTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRFNST 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 129 HLYVCGTGAYNPMCTYVnrgrRAQDYIFylePERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTdAAIFRTLgK 208
Cdd:cd11262    83 HLYTCGTHAFRPLCAYI----DAERFTL---SSQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQYEFRSF-PDIRRNS-P 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 209 QTAMRTDQYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAEAPQSPAVY--ARIGRICLNDDGGHCCLVNKW 283
Cdd:cd11262   154 QPTLRTEEAPTRWLNDADFVGSVLVResmNSSVGDDDKIYFFFTERSQEETAYFSQSrvARVARVCKGDRGGKKTLQRKW 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 284 STFLKARLVCSVPgedGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPN 363
Cdd:cd11262   234 TSFLKARLVCYIP---EYEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 364 YQWMPFSGKMPYPRPGTCPGGTF-TPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYrlTTIAVDQVDA 442
Cdd:cd11262   311 SKWSRYTGKVPEPRPGSCITDEHrSQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIY--TKIAVQTVRG 388
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591854 443 ADGR-YEVLFLGTDRGTVQKVIVLpkddqEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 514
Cdd:cd11262   389 LDGRvYDVLFLGTDEGWLHKAVVI-----GSAVHIIEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
53-517 8.40e-110

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: 341.23  E-value: 8.40e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  53 NTTDYRILLkDEDHDRMYVGSKDYVLSLDLHDInREPLIIHWAASPQRIEECVLSGKDvNGECGNFVRLIQPWNRTHLYV 132
Cdd:cd11237     2 THSDHFKLL-DQDGNSLLVGARNAVYNISLSDL-TENQRIEWPSSDAHREMCLLKGKS-EDDCQNYIRVLAKKSAGRLLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 133 CGTGAYNPMCTYVNRgrraQDYIFYLEPERleSGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTlgkqtAM 212
Cdd:cd11237    79 CGTNAYKPLCREYTV----KDGGYRVEREF--DGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYRE-----PL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 213 RTDQYNSRWLNDPSFIHaelipdSAERNDdKLYFFFRERSAEAPQ-SPAVYARIGRICLNDDGGHCCLVNKWSTFLKARL 291
Cdd:cd11237   148 RTERYDLKQLNAPNFVS------SFAYGD-YVYFFFRETAVEYINcGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPGEdgIETHFDELQ---DVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMP 368
Cdd:cd11237   221 NCSVPGE--YPFYFNEIQstsDIVEGGYGGKSAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLP 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 369 FSG-KMPYPRPGTCpggtftpsMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVD-QVDAADGR 446
Cdd:cd11237   299 VPSnKVPEPRPGQC--------VNDSRTLPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQYRFTQIAVDpQVKALDGK 370
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591854 447 -YEVLFLGTDRGTVQKVIVLPKDDQEMEELMLE--EVEVFKDPAPVKTMTISSKRQQ--LYVASAVGVTHLSLHRC 517
Cdd:cd11237   371 yYDVLFIGTDDGKVLKAVNIASADTVDKVSPVVieETQVFPRGVPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
56-509 1.54e-103

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: 326.04  E-value: 1.54e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11259    19 NYSTLLLSEDKDVLYVGAREAVFALNALNISEKQHELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLNDTFLYVCGT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 136 GAYNPMCTYVNrgrrAQDYIFYlepERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLgKQTAMRTd 215
Cdd:cd11259    99 NAFQPTCDYLN----LTSFRLL---GKNEDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRNS-SQSPLRT- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 216 QYNSRWLNDPSFIHAELI---PDSAERNDDKLYFFFRERSAEAP-QSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARL 291
Cdd:cd11259   170 EYAIPWLNEPSFVFADVIradPDSPDGEDDKIYFFFTEVSVEYEfVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKARL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPGEDGIethFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFN-GPFAHK---EGPNYQWM 367
Cdd:cd11259   250 ICSIPDKNLV---FNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHTKWV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 368 PFSGKMPYPRPGTCPGGTFTPS-MKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYrlTTIAVDQVDAADGR 446
Cdd:cd11259   327 RYNGEVPKPRPGACINNEARAAnYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNY--TQIVVDRVQALDGT 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591854 447 -YEVLFLGTDRGTVQKVIVLPKDdqemeELMLEEVEVFKDPAPVKTMTISSK--RQQLYVASAVGV 509
Cdd:cd11259   405 iYDVMFISTDRGALHKAISLENE-----VHIIEETQLFPDFEPVQTLLLSSKkgRRFLYAGSNSGV 465
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
56-514 2.05e-99

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: 314.54  E-value: 2.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11260     8 NYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMNDSRMYVCGT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 136 GAYNPMCTYVNrgrrAQDYIFYLEpERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTlgKQTAMRTd 215
Cdd:cd11260    88 NAFSPTCDYIS----YDDGQLTLE-GKQEDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRS--SPITIRT- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 216 QYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAEAP-QSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARL 291
Cdd:cd11260   160 EFKSSWLNEPNFIYMAAVPeseDSPEGDDDKIYLFFSETAVEYDfYNKLVVSRVARVCKGDLGGQRTLQKKWTSFLKARL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPgedgiETHFDEL-QDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFN-----GPFAhKEGPNYQ 365
Cdd:cd11260   240 DCSVP-----EPSLPYViQDVFHVCHQDWRKCVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrgkfkTPVA-VETSFVK 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 366 WMPFSGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPyrLTTIAVDQVDAAD 444
Cdd:cd11260   314 WVMYSGELPVPRPGACiNNAARTSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGAL--FTRIVVDMVTAAD 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591854 445 G-RYEVLFLGTDRGTVQKVIvlpkdDQEMEELMLEEVEVFKDPAPVKTMTISSKrqQLYVASAVGVTHLSL 514
Cdd:cd11260   392 GqSYPVMFIGTANGYVLKAV-----NYDGEMHIIEEVQLFEPEEPIDILRLSQN--QLYAGSASGVVQMPV 455
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
67-466 6.24e-99

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: 313.68  E-value: 6.24e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  67 DRMYVGSKDYVLSLDLHDINREPLI----IHWAASPQRIEECVLSGKDvNGECGNFVRLIQPWNRTHLYVCGTGAYNPMC 142
Cdd:cd11242    19 RTLYIAARDHVYTVDLDASHTEEIVpskkLTWRSRQADVENCRMKGKH-KDECHNFIKVLVPRNDETLFVCGTNAFNPVC 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 143 TYVNrgrraqdyIFYLEPERLE-SGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRW 221
Cdd:cd11242    98 RNYR--------IDTLEQDGEEiSGMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYDSKW 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 222 LNDPSFIHAElipdsaeRNDDKLYFFFRERSAE-APQSPAVYARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGED 299
Cdd:cd11242   170 LKEPHFVHAV-------EYGDYVYFFFREIAVEyNTLGKVVFSRVARVCKNDMGGSPRVLEKqWTSFLKARLNCSVPGDS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 300 GIetHFDELQDVfvqqTQDVR---NPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPY 375
Cdd:cd11242   243 HF--YFDVLQAV----TDVIRingRPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPVPeDRVPK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 376 PRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTD 455
Cdd:cd11242   317 PRPGCCAGSGSAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYRLTQIAVDNAAGPYQNYTVVFLGSE 396
                         410
                  ....*....|.
gi 2462591854 456 RGTVQKVIVLP 466
Cdd:cd11242   397 AGTVLKFLARI 407
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
56-514 2.54e-96

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: 306.73  E-value: 2.54e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIhWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11258    11 NYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPIS-WEAPAEKKTECAQKGKSNQTECFNYIRFLQPYNQSHLYTCGT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 136 GAYNPMCTYVNRGRraqdyiFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTd 215
Cdd:cd11258    90 YAFQPKCAYINMLT------FTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMKT- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 216 QYNSRWLNDPSFIHAELIPDSAER---NDDKLYFFFRERSAEAP-QSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARL 291
Cdd:cd11258   163 EYLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDcDSEQVVARVARVCKGDLGGARTLQKKWTTFLKARL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPgedGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG 371
Cdd:cd11258   243 LCSIP---EWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRYTD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 372 KMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGApyRLTTIAVDQVDAADGR-YEV 449
Cdd:cd11258   320 PVPSPRPGSCiNNWHRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNS--NFTHVVWTRVLGLDGEtYSV 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591854 450 LFLGTDRGTVQKVIVLpkddqEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 514
Cdd:cd11258   398 LFIGTLDGWLIKAVSL-----GSWVHMIEELQVFDQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
53-514 1.44e-95

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: 304.14  E-value: 1.44e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHD--INREPLIIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHL 130
Cdd:cd11256     6 NVHNYDQLLLSPDETTLYVGARDNILALGIRTpgPIRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPVNGTHL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 131 YVCGTGAYNPMCTYVNrgrrAQDyiFYLEPERLE----SGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTL 206
Cdd:cd11256    86 YTCGTYAFSPACTYIE----LDH--FSLPPPNGTiitmDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 207 GKQTAMRTDQYNsRWLN-DPSFIHAELIPDsaernDDKLYFFFRERSAEAPQSPAVY-ARIGRICLNDDGGHCCLVNKWS 284
Cdd:cd11256   160 GTKVSLKTDGFL-RWLNaDAVFVASFNPQG-----DSKVYFFFEETAREFDFFEKLTvARVARVCKNDVGGEKLLQKKWT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 285 TFLKARLVCSVPGedgiETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSV--FRGSAVCVYSMADIRMVFNGPFAHKEGP 362
Cdd:cd11256   234 TFLKAQLTCSQQG----HFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLggRRSSAVCAYKLNDIEKVFNGKYKELNKE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 363 NYQWMPFSGKMPYPRPGTCPGGTFTpsmkstkdypDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYrlTTIAVDQVDA 442
Cdd:cd11256   310 SSRWTRYMGPVSDPRPGSCSGGKSS----------DKALNFMKDHFLMDEVVLPGAGRPLLVKSNVQY--TRIAVDSVQG 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591854 443 ADGR-YEVLFLGTDRGTVQKVIVLPKDDqemeELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 514
Cdd:cd11256   378 VSGHnYTVMFLGTDKGFLHKAVLMGGSE----SHIIEEIELLTPPEPVENLLLAANEGVVYIGYSAGVWRVPL 446
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
55-514 1.31e-93

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: 299.85  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  55 TDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPL--IIHWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNRTHLYV 132
Cdd:cd11257     8 SNYTALLLSKDGNMLYVGARETLFALSSNDISPTGEqqELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRLNSTHLFT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 133 CGTGAYNPMCTYVNRGRraqdyiFYLEPER-----LESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11257    88 CGTYAFSPICTYIVMTN------FSLERDEkgeplLEDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIYRSLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDqyNS-RWLNDPSFIHAELIPDS---AERNDDKLYFFFRERSAEAP-QSPAVYARIGRICLNDDGGHCCLVNK 282
Cdd:cd11257   162 SGTPLKTE--NSlNWLQDPAFVGSAYIQESlpkLVGDDDKIYFFFSETGKEFDfFENTIVSRIARVCKGDEGGERVLQKR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 283 WSTFLKARLVCSVPGeDGIEthFDELQDVFV--QQTQDVRNPVIYAVFTS--SGSVFRGSAVCVYSMADIRMVFNGPFAH 358
Cdd:cd11257   240 WTTFLKAQLLCSLPD-DGFP--FNVLQDVFVltPSPEDWKDTLFYGVFTSqwHKGTAGSSAVCVFTMDQVQRAFNGLYKE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 359 KEGPNYQWMPFSGKMPYPRPGTCPGGTFTP-SMKSTKDYPDEVINFMRSHPLMYQAVyplQRRPLVVRTGAPYrlTTIAV 437
Cdd:cd11257   317 VNRETQQWYTYTHPVPEPRPGACITNSARErKINSSLHMPDRVLNFVKDHFLMDGQV---RSQPLLLQPQVRY--TQIAV 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591854 438 DQVDAADGRYEVLFLGTDRGTVQKVIVLPKddqemEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 514
Cdd:cd11257   392 HRVKGLHKTYDVLFLGTDDGRLHKAVSVGP-----MVHIIEELQIFSEGQPVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
56-463 1.15e-92

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: 297.33  E-value: 1.15e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDedHDRMYVGSKDYVLSLDLHDINREPLI----IHWAASPQRIEECVLSGKDVNgECGNFVRLIQPWNRTHLY 131
Cdd:cd11269    10 DFQLMLKI--RDTLYIAGRDQVYTVNLNEVPKTEVTpsrkLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDEMVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 132 VCGTGAYNPMCTYVNRGRraqdyiFYLEPERLeSGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTA 211
Cdd:cd11269    87 VCGTNAFNPMCRYYRLST------LEYDGEEI-SGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 212 MRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAEAPQ-SPAVYARIGRICLNDDGGHCCLVNK-WSTFLKA 289
Cdd:cd11269   160 LRTIKYDSKWIKEPHFLHAI-------EYGNYVYFFFREIAVEHNNlGKAVYSRVARICKNDMGGSQRVLEKhWTSFLKA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 290 RLVCSVPGEDGIetHFDELQDVfvQQTQDVRN-PVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMP 368
Cdd:cd11269   233 RLNCSVPGDSFF--YFDVLQSI--TDIIEINGiPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 369 F-SGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRY 447
Cdd:cd11269   309 VpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTAIAVDHAAGPHQNY 388
                         410
                  ....*....|....*.
gi 2462591854 448 EVLFLGTDRGTVQKVI 463
Cdd:cd11269   389 TVIFVGSEAGVVLKIL 404
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
57-514 2.19e-87

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: 282.78  E-value: 2.19e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWA---ASPQRIEECVLSGKDVNGECGNFVRLIQPWN-RTHLYV 132
Cdd:cd11238     3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINDTGNNCARDeltLSPSDVSECVSKGKDEEYECRNHVRVIQPMGdGQTLYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 133 CGTGAYNPmctyvnrgrraQDYIFYL----EPERLES---GKGKCPYDPKLDTASALI---NEE----LYAGVYIDFMGT 198
Cdd:cd11238    83 CSTNAMNP-----------KDRVLDAnllhLPEYVPGpgnGIGKCPYDPDDNSTAVWVewgNPGdlpaLYSGTRTEFTKA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 199 DAAIFRT----LGKQ---TAMRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEAPQ-SPAVYARIGRICL 270
Cdd:cd11238   152 NTVIYRPplynNTKGrheSFMRTLKYDSKWLDEPNFVGSFDI-------GDYVYFFFRETAVEYINcGKVVYSRVARVCK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 271 NDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVF-VQQTQDVRnpvIYAVFTSSGSVFRGSAVCVYSMADIR 349
Cdd:cd11238   225 KDTGGKNVLRQNWTTFLKARLNCSISGE--FPFYFNEIQSVYkVPGRDDTL---FYATFTTSENGFTGSAVCVFTLSDIN 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 350 MVFN-GPFAHKEGPNYQWMPF-SGKMPYPRPGTCPGgtftpsmkSTKDYPDEVINFMRSHPLMYQAVYplQRRPLVVRtg 427
Cdd:cd11238   300 AAFDtGKFKEQASSSSAWLPVlSSEVPEPRPGTCVN--------DSATLSDTVLHFARTHPLMDDAVS--HGPPLLYL-- 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 428 APYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKvIVLPKDDQeMEELMLEEVEVFKDPAPVKTMTIsSKRQQLYVASAV 507
Cdd:cd11238   368 RDVVFTHLVVDKLRIDDQEYVVFYAGSNDGKVYK-IVHWKDAG-ESKSNLLDVFELTPGEPIRAMEL-LPGEFLYVASDH 444

                  ....*..
gi 2462591854 508 GVTHLSL 514
Cdd:cd11238   445 RVSQIDL 451
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
53-514 1.76e-84

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: 274.82  E-value: 1.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLIIH--WAASPQRIEECVLSGKDVNgECGNFVRLIQPWNRThL 130
Cdd:cd11241     5 YVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLS---LLQAvpWNSDEDTKRQCQSKGKSVE-ECQNYVRVLLVVGKN-L 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 131 YVCGTGAYNPMCTYVNRGRRAQ--DYIfyleperleSGKGKCPYDPKLDTASALINE-ELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11241    80 FTCGTYAFSPVCTIRKLSNLTQilDTI---------SGVARCPYSPAHNSTALISASgELYAGTVYDFSGRDPAIYRSLG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDQYNSRWLNDPSFIhaelipdSAERNDDKLYFFFRERSAEAPQS-PAVYARIGRICLNDDGGHCCLVNKWSTF 286
Cdd:cd11241   151 GKPPLRTAQYNSKWLNEPNFV-------GSYEIGNHTYFFFRENAVEHQDCgKTVYSRIARVCKNDIGGRFLLEDTWTTF 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 287 LKARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQW 366
Cdd:cd11241   224 MKARLNCSLPGE--FPFYYNEIQGTFYLPETD----LIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAW 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 367 MPFsgkmPYPRPGTCPGGTFTPSMKSTKDyPDEVINFMRsHPLMYQAVYPLQRRPLVVRTGApyRLTTIAVDQVDAADGR 446
Cdd:cd11241   298 LPT----PNPHPNFQCTTSIDRGQPANTT-ERDLQDAQK-YQLMAEVVQPVTKIPLVTMDDV--RFSKLAVDVVQGRGTQ 369
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591854 447 -YEVLFLGTDRGTVQKVIVLPKDDQEMEELMLEEVEVFKDpAPVKTMTISSKRQQLYVASAVGVTHLSL 514
Cdd:cd11241   370 lVHIFYVGTDYGTILKMYQPHRSQKSCTLEEIKILPAMKG-EPITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
69-469 2.42e-83

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: 272.86  E-value: 2.42e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  69 MYVGSKDYVLSLDLHDINREPLIIH----WAASPQRIEECVLSGKDvNGECGNFVRLIQPWNRTHLYVCGTGAYNPMCty 144
Cdd:cd11267    21 LYIGDRDNLYRVELDPTAGTEMRYHkkltWRSNKNDINVCRMKGKH-EGECRNFIKVLLLRDYGTLFVCGTNAFNPVC-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 145 vnrgrrAQDYIFYLEP--ERLeSGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWL 222
Cdd:cd11267    98 ------ANYSIDTLEPvgDNI-SGMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRTVKHDSKWF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 223 NDPSFIHA-ELIPdsaernddKLYFFFRERSAEAPQ-SPAVYARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEd 299
Cdd:cd11267   171 KEPYFVHAvEWGS--------HVYFFFREIAMEFNYlEKVVVSRVARVCKNDMGGSQRVLEKqWTSFLKARLNCSVPGD- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 300 gieTHFdelqdVF--VQQTQDVRN----PVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKM 373
Cdd:cd11267   242 ---SHF-----YFnvLQAVSDILNlggrPVVLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEEL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 374 -PYPRPGTCPGgtftPSMK--STKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVL 450
Cdd:cd11267   314 vPRPRPGCCAA----PGMRynSSSTLPDEVLNFVKTHPLMDEAVPSLGHAPWIVRTMTRYQLTHMVVDTEAGPHGNHTVV 389
                         410
                  ....*....|....*....
gi 2462591854 451 FLGTDRGTVQKVIVLPKDD 469
Cdd:cd11267   390 FLGSTRGTVLKFLIIPNAS 408
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
69-464 3.71e-83

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: 272.29  E-value: 3.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  69 MYVGSKDYVLSLDLHDINREPLI----IHWAASPQRIEECVLSGKDVNgECGNFVRLIQPWNRTHLYVCGTGAYNPMCTY 144
Cdd:cd11266    21 LYIAARDHIYTVDIDTSHTEEIYfskkLTWKSRQADVDTCRMKGKHKD-ECHNFIKVLLKRNDDTLFVCGTNAFNPSCRN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 145 VNrgrraQDYIFYLEPERleSGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLND 224
Cdd:cd11266   100 YK-----MDTLEFFGDEF--SGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 225 PSFIHAElipdsaeRNDDKLYFFFRERSAE-APQSPAVYARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIe 302
Cdd:cd11266   173 PYFVQAV-------DYGDYIYFFFREIAVEyNSMGKVVFPRVAQVCKNDMGGSQRVLEKqWTSFLKARLNCSVPGDSHF- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 303 tHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG-KMPYPRPGTC 381
Cdd:cd11266   245 -YFNILQAVTDVIHINGRD-VVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVPDeRVPKPRPGCC 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 382 PGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQK 461
Cdd:cd11266   323 AGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVDNAAGPYQNHTVVFLGSEKGIILK 402

                  ...
gi 2462591854 462 VIV 464
Cdd:cd11266   403 FLA 405
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
54-512 7.20e-80

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: 263.28  E-value: 7.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  54 TTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECVLSGKDvNGECGNFVRLIQPWNRTHLYVC 133
Cdd:cd11261    11 TYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERPRRIDWMVPEAHRQNCRKKGKK-EAECHNFIRILAIANASHLLTC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 134 GTGAYNPMCTYVNRGRraqdyifYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGK-QTAM 212
Cdd:cd11261    90 GTFAFDPKCGVIDVSS-------FQQVERLESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAVGRaEEWI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 213 RTDQYNSrWLNDPSFIHAELIPDSA---ERNDDKLYFFFRERSAEAPQ-SPAVYARIGRICLNDDGGHCCLVNKWSTFLK 288
Cdd:cd11261   163 RTETLPS-WLNAPAFVAAVFLSPAEwgdEDGDDEIYFFFTETAREYDSyERIKVPRVARVCAGDLGGRKTLQQRWTTFLK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 289 ARLVCSVPgEDGieTHFDELQDVFVQQTQDVRN-PVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 367
Cdd:cd11261   242 ADLLCPGP-EHG--RASSILQDVTTLRPLPGAGtPIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 368 PFS-GKMPYPRPGTCpggtFTPSMK-----STKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYrlTTIAVDQVD 441
Cdd:cd11261   319 PVMdSDVPQPRPGEC----ITNNMKllgfgSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAY--LRVAAHRVT 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591854 442 AADGR-YEVLFLGTDRGTVQKVIVLpkddqEMEELMLEEVEVFKDPAPVKTMTIssKRQQLYVASAVGVTHL 512
Cdd:cd11261   393 SLSGKeYDVLYLGTEDGHLHRAVRI-----GAQLSVLEDLALFPEPQPVENLQL--HHNWLLVGSDTEVTQI 457
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
56-463 1.60e-78

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: 259.66  E-value: 1.60e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDedHDRMYVGSKDYVLSLDLHDInREPLI----IHWAAspQRIEECVLSGKdVNGECGNFVRLIQPWNRTHLY 131
Cdd:cd11270    10 DFQRMLRI--NHMVYIAARDHVFAINLSAS-LERIVpqqkLTWKT--KDVEKCTVRGK-NSDECYNYIKVLVPRNDETLF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 132 VCGTGAYNPMCTYVNrgrraqdyIFYLEPERLE-SGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQT 210
Cdd:cd11270    84 ACGTNAFNPTCRNYK--------MSSLEQDGEEvIGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLGESS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 211 -AMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAEAPQSPAV-YARIGRICLNDDGGHCCLVNK-WSTFL 287
Cdd:cd11270   156 pVLRTVKYDSKWLREPHFLHAI-------EYGNYVYFFLSEIAVEYTTLGKVvFSRVARVCKNDNGGSPRVLERyWTSFL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 288 KARLVCSVPGEDGIetHFDELQDVFVQQTQDVRnPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 367
Cdd:cd11270   229 KARLNCSVPGDSFF--YFDVLQSLTNVMQINHR-PAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWT 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 368 PF-SGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGR 446
Cdd:cd11270   306 PVpDEAVPKPRPGSCAGDGPAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFKLTQIAVDTAAGPYKN 385
                         410
                  ....*....|....*..
gi 2462591854 447 YEVLFLGTDRGTVQKVI 463
Cdd:cd11270   386 YTVVFLGSENGHVLKVL 402
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
56-463 2.81e-78

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: 258.37  E-value: 2.81e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWAASPQRIEECVLSGKdVNGECGNFVRLIQPwNRTHLYVC 133
Cdd:cd11264     8 DFSQLALDLNRNQLIVGARNYLFRLSLHNVS---LIqaTEWGSDEDTRRSCQSKGK-TEEECQNYVRVLIV-YGKKVFTC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 134 GTGAYNPMCTYVNRGRRAQDYifylepERLeSGKGKCPYDPKlDTASALINE--ELYAGVYIDFMGTDAAIFRTLGKQTA 211
Cdd:cd11264    83 GTNAFSPVCTSRQVGNLSKVI------ERI-NGVARCPYDPR-HNSTAVITSrgELYAATVIDFSGRDPAIYRSLGSVPP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 212 MRTDQYNSRWLNDPSFIHAELIPDSAernddklYFFFRERSAEAPQSPAVYARIGRICLNDDGGHCCLVNKWSTFLKARL 291
Cdd:cd11264   155 LRTAQYNSKWLNEPNFIAAYDIGLFT-------YFFFRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFMKARL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG 371
Cdd:cd11264   228 NCSRPGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTAN 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 372 KMPYPRPGTCPggtftpsmkstKDYPDE-----VINFMRSHPLMYQAVYPLQRRPLVvrTGAPYRLTTIAVDQVDAADGR 446
Cdd:cd11264   302 PIPNFQCGTLS-----------DDSPNEnlterSLQDAQRLFLMNDVVQPVTVDPLV--TQDSVRFSKLVVDIVQGKDTL 368
                         410
                  ....*....|....*..
gi 2462591854 447 YEVLFLGTDRGTVQKVI 463
Cdd:cd11264   369 YHVMYIGTEYGTILKAL 385
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
53-503 3.60e-74

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: 247.25  E-value: 3.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWAASPQRIEECVLSGKDvNGECGNFVRLIQPwNRTHL 130
Cdd:cd11263     5 NAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLS---LIqaVEWECDEATKKACYSKGKS-KEECQNYIRVLLV-GGDRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 131 YVCGTGAYNPMCT--YVNRGRRAQDYIfyleperleSGKGKCPYDPKLDTASALINE-ELYAGVYIDFMGTDAAIFRTLG 207
Cdd:cd11263    80 FTCGTNAFTPICTnrTLNNLTEIHDQI---------SGMARCPYSPQHNSTALLTSSgELYAATAMDFPGRDPAIYRSLG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 208 KQTAMRTDQYNSRWLNDPSFIHAELIPDSAernddklYFFFRERSAEAPQSPAVYARIGRICLNDDGGHCCLVNKWSTFL 287
Cdd:cd11263   151 ILPPLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFM 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 288 KARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWM 367
Cdd:cd11263   224 KARLNCSRPGE--IPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 368 PFSGKMPYPRPGTCPGGTFtpsMKSTKDYPDEVINFMrshpLMYQAVYPLQRRPLVVRTGApyRLTTIAVDQVDAADGRY 447
Cdd:cd11263   298 PYPNPNPNFQCGTMDQGLY---VNLTERNLQDAQKFI----LMHEVVQPVTPVPYFMEDNS--RFSHVAVDVVQGKDMLF 368
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591854 448 EVLFLGTDRGTVQKviVLPKDDQEMEELMLEEVEVF--KDPAPVKTMTISSKRQQLYV 503
Cdd:cd11263   369 HIIYLATDYGTIKK--VLAPLNQSSSSCLLEEIELFpkRQREPIRSLQILHSQSVLFV 424
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
53-512 7.04e-74

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: 246.62  E-value: 7.04e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDInrEPL-IIHWAASPQRIEECVLSGKDVNgECGNFVRLIQPwNRTHLY 131
Cdd:cd11265     5 EVTSYSQMLFDVARNQVIVGARDNLYRLSLDGL--ELLeRASWPAAESKVALCQNKGQSEE-DCHNYVKVLLS-YGKQLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 132 VCGTGAYNPMCTYvnRGRRAQDYIfylepERLESGKGKCPYDPkLDTASALINE--ELYAGVYIDFMGTDAAIFRTLGKQ 209
Cdd:cd11265    81 ACGTNAFSPRCSW--REMENLTSV-----TEWDSGVAKCPYSP-HANITALLSSsgQLFVGSPTDFSGSDSAIYRTLGTS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 210 TA--MRTDQYNSRWLNDPSFIhaelipDSAErNDDKLYFFFRERSAEAPQ-SPAVYARIGRICLNDDGGHCCLV-NKWST 285
Cdd:cd11265   153 NKsfLRTKQYNSKWLNEPQFV------GSFE-TGNFVYFLFRESAVEYMNcGKVIYSRIARVCKNDVGGGTMLLkDNWTT 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 286 FLKARLVCSVPGEdgIETHFDELQDVFVQQTQDVrnpvIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQ 365
Cdd:cd11265   226 FLKARLNCSLPGE--YPFYFDEIQGMTYLPDEGI----LYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAA 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 366 WmpfsGKMPYP---RPGTCPGGTFTPSMKSTKdypdevinfmrsHPLMYQAVYPLQRRPLVVRTGApyRLTTIAVDQVDA 442
Cdd:cd11265   300 W----ERVNVNhrdHFNQCSSSSSSHLLESSR------------YQLMDEAVQPITLEPLHHAKLE--RFSHIAVDVIPT 361
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591854 443 A-DGRYEVLFLGTDRGTVQKVIVLPKDDQemeELMLEEVEVFKDPA-PVKTMTISSKRQQLYVASAVGVTHL 512
Cdd:cd11265   362 KiHQSVHVLYVATTGGLIKKISVLPRTQE---TCLVEIWQPLPTPDsPIKTMQYLKVTDSLYVGTELALMRI 430
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
308-496 1.54e-73

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: 236.40  E-value: 1.54e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 308 LQDVFVQQ--TQDVRNPVIYAVFTSS-GSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG 384
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 385 TFtpsmksTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGapYRLTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIV 464
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTG--VRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462591854 465 LPKDD-------QemeelmleeveVFKDPAPVKTMTISS 496
Cdd:pfam01403 153 VGSEEshiieeiQ-----------VFPEPQPVLNLLLSS 180
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
69-463 4.98e-69

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: 234.59  E-value: 4.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  69 MYVGSKDYVLSLDLHDINR-EPLI----IHWAAspQRIEECVLSGKdVNGECGNFVRLIQPWNRTHLYVCGTGAYNPMCT 143
Cdd:cd11268    21 LLVAARDHVFSFDLQAEEEgEGLVpnkyLTWRS--QDVENCAVRGK-LTDECYNYIRVLVPWDSQTLLACGTNSFSPVCR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 144 YVNRGRRAQdyifylEPERLeSGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLN 223
Cdd:cd11268    98 SYGITSLQQ------EGEEL-SGQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 224 DPSFIHaelipdsAERNDDKLYFFFRERSAEAPQSPAV-YARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGI 301
Cdd:cd11268   171 EPHFVQ-------ALEHGDHVYFFFREVSVEDARLGRVqFSRVARVCKRDMGGSPRALDRhWTSFLKLRLNCSVPGDSTF 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 302 etHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGT 380
Cdd:cd11268   244 --YFDVLQALTGPVNLHGRS-ALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVSeDRVPSPRPGS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 381 CPGGTFTPSMKSTKDYPDEVINFMRSHPLMYQAVYPLQRRPLVVRTGAPYrLTTIAVDQVDAADGRYEVLFLGTDRGTVQ 460
Cdd:cd11268   321 CAGVGGAALFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLTLTSRAL-LTQVAVDGMAGPHSNITVMFLGSNDGTVL 399

                  ...
gi 2462591854 461 KVI 463
Cdd:cd11268   400 KVL 402
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
57-514 9.26e-65

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: 221.26  E-value: 9.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  57 YRILLKDEDHDRMYVGSKDYVLSLDL---HDINREPLIIHWAASpqrieecvLSGKDVNGECGNFVRLIQPWNRThLYVC 133
Cdd:cd11243     4 YPVFFHEAGSSSVYVGGQGALYLLDFtgsAVIVKKIPDEKTEKD--------CKKRATLDDCENYITLIKKLDYR-LLVC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 134 GTGAYNPMCTYVNRGrraqdyifylEPERLESGKGKCPYDPKLDTASALINEELYAGvyIDFMGTDAAIFRTLGKQTAMR 213
Cdd:cd11243    75 GTNAGSPKCWFLVNQ----------TLVTLSADRGVAPFLPDENSLVLIEGNNVYST--ISGKKGNIPRFRRYGGKKELY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 214 TDqynSRWLNDPSFIHAELIPdSAERNDDKLYFFFRERSAEA-PQSPAVYARIGRICLNDDGGHCCL-VNKWSTFLKARL 291
Cdd:cd11243   143 TS---DTVMQKPQFVKATLLP-EDEQYQDKIYYFFREDNEDKgPEAEPNISRVARLCKEDQGGTSSLsTSKWSTFLKARL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 292 VCSVPGEDGietHFDELQDVFVQQTQDVRNPVIYAVFTSSgsvFRGSAVCVYSMADIRMVFNgpfahkegpNYQWMPFSG 371
Cdd:cd11243   219 VCGDPATPM---NFNRLQDVFLLPKEEWREAVVYGVFSNT---WGSSAVCSYSLGDIDKVFR---------TSSLKGYSG 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 372 KMPYPRPGTC-PGGTFTPSmkstkdypdEVINFMRSHPLMYQAVYPLQRRPLVVRTGApYRLTTIAVDQVDAADGR-YEV 449
Cdd:cd11243   284 SLPNPRPGTCvPPEQTHPS---------ETFSFADEHPELDDRIEPDEPRKLPVFQNK-DHYQKVVVDEVRASDGVsYDV 353
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591854 450 LFLGTDRGTVQKVIVLPKDDqemeeLMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVTHLSL 514
Cdd:cd11243   354 LYLATDKGKIHKVVESKGQT-----HNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
56-510 3.99e-51

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: 183.56  E-value: 3.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLII---HWAASPQRIEECVLSGKDVNGECGNFVRLIQPWNR-THLY 131
Cdd:cd09295     1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLSCIspeLNFGFNEDQKAFCPLRRGKWTECINYIKVLQQKGDlDILA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 132 VCGTGAYNPMCTYVNrgrraQDYIFYLEPERLESGKGKCPYDPKLDTASALINEELYAGVYIDFM-GTDAAIFRTLGKQT 210
Cdd:cd09295    81 VCGSNAAQPSCGSYR-----LDVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNVH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 211 AMRTDQYNSRWLNDPSFIHAELIPDSaernDDKLYFFFRERSAEAPQSPAVY-ARIGRICLNDDGGHCCLVNKWSTFLKA 289
Cdd:cd09295   156 YLRIVVDSSTGLDEITFVYAFVSGDD----DDEVYFFFRQEPVEYLKKGMVYvPRIARVCKLDVGGCHRLKKKLTSFLKA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 290 RLVCSVPGEDgieTHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPfahkegpnyqwmpf 369
Cdd:cd09295   232 DLNCSRPQSG---FAFNLLQDATGDTKNLIQD-VKFAIFSSCLNKSVESAVCAYLFTDINNVFDDP-------------- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 370 sgkmpyprpgtcpggtftpsmkstkdypdevinfmrshplmyqaVYPLQRRPLVVRTGAPYRLTTIAVDQVDAADGRYEV 449
Cdd:cd09295   294 --------------------------------------------VEAINNRPLYAHQNQRSRLTSIAVDATKQKSVGYQV 329
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591854 450 LFLGTDRGTVQKVIVlpkDDQEMEELMLEEVEVFKDPAPVKTMTISSKRQQLYVASAVGVT 510
Cdd:cd09295   330 VFLGLKLGSLGKALA---FFFLYKGHIIEEWKVFKDSSRITNLDLSRPPLYLYVGSESGVL 387
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
577-666 2.28e-38

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: 137.48  E-value: 2.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 577 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKH 656
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|
gi 2462591854 657 VVTRVQLHVL 666
Cdd:cd05871    81 TLVKIRLHVI 90
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
587-668 6.44e-13

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: 64.79  E-value: 6.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 587 AGSAAFLECQPRSPQATVKWLFQRDPGDRRReirAEDRFLRTEQGLLLRALQLSDRGLYSCTATENNFKHVVTRVQLHVL 666
Cdd:cd04979    10 EGDTVILSCSVKSNNAPVTWIHNGKKVPRYR---SPRLVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSVTLHVL 86

                  ..
gi 2462591854 667 GR 668
Cdd:cd04979    87 ER 88
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
447-557 5.27e-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: 56.09  E-value: 5.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 447 YEVLFLGTDRGTVQKVIVlpkDDQEMEELMLEEVEVFKDPAPV-KTMTISSKRQQLYVASAVGVTHLSLHRCQAYgAACA 525
Cdd:cd11272   406 YSVVFVGTKSGKLKKIRA---DGPPHGGVQYEMVSVFKDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQY-TTCG 481
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462591854 526 DCCLARDPYCAWdgqaCSRYTASSKR-RSRRQD 557
Cdd:cd11272   482 ECLSSGDPHCGW----CALHNMCSRRdKCQRAW 510
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
516-553 3.42e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 3.42e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462591854  516 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 553
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
581-665 6.84e-07

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: 47.50  E-value: 6.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854  581 SVQYGVAGSAAFLECQPRS-PQATVKWLFQRDpgdrrREIRAEDRFLRTEQG----LLLRALQLSDRGLYSCTATeNNFK 655
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGsPPPEVTWYKQGG-----KLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAAT-NSSG 75
                           90
                   ....*....|
gi 2462591854  656 HVVTRVQLHV 665
Cdd:smart00410  76 SASSGTTLTV 85
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
245-467 9.52e-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: 51.95  E-value: 9.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 245 YFFFRERSaEAPQSPAVYARIGRICLNDdgghcclvNKWSTFLKARLVCSvpGEDGieTHFDELQDVFV---------QQ 315
Cdd:cd11236   196 YFVTVQRK-SVDDESPYISRLVRVCQSD--------SNYYSYTEVPLQCT--GGDG--TNYNLLQAAYVgkagsdlarSL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 316 TQDVRNPVIYAVF----TSSGSVFRGSAVCVYSMADIRMVFNgpfahkegpnyqwmpfsgkmpyprpgtcpggtftpsmk 391
Cdd:cd11236   263 GISTDDDVLFGVFskskGPSAEPSSKSALCVFSMKDIEAAFN-------------------------------------- 304
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591854 392 stkdypdevinfmRSHPLmyQAVYPLQRRPLVVRTgapyRLTTIAVDQVDaadgRYEVLFLGTDRGTVQKVIVLPK 467
Cdd:cd11236   305 -------------DNCPL--GGGVPITTSAVLSDS----LLTSVAVTTTR----NHTVAFLGTSDGQLKKVVLESS 357
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
236-470 5.97e-06

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


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 49.54  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 236 SAERNDDKLYFFFRERSAEAPQSPAVYarIGRICLNDdgghcclvNKWSTFLKARLVCsvpgEDGIETHFDELQDVFVQQ 315
Cdd:cd11245   188 YAFADNGYIYFLFSRRPGTADSTKRTY--ISRLCEND--------HHYYSYVELPLNC----TVNQENTYNLVQAAYLAK 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 316 TQDVRN-PVIYAVFTSSGSVFRG----SAVCVYSMADIRMVFN--------GPFAHKEGPNYQWMPFSGK-----MPYPR 377
Cdd:cd11245   254 PGKVLNgKVLFGVFSADEASTAApdgrSALCMYPLSSVDARFErtrescytGEGLEDDKPETAYIEYNVKsicktLPDKN 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 378 PGTCP-GGTFTPSmkstkdypdevinfmrshPLMYQavYPLQRRPLVVRtgaPYRLTTIAVdqvdAADGRYEVLFLGTDR 456
Cdd:cd11245   334 VKAYPcGAEHTPS------------------PLASR--YPLAAKPILTR---NDMLTAVAV----AVENGHTIAFLGDSG 386
                         250
                  ....*....|....
gi 2462591854 457 GTVQKVIVLPKDDQ 470
Cdd:cd11245   387 GQLHKVYLDPNHTD 400
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
593-665 2.44e-05

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 43.15  E-value: 2.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591854 593 LECQPR-SPQATVKWLFQRDPGDRRREiraedRFLRTEQGLLLRALQLSDRGLYSCTATeNNFKHVVTRVQLHV 665
Cdd:cd20978    21 LPCQVTgVPQPKITWLHNGKPLQGPME-----RATVEDGTLTIINVQPEDTGYYGCVAT-NEIGDIYTETLLHV 88
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
591-650 6.85e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.55  E-value: 6.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591854 591 AFLECQPR-SPQATVKWLfqRDPGDRRREIRAEDRFLRTEQGLLLRALQLSDRGLYSCTAT 650
Cdd:cd00096     1 VTLTCSASgNPPPTITWY--KNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
581-650 1.20e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.01  E-value: 1.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591854 581 SVQYGVAGSAAFLECQPR-SPQATVKWLFqrdPGDRRREIRAEDRFLRTEQGLL-LRALQLSDRGLYSCTAT 650
Cdd:pfam13927   9 SSVTVREGETVTLTCEATgSPPPTITWYK---NGEPISSGSTRSRSLSGSNSTLtISNVTRSDAGTYTCVAS 77
Sema_plexin_B1 cd11275
The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the ...
245-469 2.01e-04

The Sema domain, a protein interacting module, of Plexin B1; Plexin B1 serves as the Semaphorin 4D receptor and functions as a regulator of developing neurons and a tumor suppressor protein for melanoma. The Sema4D-plexin B signaling complex regulates dendritic and axonal complexity. The activation of Plexin B1 by Sema4D produces an acute collapse of axonal growth cones in hippocampal and retinal neurons over the early stages of neurite outgrowth and promotes branching and complexity. As a tumor suppressor, plexin B1 abrogates activation of the oncogenic receptor, c-Met, by its ligand, hepatocyte growth factor (HGF), in melanoma. Furthermore, plexin B1 suppresses integrin-dependent migration and activation of pp125FAK and inhibits Rho activity. Plexin B1 is highly expressed in endothelial cells and its activation by Sema4D elicits a potent proangiogenic response. 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: 200536 [Multi-domain]  Cd Length: 461  Bit Score: 44.57  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 245 YFFFRERSAEApQSPAVYARIGRICLNDdgghcclvNKWSTFLKARLVCsvpgeDGIETHFDELQDVFVQQTQ------- 317
Cdd:cd11275   209 YFLFYRRDLKS-QSREYKTYISRICLDD--------SHYYSYVELPLLC-----QSKANTYSLLQAAYVTQPGerlaqgq 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 318 -DVRNPVIYAVFTS----SGSVFRGSAVCVYSMADIRMVFN---GPFAHKEG----------------PNYQWMPFSGKM 373
Cdd:cd11275   275 lDTDGEVLFAAFSAwqasSGKLSEESALCAYPMDEVDRLTNwtrDVCYTRDGkaedgtevayieydvsSNCVQLPADTLD 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 374 PYPrpgtCpGGTFTPSMKSTKDypdevinfmrshplmyqavyPLQRRPLVVRTGApyRLTTIAVDqvdaADGRYEVLFLG 453
Cdd:cd11275   355 AYP----C-GSDHTPSPMASRV--------------------PLEATPLLEWTEI--RLTAVAVN----VEDGHTIAFLG 403
                         250
                  ....*....|....*.
gi 2462591854 454 TDRGTVQKVIVLPKDD 469
Cdd:cd11275   404 DSRGRLHKVYLGAGGD 419
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
241-462 2.06e-04

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


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 44.38  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 241 DDKLYFFFRERSAEAPQSPAVYarIGRICLNDDGGHcclvnkwsTFLKARLVCSVPgedgiETHFDELQDVFV------- 313
Cdd:cd11276   198 DNNYVYFLFNQQLGHPDKNRTL--IARLCENDHHYY--------SYTEMDLNCRDG-----ANAYNKCQAAYVstpgkel 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 314 -QQTQDVR--NPVIYAVFTSSGSVFRGSAVCVYSMADI--RMVFNGPFAH---KEGPNYQWMPFSGKMPyprpgtCPGGT 385
Cdd:cd11276   263 aQNYGNSIlsDKVLFAVFSRDEKDSGESALCMFPLKSInaKMEANREACYtgtIDDRDVFYKPFHSQKD------IICGS 336
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591854 386 FTPsmKSTKDYP--DEvinFMRShPLMYQAVYPLqRRPLVVRTGApyRLTTIAVdqvdAADGRYEVLFLGTDRGTVQKV 462
Cdd:cd11276   337 HQQ--KNSKSFPcgSE---HLPY-PLGSRDELAL-TAPVLQRGGL--NLTAVTV----AVENGHTVAFLGTSDGRILKV 402
I-set pfam07679
Immunoglobulin I-set domain;
588-665 3.33e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 40.32  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 588 GSAAFLECQPR-SPQATVKWLFQRdpgdrrREIRAEDRFLRTEQG----LLLRALQLSDRGLYSCTATeNNFKHVVTRVQ 662
Cdd:pfam07679  15 GESARFTCTVTgTPDPEVSWFKDG------QPLRSSDRFKVTYEGgtytLTISNVQPDDSGKYTCVAT-NSAGEAEASAE 87

                  ...
gi 2462591854 663 LHV 665
Cdd:pfam07679  88 LTV 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
576-654 4.18e-04

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 39.75  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 576 KNAVESVQYGVAGSAAFLECQPR-SPQATVKWLFqrdpGDRRreIRAEDRFLRTEQG-LLLRALQLSDRGLYSCTAtENN 653
Cdd:cd04969     5 LNPVKKKILAAKGGDVIIECKPKaSPKPTISWSK----GTEL--LTNSSRICILPDGsLKIKNVTKSDEGKYTCFA-VNF 77

                  .
gi 2462591854 654 F 654
Cdd:cd04969    78 F 78
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
588-666 4.98e-04

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: 39.80  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 588 GSAAFLECQPRSPQATVKWLFQRDPgdrrreIRAED-RFLRTEQGLLLRALQLSDRGLYSCTATEN-NFKHVVTRVQLHV 665
Cdd:cd05873    11 GGNAELKCSPKSNLARVVWKFQGKV------LKAESpKYGLYGDGLLIFNASEADAGRYQCLSVEKsKAKTFFQTVAKYV 84

                  .
gi 2462591854 666 L 666
Cdd:cd05873    85 L 85
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
516-557 1.16e-03

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 37.69  E-value: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462591854 516 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRSRRQD 557
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRRSACGAPEGNCEE 43
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
586-666 9.79e-03

Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are composed of the immunoglobulin (Ig)-like domain of Sema4B and similar proteins. Sema4B is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4B has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4B has been shown to preferentially regulate the development of the postsynaptic specialization at the glutamatergic synapses. This cytoplasmic domain includes a PDZ-binding motif upon which the synaptic localization of Sem4B is dependent. Sema4B is a ligand of CLCP1. CLCP1 was identified in an expression profiling analysis, which compared a highly metastic lung cancer subline with its low metastic parental line. Sema4B was shown to promote CLCP1 endocytosis and their interaction is a potential target for therapeutic intervention of metastasis.


Pssm-ID: 409456  Cd Length: 86  Bit Score: 35.88  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591854 586 VAGSAAFLECQPRSPQATVKWLFqrdPGdrrREIRAEDRFLR-TEQGLLLRALQLSDRGLYSCTATENNFKHVVTRVQLH 664
Cdd:cd05872     9 VAGADVVLPCQLRSNLASPVWLF---NG---TPLNAQFSYLRlGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYSLN 82

                  ..
gi 2462591854 665 VL 666
Cdd:cd05872    83 VV 84
 
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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