NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|341942018|sp|O88632|]
View 

RecName: Full=Semaphorin-3F; AltName: Full=Semaphorin IV; Short=Sema IV; Flags: Precursor

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
48-548 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: 1011.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNR 127
Cdd:cd11254    1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 128 THLYVCGTGAYNPMCTYVNRGRRAQalpwtqmqvvrgrgsratdgadrptptaprqDYIFYLEPEKLESGKGKCPYDPKL 207
Cdd:cd11254   81 THLYVCGTGAYNPVCAYINRGRRAE-------------------------------DYMFRLEPDKLESGKGKCPYDPKQ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 208 DTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAP 287
Cdd:cd11254  130 DSVSALINGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAP 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 288 QNPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFR 367
Cdd:cd11254  210 QSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFK 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 368 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYP 447
Cdd:cd11254  290 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYP 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 448 LQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELMLEEVEVFKEPAPVKTMTISS 527
Cdd:cd11254  370 VHRRPLVVRTNVNYRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISS 449
                        490       500
                 ....*....|....*....|.
gi 341942018 528 KRQQLYVASAVGVTHLSLHRC 548
Cdd:cd11254  450 KRQQLYVSSAVGVTHLSLHRC 470
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
608-697 1.30e-37

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: 135.55  E-value: 1.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 608 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPSDRRREIRAEDRFLRTEQGLLLRALQLGDRGLYSCTATENNFKH 687
Cdd:cd05871    1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                         90
                 ....*....|
gi 341942018 688 IVTRVQLHVL 697
Cdd:cd05871   81 TLVKIRLHVI 90
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
547-584 2.55e-07

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.92  E-value: 2.55e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 341942018   547 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 584
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 ...
48-548 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: 1011.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNR 127
Cdd:cd11254    1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 128 THLYVCGTGAYNPMCTYVNRGRRAQalpwtqmqvvrgrgsratdgadrptptaprqDYIFYLEPEKLESGKGKCPYDPKL 207
Cdd:cd11254   81 THLYVCGTGAYNPVCAYINRGRRAE-------------------------------DYMFRLEPDKLESGKGKCPYDPKQ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 208 DTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAP 287
Cdd:cd11254  130 DSVSALINGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAP 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 288 QNPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFR 367
Cdd:cd11254  210 QSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFK 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 368 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYP 447
Cdd:cd11254  290 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYP 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 448 LQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELMLEEVEVFKEPAPVKTMTISS 527
Cdd:cd11254  370 VHRRPLVVRTNVNYRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISS 449
                        490       500
                 ....*....|....*....|.
gi 341942018 528 KRQQLYVASAVGVTHLSLHRC 548
Cdd:cd11254  450 KRQQLYVSSAVGVTHLSLHRC 470
Sema smart00630
semaphorin domain;
57-521 1.24e-148

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 440.27  E-value: 1.24e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018    57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGTG 136
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   137 AYNPMCTYVNRGrraqalpwtqmqvvrgrgsratdgadrptptaprqdyifylepeklesgkgkcpydpkldtasaline 216
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   217 ELYAGVYIDFMGTDAAIFRTLG----KQTA---MRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEA-PQ 288
Cdd:smart00630  93 ELYVGTVADFSGSDPAIPRSLSvrrlKGTSgvsLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDdNC 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   289 NPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRG 368
Cdd:smart00630 166 GKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPG 243
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   369 SAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFtpsmkSTKDYPDEVINFMRTHPLMYQAVYP 447
Cdd:smart00630 244 SAVCAFSLSDINAVFNGPFKECETSTSQWLPYSrGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQP 318
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341942018   448 LQRRPLVVRTGAPYRLTTVAVDQVdAADGRYEVLFLGTDRGTVQKVIVLPKDDQeVEELMLEEVEVFKEPAPVK 521
Cdd:smart00630 319 LTGRPLFVKTDSNYLLTSIAVDRV-ATDGNYTVLFLGTSDGRILKVVLSESSSS-SESVVLEEISVFPDGSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
339-527 2.49e-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: 2.49e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  339 LQDVFVQQ--TQDVRNPVIYAVFTSS-GSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG 415
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  416 TFtpsmksTKDYPDEVINFMRTHPLMYQAVYPLQRRPLVVRTGapYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIV 495
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTG--VRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341942018  496 LPKDD-------QeveelmleeveVFKEPAPVKTMTISS 527
Cdd:pfam01403 153 VGSEEshiieeiQ-----------VFPEPQPVLNLLLSS 180
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
608-697 1.30e-37

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: 135.55  E-value: 1.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 608 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPSDRRREIRAEDRFLRTEQGLLLRALQLGDRGLYSCTATENNFKH 687
Cdd:cd05871    1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                         90
                 ....*....|
gi 341942018 688 IVTRVQLHVL 697
Cdd:cd05871   81 TLVKIRLHVI 90
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
547-584 2.55e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.92  E-value: 2.55e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 341942018   547 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 584
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
612-696 1.57e-06

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: 46.73  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   612 SVQYGVAGSAAFLECQPRS-PQATVKWLFQRDpsdrrREIRAEDRFLRTEQG----LLLRALQLGDRGLYSCTATENNFK 686
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGsPPPEVTWYKQGG-----KLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGS 76
                           90
                   ....*....|
gi 341942018   687 HIVTrVQLHV 696
Cdd:smart00410  77 ASSG-TTLTV 85
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
547-588 8.04e-04

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: 38.07  E-value: 8.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 341942018  547 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRSRRQD 588
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRRSACGAPEGNCEE 43
I-set pfam07679
Immunoglobulin I-set domain;
619-696 9.24e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.78  E-value: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  619 GSAAFLECQPR-SPQATVKWLFQRDP--SDRRREIRAEDrflrTEQGLLLRALQLGDRGLYSCTATeNNFKHIVTRVQLH 695
Cdd:pfam07679  15 GESARFTCTVTgTPDPEVSWFKDGQPlrSSDRFKVTYEG----GTYTLTISNVQPDDSGKYTCVAT-NSAGEAEASAELT 89

                  .
gi 341942018  696 V 696
Cdd:pfam07679  90 V 90
 
Name Accession Description Interval E-value
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
48-548 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: 1011.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNR 127
Cdd:cd11254    1 FSFLLNTSDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 128 THLYVCGTGAYNPMCTYVNRGRRAQalpwtqmqvvrgrgsratdgadrptptaprqDYIFYLEPEKLESGKGKCPYDPKL 207
Cdd:cd11254   81 THLYVCGTGAYNPVCAYINRGRRAE-------------------------------DYMFRLEPDKLESGKGKCPYDPKQ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 208 DTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAP 287
Cdd:cd11254  130 DSVSALINGELYAGVYIDFMGTDAAIFRTMGKQPAMRTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAP 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 288 QNPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFR 367
Cdd:cd11254  210 QSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLVCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFK 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 368 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYP 447
Cdd:cd11254  290 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGKIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYP 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 448 LQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELMLEEVEVFKEPAPVKTMTISS 527
Cdd:cd11254  370 VHRRPLVVRTNVNYRFTTIAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISS 449
                        490       500
                 ....*....|....*....|.
gi 341942018 528 KRQQLYVASAVGVTHLSLHRC 548
Cdd:cd11254  450 KRQQLYVSSAVGVTHLSLHRC 470
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
48-548 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: 862.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNR 127
Cdd:cd11239    1 FLGSMNSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPKKIYWPASPERIEECKMAGKDPNTECANFVRVLQPYNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 128 THLYVCGTGAYNPMCTYVNRGRRAqalpwtqmqvvrgrgsratdgadrptptaprQDYIFYLEPEKLESGKGKCPYDPKL 207
Cdd:cd11239   81 THLYACGTGAFHPICAFINVGRRL-------------------------------EDPIFKLDDSSLESGRGKCPFDPNQ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 208 DTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAP 287
Cdd:cd11239  130 PFASVLIDGELYSGTAIDFMGRDAAIFRSLGHRHYIRTEQYDSRWLNEPKFVGAYLIPDSDNPDDDKVYFFFREKAVEAE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 288 QN-PAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVF 366
Cdd:cd11239  210 GSgKAIYSRVGRICKNDVGGQRSLVNKWSTFLKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVF 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 367 RGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVY 446
Cdd:cd11239  290 KGSAVCVYSMADIRAAFNGPFAHKEGPNYQWVEYQGKVPYPRPGTCPSKTYGPLYKSTKDFPDDVISFARSHPLMYNPVY 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 447 PLQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELMLEEVEVFKEPAPVKTMTIS 526
Cdd:cd11239  370 PLHGRPLLIRTNVPYRLTQIAVDRVEAEDGQYDVLFIGTDSGTVLKVVSLPKENWEMEEVILEELQVFKHPSPITSMEIS 449
                        490       500
                 ....*....|....*....|..
gi 341942018 527 SKRQQLYVASAVGVTHLSLHRC 548
Cdd:cd11239  450 SKRQQLYVGSAEGVVQLPLHRC 471
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
53-548 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: 686.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYV 132
Cdd:cd11251    6 RPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNRTHLYV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 133 CGTGAYNPMCTYVNRGRRAQalpwtqmqvvrgrgsratdgadrptptaprqDYIFYLEpEKLESGKGKCPYDPKLDTASA 212
Cdd:cd11251   86 CGSGAFSPVCVYVNRGRRSE-------------------------------EQVFHID-SKAESGKGRCSFNPNVNTVSV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 213 LINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQNP-A 291
Cdd:cd11251  134 MINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTkQ 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 292 VYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAV 371
Cdd:cd11251  214 IHSMIARVCPNDTGGQRSLVNKWTTFLKARLVCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAV 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 372 CVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPLQRR 451
Cdd:cd11251  294 CVYHMSDIQTVFNGPFAHKEGPNHQLIAYQGRIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRR 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 452 PLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELMLEEVEVFKEPAPVKTMTISSKRQQ 531
Cdd:cd11251  374 PLLVRTGTDYKYTKIAVDRVNAADGRYHVLFLGTDKGTVQKVVVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQ 453
                        490
                 ....*....|....*..
gi 341942018 532 LYVASAVGVTHLSLHRC 548
Cdd:cd11251  454 LYVSSEEGISQVSLHRC 470
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
30-548 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: 627.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  30 PRVRLSFKELKATGTAHFFNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIhWAASPQRIEECILSGK 109
Cdd:cd11249    5 PRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNIKDFQKIV-WPVSPSRRDECKWAGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 110 DGNGECGNFVRLIQPWNRTHLYVCGTGAYNPMCTYVNRGRRAQalpwtqmqvvrgrgsratdgadrptptaprqDYIFYL 189
Cdd:cd11249   84 DILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPE-------------------------------DNIFRL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 190 EPEKLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAE 269
Cdd:cd11249  133 EDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDN 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 270 RNDDKLYFFFRERSAEAPQ-NPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQ 348
Cdd:cd11249  213 PEDDKIYFFFRENAIDGEHtGKATHARIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSK 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 349 DVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTpSMKSTKDYP 428
Cdd:cd11249  293 DPKNPIVYAVFTTSSNIFKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFG-GFDSTKDLP 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 429 DEVINFMRTHPLMYQAVYPLQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDD-QEVEELM 507
Cdd:cd11249  372 DDVITFARSHPAMYNPVFPINNRPIIIKTDVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETwHDLEEVL 451
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 341942018 508 LEEVEVFKEPAPVKTMTISSKRQQLYVASAVGVTHLSLHRC 548
Cdd:cd11249  452 LEEMTVFREPTAISAMELSTKQQQLYIGSAIGVSQLPLHRC 492
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
57-548 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: 601.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGTG 136
Cdd:cd11250   10 YDALLLDEERGRLFVGAKNYLASLSLDNISKQEKKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHLYACGTG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 137 AYNPMCTYVNRGRRAqalpwtqmqvvrgrgsratdgadrptptaprQDYIFYLEPEKLESGKGKCPYDPKLDTASALINE 216
Cdd:cd11250   90 AFHPTCAFVEVGQRM-------------------------------EDHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 217 ELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQNPAV-YAR 295
Cdd:cd11250  139 ELYSGVATDLMGRDFTIFRSLGQRPSLRTEQHDSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAGLGKQsYSR 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 296 IGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYS 375
Cdd:cd11250  219 IGQICRNDMGGQRSLVNKWTTFLKARLVCSVPGNEGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYT 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 376 MADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTpSMKSTKDYPDEVINFMRTHPLMYQAVYPLQRRPLVV 455
Cdd:cd11250  299 MNDVRRAFLGPFAHKEGPNYQWVSYQGKVPYPRPGMCPSKTFG-SFESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFL 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 456 RTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDD-QEVEELMLEEVEVFKEPAPVKTMTISSKRQQLYV 534
Cdd:cd11250  378 RTGIPYTFTQIAVDRVAAADGHYDVMFIGTDVGSVLKVISVPKGSwPSNEELLLEELHVFKDSSPITSMQISSKRQQLYV 457
                        490
                 ....*....|....
gi 341942018 535 ASAVGVTHLSLHRC 548
Cdd:cd11250  458 GSRSGVSQLPLHRC 471
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
56-548 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: 578.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11252    9 DFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNRTHVYVCGT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 136 GAYNPMCTYVNRGrraqalpwtqmqvvrgrgsratdgadrptptAPRQDYIFYLEPEKLESGKGKCPYDPKLDTASALIN 215
Cdd:cd11252   89 GAFHPTCGYIELG-------------------------------THKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 216 EELYAGVYIDFMGTDAAIFRTLG---KQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAP-QNPA 291
Cdd:cd11252  138 EYLYAGTASDFLGKDTTFTRSLGptpDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGStSDKS 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 292 VYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAV 371
Cdd:cd11252  218 VLSRVGRVCKNDVGGQRSLINKWTTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAV 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 372 CVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPLQRR 451
Cdd:cd11252  298 CVYSMADIRAVFNGPYAHKESPDHRWVQYEGRIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGG 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 452 PLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELMLEEVEVFKEPAPVKTMTISSKRQQ 531
Cdd:cd11252  378 PVFTRINVDYRLTQIVVDHVAAEDGQYDVMFLGTDIGTVLKVVSITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQQ 457
                        490
                 ....*....|....*..
gi 341942018 532 LYVASAVGVTHLSLHRC 548
Cdd:cd11252  458 LYIGSRDGLVQLSLHRC 474
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
48-548 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: 568.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  48 FNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNR 127
Cdd:cd11255    1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 128 THLYVCGTGAYNPMCTYVNRGrraqalpwtqmqvvrgrgsratdgadrptptaPRQDYIFYLEPEKLESGKGKCPYDPKL 207
Cdd:cd11255   81 THLLACGTGAFQPVCALINVG--------------------------------HRGEHVFSLDPTTVESGRGRCPHEPKR 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 208 DTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQyNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAP 287
Cdd:cd11255  129 PFASTFTGGELYTGLTADFLGRDSVIFRGFGTRSPLRTET-DQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETA 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 288 Q--NPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSV 365
Cdd:cd11255  208 EddDGAIHSRVGRLCANDAGGQRVLVNKWSTFIKARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNV 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 366 FRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG-TFTPS--MKSTKDYPDEVINFMRTHPLMY 442
Cdd:cd11255  288 FQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWGPYEGKVPYPRPGVCPSKiTAQPGraFRSTKDYPDEVLQFARAHPLMW 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 443 QAVYPLQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELML-EEVEVFKEPAPVK 521
Cdd:cd11255  368 RPVYPSHRRPVLVKTGLPYRLTQIVVDRVEAEDGYYDVMFIGTDSGSVLKVIVLQKGNSAAGEEVTlEELQVFKVPTPIT 447
                        490       500
                 ....*....|....*....|....*..
gi 341942018 522 TMTISSKRQQLYVASAVGVTHLSLHRC 548
Cdd:cd11255  448 EMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
56-548 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: 537.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGnGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11253    9 DLHTMLLDEYQERLFVGGRDLLYSLSLERISANYKEIHWPSTQLQVEDCIMKGRDK-PECANYIRVLHHYNRTHLLACGT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 136 GAYNPMCTYVNRGRRAQalpwtqmqvvrgrgsratdgadrptptaprqDYIFYLEPEKLESGKGKCPYDPKLDTASALIN 215
Cdd:cd11253   88 GAFDPVCAFIRVGRGSE-------------------------------DHLFQLESDKFERGRGRCPFDPNSSFISTLIG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 216 EELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQ-NPAVYA 294
Cdd:cd11253  137 GELFVGLYSDYWGRDAAIFRTMNHLAHIRTEHDDERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGgNHAIYT 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 295 RIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVY 374
Cdd:cd11253  217 RVGRVCANDQGGQRMLVNKWSTFLKTRLICSVPGPNGIDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVY 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 375 SMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCP----GGTFTpsmkSTKDYPDEVINFMRTHPLMYQAVYPLQR 450
Cdd:cd11253  297 HMASIRAAFNGPFAHKEGPEYHWSVYEGKVPYPRPGSCAskvnGGHYG----TTKDYPDEALRFARSHPLMYQAVKPVHK 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 451 RPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVI-VLPKDDQEVEELMLEEVEVFKEPAPVKTMTISSKR 529
Cdd:cd11253  373 RPILVKTDGKYNLKQIAVDRVEAEDGQYDVLFIGTDNGIVLKVItIYNQETETMEEVILEELQVFKVPVPIISMEISSKR 452
                        490
                 ....*....|....*....
gi 341942018 530 QQLYVASAVGVTHLSLHRC 548
Cdd:cd11253  453 QQLYIGSESGVAQIRFHQC 471
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
55-546 3.42e-155

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


Pssm-ID: 200496 [Multi-domain]  Cd Length: 437  Bit Score: 459.18  E-value: 3.42e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  55 TDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREpLIIHWAASPQRIEECILSGKDGNgECGNFVRLIQPWNRTHLYVCG 134
Cdd:cd11235    1 LKYHTKLLHEDRSTLYVGARDRVYLVDLDSLYTE-QKVAWPSSPDDVDTCYLKGKSKD-DCRNFIKVLEKNSDDSLLVCG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 135 TGAYNPMCTYVNrgrraqalpwtqmqvvrgrgsratdgadrptptaprqDYIFYLEpEKLESGKGKCPYDPKLDTASALI 214
Cdd:cd11235   79 TNAFNPSCRNYN-------------------------------------VETFELV-GKEESGRGKCPYDPDHNSTALFA 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 215 NEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPdsaerndDKLYFFFRERSAE-APQNPAVY 293
Cdd:cd11235  121 DGELYSGTSADFLGTDPVIYRTLGHNPPLRTEYHDSKWLNEPQFVGAFDIG-------DYVYFFFREIAVEyINCGKAVY 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 294 ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCV 373
Cdd:cd11235  194 SRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFP--FYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCA 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 374 YSMADIRMVFNGPFAHKEGPNYQWMPFSG-KMPYPRPGTCPGgtftpsmkSTKDYPDEVINFMRTHPLMYQAVYPLQRRP 452
Cdd:cd11235  272 YSLSDIEAVFNGPFKEQHSSNSAWLPVPDeRVPEPRPGTCVD--------DSSPLPDDTLNFIKSHPLMDEAVTPILNRP 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 453 LVVRTGAPYRLTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKDDQeVEELMLEEVEVFKEPAPVKTMTISSKRQQ 531
Cdd:cd11235  344 LFIKTDVNYRFTKIAVDRVQAKLGQtYDVLFVGTDRGIILKVVSLPEQGL-QASNILEEMPVGPPPEPIQTMQLSRKRRS 422
                        490
                 ....*....|....*
gi 341942018 532 LYVASAVGVTHLSLH 546
Cdd:cd11235  423 LYVGSETGVLQVPLA 437
Sema smart00630
semaphorin domain;
57-521 1.24e-148

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 440.27  E-value: 1.24e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018    57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGTG 136
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   137 AYNPMCTYVNRGrraqalpwtqmqvvrgrgsratdgadrptptaprqdyifylepeklesgkgkcpydpkldtasaline 216
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   217 ELYAGVYIDFMGTDAAIFRTLG----KQTA---MRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFFFRERSAEA-PQ 288
Cdd:smart00630  93 ELYVGTVADFSGSDPAIPRSLSvrrlKGTSgvsLRTVLYDSKWLNEPNFVYAFES-------GDFVYFFFRETAVEDdNC 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   289 NPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGieTHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRG 368
Cdd:smart00630 166 GKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPG 243
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   369 SAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFtpsmkSTKDYPDEVINFMRTHPLMYQAVYP 447
Cdd:smart00630 244 SAVCAFSLSDINAVFNGPFKECETSTSQWLPYSrGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQP 318
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341942018   448 LQRRPLVVRTGAPYRLTTVAVDQVdAADGRYEVLFLGTDRGTVQKVIVLPKDDQeVEELMLEEVEVFKEPAPVK 521
Cdd:smart00630 319 LTGRPLFVKTDSNYLLTSIAVDRV-ATDGNYTVLFLGTSDGRILKVVLSESSSS-SESVVLEEISVFPDGSPIS 390
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
55-545 3.70e-131

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: 397.94  E-value: 3.70e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  55 TDYRILLKDEDHDRMYVGSKDYVLSLDLHDINRE-PLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVC 133
Cdd:cd11240    7 QNYSTLLLSEDEGTLYVGAREALFALNVSDISTElKDKIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYNSTHLYVC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 134 GTGAYNPMCTYVNrgrraqalpwtqmqvvrgrgsrATDgadrptptaprqdyiFYLEPEKLESGKGKCPYDPKLDTASAL 213
Cdd:cd11240   87 GTFAFSPRCTYIN----------------------LSD---------------FSLSSIKFEDGKGRCPFDPAQRYTAIM 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 214 INEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDqYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAE-APQN 289
Cdd:cd11240  130 VDGELYSATVNNFLGSEPVISRNHSEGNVLKTE-NTLRWLNEPAFVGSAHIResiDSPDGDDDKIYFFFTETAVEyDFYE 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 290 PAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgiETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGS 369
Cdd:cd11240  209 KVTVSRVARVCKGDLGGQRTLQKKWTTFLKAQLVCSQPDS---GLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLS 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 370 AVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPL 448
Cdd:cd11240  286 AVCAYSLEDIKKVFSGKYKEFNRETSKWSRYTGPVPDPRPGACiTNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPI 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 449 QrRPLVVRTGAPYrlTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKddqevEELMLEEVEVFKEPAPVKTMTISS 527
Cdd:cd11240  366 N-RPLLVKSGVNY--TRIAVHRVQALDGQtYTVLFLGTEDGFLHKAVSLDG-----GMHIIEEIQLFDQPQPVKNLLLSS 437
                        490
                 ....*....|....*...
gi 341942018 528 KRQQLYVASAVGVTHLSL 545
Cdd:cd11240  438 SKGVLYVGSSSGVVQVPL 455
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
50-545 1.51e-117

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: 362.54  E-value: 1.51e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  50 FLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDI-NREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRT 128
Cdd:cd11262    3 FRGPAQNYSTLLLEDESGRLYVGARGAIFSLNASDIsDSSALTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRFNST 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 129 HLYVCGTGAYNPMCTYVnrgrraqalpwtqmqvvrgrgsratDGADRPTPTAPrqdyifylepeklESGKGKCPYDPKLD 208
Cdd:cd11262   83 HLYTCGTHAFRPLCAYI-------------------------DAERFTLSSQF-------------EEGKEKCPYDPAKG 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 209 TASALINEELYAGVYIDFMGTdAAIFRTLgKQTAMRTDQYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAE 285
Cdd:cd11262  125 YTGLIVDGQLYTASQYEFRSF-PDIRRNS-PQPTLRTEEAPTRWLNDADFVGSVLVResmNSSVGDDDKIYFFFTERSQE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 286 APQNPAVY--ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGedgIETHFDELQDVFVQQTQDVRNPVIYAVFTSSG 363
Cdd:cd11262  203 ETAYFSQSrvARVARVCKGDRGGKKTLQRKWTSFLKARLVCYIPE---YEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEW 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 364 SVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTF-TPSMKSTKDYPDEVINFMRTHPLMY 442
Cdd:cd11262  280 KNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYTGKVPEPRPGSCITDEHrSQGINSSQDLPDNVLDFVRRHPLMA 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 443 QAVYPLQRRPLVVRTGAPYrlTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLpkddqEVEELMLEEVEVFKEPAPVK 521
Cdd:cd11262  360 EQVLPVEGRPLLFKRNVIY--TKIAVQTVRGLDGRvYDVLFLGTDEGWLHKAVVI-----GSAVHIIEELQVFREPQPVE 432
                        490       500
                 ....*....|....*....|....
gi 341942018 522 TMTISSKRQQLYVASAVGVTHLSL 545
Cdd:cd11262  433 NLVISKKQNSLYVGARSGVVQVPL 456
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
53-548 3.02e-105

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: 330.45  E-value: 3.02e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  53 NTTDYRILLkDEDHDRMYVGSKDYVLSLDLHDInREPLIIHWAASPQRIEECILSGKDGNgECGNFVRLIQPWNRTHLYV 132
Cdd:cd11237    2 THSDHFKLL-DQDGNSLLVGARNAVYNISLSDL-TENQRIEWPSSDAHREMCLLKGKSED-DCQNYIRVLAKKSAGRLLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 133 CGTGAYNPMCTYVNRgrraqalpwtqmqvvrgrgsratdgadrptptaprQDYIFYLEPEKleSGKGKCPYDPKLDTASA 212
Cdd:cd11237   79 CGTNAYKPLCREYTV-----------------------------------KDGGYRVEREF--DGQGLCPYDPKHNSTAV 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 213 LINEELYAGVYIDFMGTDAAIFRTlgkqtAMRTDQYNSRWLNDPSFIHaelipdSAERNDdKLYFFFRERSAEAPQ-NPA 291
Cdd:cd11237  122 YADGQLYSATVADFSGADPLIYRE-----PLRTERYDLKQLNAPNFVS------SFAYGD-YVYFFFRETAVEYINcGKA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 292 VYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQ---DVFVQQTQDVRNPVIYAVFTSSGSVFRG 368
Cdd:cd11237  190 IYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGE--YPFYFNEIQstsDIVEGGYGGKSAKLIYGVFTTPVNSISG 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 369 SAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSG-KMPYPRPGTCpggtftpsMKSTKDYPDEVINFMRTHPLMYQAVYP 447
Cdd:cd11237  268 SAVCAFSLQDILEVFDGSFKEQQDINSNWLPVPSnKVPEPRPGQC--------VNDSRTLPDVTVNFIKSHPLMDEAVPS 339
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 448 LQRRPLVVRTGAPYRLTTVAVD-QVDAADGR-YEVLFLGTDRGTVQKVIVLPKDDQEVEELMLE--EVEVFKEPAPVKTM 523
Cdd:cd11237  340 FFGRPILVRTSLQYRFTQIAVDpQVKALDGKyYDVLFIGTDDGKVLKAVNIASADTVDKVSPVVieETQVFPRGVPIRNL 419
                        490       500
                 ....*....|....*....|....*..
gi 341942018 524 TISSKRQQ--LYVASAVGVTHLSLHRC 548
Cdd:cd11237  420 LIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
56-540 6.04e-98

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: 312.18  E-value: 6.04e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11259   19 NYSTLLLSEDKDVLYVGAREAVFALNALNISEKQHELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLNDTFLYVCGT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 136 GAYNPMCTYVNrgrraqalpwtqmqvvrgrgsrATDgadrptptaprqdyiFYLEpEKLESGKGKCPYDPKLDTASALIN 215
Cdd:cd11259   99 NAFQPTCDYLN----------------------LTS---------------FRLL-GKNEDGKGRCPFDPAQSYTSVMVD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 216 EELYAGVYIDFMGTDAAIFRTLgKQTAMRTdQYNSRWLNDPSFIHAELI---PDSAERNDDKLYFFFRERSAEAP-QNPA 291
Cdd:cd11259  141 GELYSGTSYNFLGSEPIISRNS-SQSPLRT-EYAIPWLNEPSFVFADVIradPDSPDGEDDKIYFFFTEVSVEYEfVGKL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 292 VYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIethFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAV 371
Cdd:cd11259  219 LIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSIPDKNLV---FNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAV 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 372 CVYSMADIRMVFN-GPFAHK---EGPNYQWMPFSGKMPYPRPGTCPGGTFTPS-MKSTKDYPDEVINFMRTHPLMYQAVY 446
Cdd:cd11259  296 CAYNLSTVEEVFSkGKYMQSatvEQSHTKWVRYNGEVPKPRPGACINNEARAAnYTSSLNLPDKTLQFVKDHPLMDDSVT 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 447 PLQRRPLVVRTGAPYrlTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKDdqeveELMLEEVEVFKEPAPVKTMTI 525
Cdd:cd11259  376 PIGNRPRLIKKDVNY--TQIVVDRVQALDGTiYDVMFISTDRGALHKAISLENE-----VHIIEETQLFPDFEPVQTLLL 448
                        490
                 ....*....|....*..
gi 341942018 526 SSK--RQQLYVASAVGV 540
Cdd:cd11259  449 SSKkgRRFLYAGSNSGV 465
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
56-545 4.14e-96

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: 306.83  E-value: 4.14e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11260    8 NYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMNDSRMYVCGT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 136 GAYNPMCTYVNrgrraqalpwtqmqvvrgrgsrATDGAdrptptaprqdyifyLEPEKL-ESGKGKCPYDPKLDTASALI 214
Cdd:cd11260   88 NAFSPTCDYIS----------------------YDDGQ---------------LTLEGKqEDGKGKCPFDPFQRYSSVMV 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 215 NEELYAGVYIDFMGTDAAIFRTlgKQTAMRTdQYNSRWLNDPSFIHAELIP---DSAERNDDKLYFFFRERSAEAP-QNP 290
Cdd:cd11260  131 DQDLYSATSMNFLGSEPVIMRS--SPITIRT-EFKSSWLNEPNFIYMAAVPeseDSPEGDDDKIYLFFSETAVEYDfYNK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 291 AVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPgedgiETHFDEL-QDVFVQQTQDVRNPVIYAVFTSSGSVFRGS 369
Cdd:cd11260  208 LVVSRVARVCKGDLGGQRTLQKKWTSFLKARLDCSVP-----EPSLPYViQDVFHVCHQDWRKCVFYAVFTSQSDSSQSS 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 370 AVCVYSMADIRMVFN-----GPFAhKEGPNYQWMPFSGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRTHPLMYQ 443
Cdd:cd11260  283 AVCAYNVTDISNVFSrgkfkTPVA-VETSFVKWVMYSGELPVPRPGACiNNAARTSGIKKSLNLPDKTLQFVKDKPLMDQ 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 444 AVYPLQRRPLVVRTGAPyrLTTVAVDQVDAADG-RYEVLFLGTDRGTVQKVIvlpkdDQEVEELMLEEVEVFKEPAPVKT 522
Cdd:cd11260  362 AVHPITGKPLLVKRGAL--FTRIVVDMVTAADGqSYPVMFIGTANGYVLKAV-----NYDGEMHIIEEVQLFEPEEPIDI 434
                        490       500
                 ....*....|....*....|...
gi 341942018 523 MTISSKrqQLYVASAVGVTHLSL 545
Cdd:cd11260  435 LRLSQN--QLYAGSASGVVQMPV 455
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
67-497 3.61e-94

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: 302.13  E-value: 3.61e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  67 DRMYVGSKDYVLSLDLHDINREPLI----IHWAASPQRIEECILSGKDgNGECGNFVRLIQPWNRTHLYVCGTGAYNPMC 142
Cdd:cd11242   19 RTLYIAARDHVYTVDLDASHTEEIVpskkLTWRSRQADVENCRMKGKH-KDECHNFIKVLVPRNDETLFVCGTNAFNPVC 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 143 TYVNrgrraqalpwtqmqvvrgrgsratdgadrptptaprqdyIFYLEPEKLE-SGKGKCPYDPKLDTASALINEELYAG 221
Cdd:cd11242   98 RNYR---------------------------------------IDTLEQDGEEiSGMARCPFDAKQANVALFADGKLYSA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 222 VYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAE-APQNPAVYARIGRIC 300
Cdd:cd11242  139 TVTDFLASDAVIYRSLGDSPTLRTVKYDSKWLKEPHFVHAV-------EYGDYVYFFFREIAVEyNTLGKVVFSRVARVC 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 301 LNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVfvqqTQDVR---NPVIYAVFTSSGSVFRGSAVCVYSM 376
Cdd:cd11242  212 KNDMGGSPRVLEKqWTSFLKARLNCSVPGDSHF--YFDVLQAV----TDVIRingRPVVLGVFTTQYNSIPGSAVCAFDM 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 377 ADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPLQRRPLVV 455
Cdd:cd11242  286 DDIEKVFEGRFKEQKSPDSAWTPVPeDRVPKPRPGCCAGSGSAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFT 365
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 341942018 456 RTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLP 497
Cdd:cd11242  366 RTMVRYRLTQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARI 407
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
56-545 7.81e-93

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: 298.25  E-value: 7.81e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIhWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGT 135
Cdd:cd11258   11 NYTTLTLAEHRGLLYVGAREAIFALSLSNIELQPPIS-WEAPAEKKTECAQKGKSNQTECFNYIRFLQPYNQSHLYTCGT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 136 GAYNPMCTYVNRGRraqalpwtqmqvvrgrgsratdgadrptptaprqdyiFYLEPEKLESGKGKCPYDPKLDTASALIN 215
Cdd:cd11258   90 YAFQPKCAYINMLT-------------------------------------FTLDRAEFEDGKGKCPYDPAKGHTGLIVD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 216 EELYAGVYIDFMGTDAAIFRTLGKQTAMRTdQYNSRWLNDPSFIHAELIPDSAER---NDDKLYFFFRERSAEAP-QNPA 291
Cdd:cd11258  133 GELYSATLNNFLGTEPVILRNLGQHYSMKT-EYLAFWLNEPHFVGSAFVPESVGSftgDDDKIYFFFSERAVEYDcDSEQ 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 292 VYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPgedGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAV 371
Cdd:cd11258  212 VVARVARVCKGDLGGARTLQKKWTTFLKARLLCSIP---EWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAV 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 372 CVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTC-PGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPLQR 450
Cdd:cd11258  289 CEYQLGEIQQVFEGPYKEYSEQAQKWGRYTDPVPSPRPGSCiNNWHRDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLG 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 451 RPLVVRTGApyRLTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLpkddqEVEELMLEEVEVFKEPAPVKTMTISSKR 529
Cdd:cd11258  369 RPLLVPCNS--NFTHVVWTRVLGLDGEtYSVLFIGTLDGWLIKAVSL-----GSWVHMIEELQVFDQEPPESLVVSQSSK 441
                        490
                 ....*....|....*.
gi 341942018 530 QQLYVASAVGVTHLSL 545
Cdd:cd11258  442 KLLFAGSRSELLQLPW 457
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
53-568 1.67e-90

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: 291.81  E-value: 1.67e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHD--INREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHL 130
Cdd:cd11256    6 NVHNYDQLLLSPDETTLYVGARDNILALGIRTpgPIRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPVNGTHL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 131 YVCGTGAYNPMCTYVNRgrraqalpwtqmqvvrgrgsratdgadrptptaprQDyiFYLEP----EKLESGKGKCPYDPK 206
Cdd:cd11256   86 YTCGTYAFSPACTYIEL-----------------------------------DH--FSLPPpngtIITMDGKGQSPFDPQ 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 207 LDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNsRWLN-DPSFIHAELIPDsaernDDKLYFFFRERSAE 285
Cdd:cd11256  129 HNYTAILVDGELYTGTMNNFRGNEPIIFRNLGTKVSLKTDGFL-RWLNaDAVFVASFNPQG-----DSKVYFFFEETARE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 286 APQNPAVY-ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGedgiETHFDELQDVFVQQTQDVRNPVIYAVFTSSGS 364
Cdd:cd11256  203 FDFFEKLTvARVARVCKNDVGGEKLLQKKWTTFLKAQLTCSQQG----HFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQ 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 365 V--FRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTpsmkstkdypDEVINFMRTHPLMY 442
Cdd:cd11256  279 LggRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPVSDPRPGSCSGGKSS----------DKALNFMKDHFLMD 348
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 443 QAVYPLQRRPLVVRTGAPYrlTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVlpkddqeveelmleevevfkepapvk 521
Cdd:cd11256  349 EVVLPGAGRPLLVKSNVQY--TRIAVDSVQGVSGHnYTVMFLGTDKGFLHKAVL-------------------------- 400
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 341942018 522 tmtisSKRQQLYVASAVGVTHLSLHRCQAYGAACADCCLARDPYCAW 568
Cdd:cd11256  401 -----MGGSESHIIEEIELLTPPEPVENLLLAANEGVVYIGYSAGVW 442
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
55-545 2.30e-90

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: 291.76  E-value: 2.30e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  55 TDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPL--IIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYV 132
Cdd:cd11257    8 SNYTALLLSKDGNMLYVGARETLFALSSNDISPTGEqqELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRLNSTHLFT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 133 CGTGAYNPMCTYVNRgrraqalpwTQMQVVRgrgsratDGADRPTptaprqdyifylepekLESGKGKCPYDPKLDTASA 212
Cdd:cd11257   88 CGTYAFSPICTYIVM---------TNFSLER-------DEKGEPL----------------LEDGKGRCPFDPEYKSTAI 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 213 LINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDqyNS-RWLNDPSFIHAELIPDS---AERNDDKLYFFFRERSAEAP- 287
Cdd:cd11257  136 MVDGELYTGTVSNFQGNDPIIYRSLGSGTPLKTE--NSlNWLQDPAFVGSAYIQESlpkLVGDDDKIYFFFSETGKEFDf 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 288 -QNPAVyARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGeDGIEthFDELQDVFV--QQTQDVRNPVIYAVFTS--S 362
Cdd:cd11257  214 fENTIV-SRIARVCKGDEGGERVLQKRWTTFLKAQLLCSLPD-DGFP--FNVLQDVFVltPSPEDWKDTLFYGVFTSqwH 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 363 GSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTP-SMKSTKDYPDEVINFMRTHPLM 441
Cdd:cd11257  290 KGTAGSSAVCVFTMDQVQRAFNGLYKEVNRETQQWYTYTHPVPEPRPGACITNSARErKINSSLHMPDRVLNFVKDHFLM 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 442 YQAVyplQRRPLVVRTGAPYrlTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKddqevEELMLEEVEVFKEPAPVK 521
Cdd:cd11257  370 DGQV---RSQPLLLQPQVRY--TQIAVHRVKGLHKTYDVLFLGTDDGRLHKAVSVGP-----MVHIIEELQIFSEGQPVQ 439
                        490       500
                 ....*....|....*....|....
gi 341942018 522 TMTISSKRQQLYVASAVGVTHLSL 545
Cdd:cd11257  440 NLLLDTHKGLLYASSHSGVVQVPV 463
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
56-494 5.32e-88

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: 285.77  E-value: 5.32e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDedHDRMYVGSKDYVLSLDLHDINREPLI----IHWAASPQRIEECILSGKDGNgECGNFVRLIQPWNRTHLY 131
Cdd:cd11269   10 DFQLMLKI--RDTLYIAGRDQVYTVNLNEVPKTEVTpsrkLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDEMVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 132 VCGTGAYNPMCTYVnrgrRAQALPWtqmqvvrgrgsratDGadrptptaprqdyifylepEKLeSGKGKCPYDPKLDTAS 211
Cdd:cd11269   87 VCGTNAFNPMCRYY----RLSTLEY--------------DG-------------------EEI-SGLARCPFDARQTNVA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 212 ALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAEAPQ-NP 290
Cdd:cd11269  129 LFADGKLYSATVADFLASDAVIYRSMGDGSALRTIKYDSKWIKEPHFLHAI-------EYGNYVYFFFREIAVEHNNlGK 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 291 AVYARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVfvQQTQDVRN-PVIYAVFTSSGSVFRG 368
Cdd:cd11269  202 AVYSRVARICKNDMGGSQRVLEKhWTSFLKARLNCSVPGDSFF--YFDVLQSI--TDIIEINGiPTVVGVFTTQLNSIPG 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 369 SAVCVYSMADIRMVFNGPFAHKEGPNYQWMPF-SGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYP 447
Cdd:cd11269  278 SAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAVpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPS 357
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 341942018 448 LQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVI 494
Cdd:cd11269  358 IIEEPWFTKTRVRYRLTAIAVDHAAGPHQNYTVIFVGSEAGVVLKIL 404
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
57-545 3.12e-83

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: 272.76  E-value: 3.12e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  57 YRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWA---ASPQRIEECILSGKDGNGECGNFVRLIQPWN-RTHLYV 132
Cdd:cd11238    3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINDTGNNCARDeltLSPSDVSECVSKGKDEEYECRNHVRVIQPMGdGQTLYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 133 CGTGAYNPmctyvnRGRRAQALPWTQMQVVRGrgsratdgadrptptaprqdyifylepekLESGKGKCPYDPKLDTASA 212
Cdd:cd11238   83 CSTNAMNP------KDRVLDANLLHLPEYVPG-----------------------------PGNGIGKCPYDPDDNSTAV 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 213 LI---NEE----LYAGVYIDFMGTDAAIFRT----LGKQ---TAMRTDQYNSRWLNDPSFIHAELIpdsaernDDKLYFF 278
Cdd:cd11238  128 WVewgNPGdlpaLYSGTRTEFTKANTVIYRPplynNTKGrheSFMRTLKYDSKWLDEPNFVGSFDI-------GDYVYFF 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 279 FRERSAEAPQ-NPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVF-VQQTQDVRnpvIY 356
Cdd:cd11238  201 FRETAVEYINcGKVVYSRVARVCKKDTGGKNVLRQNWTTFLKARLNCSISGE--FPFYFNEIQSVYkVPGRDDTL---FY 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 357 AVFTSSGSVFRGSAVCVYSMADIRMVFN-GPFAHKEGPNYQWMP-FSGKMPYPRPGTCPGgtftpsmkSTKDYPDEVINF 434
Cdd:cd11238  276 ATFTTSENGFTGSAVCVFTLSDINAAFDtGKFKEQASSSSAWLPvLSSEVPEPRPGTCVN--------DSATLSDTVLHF 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 435 MRTHPLMYQAVYplQRRPLVVRtgAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKvIVLPKDDQeVEELMLEEVEVF 514
Cdd:cd11238  348 ARTHPLMDDAVS--HGPPLLYL--RDVVFTHLVVDKLRIDDQEYVVFYAGSNDGKVYK-IVHWKDAG-ESKSNLLDVFEL 421
                        490       500       510
                 ....*....|....*....|....*....|.
gi 341942018 515 KEPAPVKTMTIsSKRQQLYVASAVGVTHLSL 545
Cdd:cd11238  422 TPGEPIRAMEL-LPGEFLYVASDHRVSQIDL 451
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
53-545 1.52e-79

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: 262.49  E-value: 1.52e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLIIH--WAASPQRIEECILSGKDGNgECGNFVRLIQPWNRThL 130
Cdd:cd11241    5 YVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLS---LLQAvpWNSDEDTKRQCQSKGKSVE-ECQNYVRVLLVVGKN-L 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 131 YVCGTGAYNPMCTyvnrgrraqalpWTQMqvvrgrgSRATDGADRptptaprqdyifylepeklESGKGKCPYDPKLDTA 210
Cdd:cd11241   80 FTCGTYAFSPVCT------------IRKL-------SNLTQILDT-------------------ISGVARCPYSPAHNST 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 211 SALINE-ELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIhaelipdSAERNDDKLYFFFRERSAEAPQ- 288
Cdd:cd11241  122 ALISASgELYAGTVYDFSGRDPAIYRSLGGKPPLRTAQYNSKWLNEPNFV-------GSYEIGNHTYFFFRENAVEHQDc 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 289 NPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRG 368
Cdd:cd11241  195 GKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGE--FPFYYNEIQGTFYLPETD----LIYAVFTTNVNGIAG 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 369 SAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFsgkmPYPRPGTCPGGTFTPSMKSTKDyPDEVINFMRtHPLMYQAVYPL 448
Cdd:cd11241  269 SAICAFNLSAINQAFNGPFKYQENNGSAWLPT----PNPHPNFQCTTSIDRGQPANTT-ERDLQDAQK-YQLMAEVVQPV 342
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 449 QRRPLVVRTGApyRLTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKdDQEVEELMLEEVEVFKEPAPVKTMTISS 527
Cdd:cd11241  343 TKIPLVTMDDV--RFSKLAVDVVQGRGTQlVHIFYVGTDYGTILKMYQPHR-SQKSCTLEEIKILPAMKGEPITSLQFLK 419
                        490
                 ....*....|....*...
gi 341942018 528 KRQQLYVASAVGVTHLSL 545
Cdd:cd11241  420 SEKSLFVGLETGVLRIPL 437
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
69-495 2.79e-79

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: 262.66  E-value: 2.79e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  69 MYVGSKDYVLSLDLHDINREPLI----IHWAASPQRIEECILSGKDGNgECGNFVRLIQPWNRTHLYVCGTGAYNPMCTY 144
Cdd:cd11266   21 LYIAARDHIYTVDIDTSHTEEIYfskkLTWKSRQADVDTCRMKGKHKD-ECHNFIKVLLKRNDDTLFVCGTNAFNPSCRN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 145 VnrgrraqalpwtqmqvvrgrgsratdgadrptptapRQDYIFYLEPEKleSGKGKCPYDPKLDTASALINEELYAGVYI 224
Cdd:cd11266  100 Y------------------------------------KMDTLEFFGDEF--SGMARCPYDAKHANVALFADGKLYSATVT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 225 DFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAE-APQNPAVYARIGRICLND 303
Cdd:cd11266  142 DFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAV-------DYGDYIYFFFREIAVEyNSMGKVVFPRVAQVCKND 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 304 DGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVCVYSMADIRMV 382
Cdd:cd11266  215 MGGSQRVLEKqWTSFLKARLNCSVPGDSHF--YFNILQAVTDVIHINGRD-VVLATFSTPYNSIPGSAVCAYDMLDIASV 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 383 FNGPFAHKEGPNYQWMPFSG-KMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPLQRRPLVVRTGAPY 461
Cdd:cd11266  292 FTGRFKEQKSPDSTWTPVPDeRVPKPRPGCCAGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRY 371
                        410       420       430
                 ....*....|....*....|....*....|....
gi 341942018 462 RLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIV 495
Cdd:cd11266  372 RLTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLA 405
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
69-500 3.82e-79

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: 262.08  E-value: 3.82e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  69 MYVGSKDYVLSLDLHDINREPLIIH----WAASPQRIEECILSGKDgNGECGNFVRLIQPWNRTHLYVCGTGAYNPMCty 144
Cdd:cd11267   21 LYIGDRDNLYRVELDPTAGTEMRYHkkltWRSNKNDINVCRMKGKH-EGECRNFIKVLLLRDYGTLFVCGTNAFNPVC-- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 145 vnrgrraqalpwtqmqvvrgrgsratdgADRPTPTaprqdyifyLEP--EKLeSGKGKCPYDPKLDTASALINEELYAGV 222
Cdd:cd11267   98 ----------------------------ANYSIDT---------LEPvgDNI-SGMARCPYDPKHANVALFADGMLFTAT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 223 YIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHA-ELIPdsaernddKLYFFFRERSAEAPQ-NPAVYARIGRIC 300
Cdd:cd11267  140 VTDFLAIDAVIYRSLGDSPALRTVKHDSKWFKEPYFVHAvEWGS--------HVYFFFREIAMEFNYlEKVVVSRVARVC 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 301 LNDDGGHCCLVNK-WSTFLKARLVCSVPGEdgieTHFdelqdVF--VQQTQDVRN----PVIYAVFTSSGSVFRGSAVCV 373
Cdd:cd11267  212 KNDMGGSQRVLEKqWTSFLKARLNCSVPGD----SHF-----YFnvLQAVSDILNlggrPVVLAVFSTPTNSIPGSAVCA 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 374 YSMADIRMVFNGPFAHKEGPNYQWMPFSGKM-PYPRPGTCPGgtftPSMK--STKDYPDEVINFMRTHPLMYQAVYPLQR 450
Cdd:cd11267  283 FDMTQVAAVFEGRFREQKSPESIWTPVPEELvPRPRPGCCAA----PGMRynSSSTLPDEVLNFVKTHPLMDEAVPSLGH 358
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 341942018 451 RPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDD 500
Cdd:cd11267  359 APWIVRTMTRYQLTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLIIPNAS 408
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
54-543 2.04e-75

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: 252.11  E-value: 2.04e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  54 TTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDgNGECGNFVRLIQPWNRTHLYVC 133
Cdd:cd11261   11 TYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERPRRIDWMVPEAHRQNCRKKGKK-EAECHNFIRILAIANASHLLTC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 134 GTGAYNPMCTYVNRGRRAQAlpwtqmqvvrgrgsratdgadrptptaprqdyifylepEKLESGKGKCPYDPKLDTASAL 213
Cdd:cd11261   90 GTFAFDPKCGVIDVSSFQQV--------------------------------------ERLESGRGKCPFEPAQRSAAIM 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 214 INEELYAGVYIDFMGTDAAIFRTLGK-QTAMRTDQYNSrWLNDPSFIHAELIPDSA---ERNDDKLYFFFRERSAEAPQ- 288
Cdd:cd11261  132 AGGVLYAATVKNFLGTEPIISRAVGRaEEWIRTETLPS-WLNAPAFVAAVFLSPAEwgdEDGDDEIYFFFTETAREYDSy 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 289 NPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPgEDGieTHFDELQDVFVQQTQDVRN-PVIYAVFTSSGSVFR 367
Cdd:cd11261  211 ERIKVPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGP-EHG--RASSILQDVTTLRPLPGAGtPIFYGIFSSQWEGAS 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 368 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCpggtFTPSMK-----STKDYPDEVINFMRTHPLM 441
Cdd:cd11261  288 ISAVCAFRPQDIRRVMNGPFREFKHDCNRGLPVMdSDVPQPRPGEC----ITNNMKllgfgSSLSLPDRVLTFVRDHPLM 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 442 YQAVYPLQRRPLVVRTGAPYrlTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLpkddqEVEELMLEEVEVFKEPAPV 520
Cdd:cd11261  364 DRPVFPADGHPLLVTTDTAY--LRVAAHRVTSLSGKeYDVLYLGTEDGHLHRAVRI-----GAQLSVLEDLALFPEPQPV 436
                        490       500
                 ....*....|....*....|...
gi 341942018 521 KTMTIssKRQQLYVASAVGVTHL 543
Cdd:cd11261  437 ENLQL--HHNWLLVGSDTEVTQI 457
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
56-494 9.67e-74

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: 246.82  E-value: 9.67e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWAASPQRIEECILSGKDGNgECGNFVRLIQPwNRTHLYVC 133
Cdd:cd11264    8 DFSQLALDLNRNQLIVGARNYLFRLSLHNVS---LIqaTEWGSDEDTRRSCQSKGKTEE-ECQNYVRVLIV-YGKKVFTC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 134 GTGAYNPMCTYVNRGRRAQALpwtqmqvvrgrgsratdgadrptptaprqdyifylepEKLeSGKGKCPYDPKlDTASAL 213
Cdd:cd11264   83 GTNAFSPVCTSRQVGNLSKVI-------------------------------------ERI-NGVARCPYDPR-HNSTAV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 214 INE--ELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAernddklYFFFRERSAEAPQNPA 291
Cdd:cd11264  124 ITSrgELYAATVIDFSGRDPAIYRSLGSVPPLRTAQYNSKWLNEPNFIAAYDIGLFT-------YFFFRENAVEHDCGKT 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 292 VYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRGSAV 371
Cdd:cd11264  197 VYSRVARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAV 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 372 CVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPggtftpsmkstKDYPDE-----VINFMRTHPLMYQAVY 446
Cdd:cd11264  271 CAFNLSAITQAFNGPFRYQENPRSAWLPTANPIPNFQCGTLS-----------DDSPNEnlterSLQDAQRLFLMNDVVQ 339
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 341942018 447 PLQRRPLVvrTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVI 494
Cdd:cd11264  340 PVTVDPLV--TQDSVRFSKLVVDIVQGKDTLYHVMYIGTEYGTILKAL 385
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
56-494 2.34e-73

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: 246.56  E-value: 2.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDedHDRMYVGSKDYVLSLDLHDInREPLI----IHWAAspQRIEECILSGKDGNgECGNFVRLIQPWNRTHLY 131
Cdd:cd11270   10 DFQRMLRI--NHMVYIAARDHVFAINLSAS-LERIVpqqkLTWKT--KDVEKCTVRGKNSD-ECYNYIKVLVPRNDETLF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 132 VCGTGAYNPMCtyvnrgrraqalpwtqmqvvrgrgsratdgadrptptapRQDYIFYLEPEKLE-SGKGKCPYDPKLDTA 210
Cdd:cd11270   84 ACGTNAFNPTC---------------------------------------RNYKMSSLEQDGEEvIGQARCPFESRQSNV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 211 SALINEELYAGVYIDFMGTDAAIFRTLGKQT-AMRTDQYNSRWLNDPSFIHAElipdsaeRNDDKLYFFFRERSAEAPQ- 288
Cdd:cd11270  125 GLFAGGDFYSATMTDFLASDAVIYRSLGESSpVLRTVKYDSKWLREPHFLHAI-------EYGNYVYFFLSEIAVEYTTl 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 289 NPAVYARIGRICLNDDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVFVQQTQDVRnPVIYAVFTSSGSVFR 367
Cdd:cd11270  198 GKVVFSRVARVCKNDNGGSPRVLERyWTSFLKARLNCSVPGDSFF--YFDVLQSLTNVMQINHR-PAVLGVFTTQANSIT 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 368 GSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPF-SGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVY 446
Cdd:cd11270  275 GSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPVpDEAVPKPRPGSCAGDGPAAGYKSSTNFPDETLTFIKSYPLMDEAVP 354
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 341942018 447 PLQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVI 494
Cdd:cd11270  355 SVNNRPCFTRTTSRFKLTQIAVDTAAGPYKNYTVVFLGSENGHVLKVL 402
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
339-527 2.49e-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: 2.49e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  339 LQDVFVQQ--TQDVRNPVIYAVFTSS-GSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGG 415
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  416 TFtpsmksTKDYPDEVINFMRTHPLMYQAVYPLQRRPLVVRTGapYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIV 495
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTG--VRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 341942018  496 LPKDD-------QeveelmleeveVFKEPAPVKTMTISS 527
Cdd:pfam01403 153 VGSEEshiieeiQ-----------VFPEPQPVLNLLLSS 180
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
53-543 7.59e-71

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: 238.91  E-value: 7.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDInrEPL-IIHWAASPQRIEECILSGKDGNgECGNFVRLIQPwNRTHLY 131
Cdd:cd11265    5 EVTSYSQMLFDVARNQVIVGARDNLYRLSLDGL--ELLeRASWPAAESKVALCQNKGQSEE-DCHNYVKVLLS-YGKQLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 132 VCGTGAYNPMCTyvnrgrraqalpWTQMQVVrgrgSRATDgadrptptaprqdyifylepekLESGKGKCPYDPkLDTAS 211
Cdd:cd11265   81 ACGTNAFSPRCS------------WREMENL----TSVTE----------------------WDSGVAKCPYSP-HANIT 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 212 ALINE--ELYAGVYIDFMGTDAAIFRTLGKQTA--MRTDQYNSRWLNDPSFIhaelipDSAErNDDKLYFFFRERSAEAP 287
Cdd:cd11265  122 ALLSSsgQLFVGSPTDFSGSDSAIYRTLGTSNKsfLRTKQYNSKWLNEPQFV------GSFE-TGNFVYFLFRESAVEYM 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 288 Q-NPAVYARIGRICLNDDGGHCCLV-NKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDVrnpvIYAVFTSSGSV 365
Cdd:cd11265  195 NcGKVIYSRIARVCKNDVGGGTMLLkDNWTTFLKARLNCSLPGE--YPFYFDEIQGMTYLPDEGI----LYATFTTPENS 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 366 FRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWmpfsGKMPYP---RPGTCPGGTFTPSMKSTKdypdevinfmrtHPLMY 442
Cdd:cd11265  269 IAGSAVCAFNLSSINAAFDGPFKHQESSGAAW----ERVNVNhrdHFNQCSSSSSSHLLESSR------------YQLMD 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 443 QAVYPLQRRPLVVRTGApyRLTTVAVDQVDAA-DGRYEVLFLGTDRGTVQKVIVLPKDDQeveELMLEEVEVFKEPA-PV 520
Cdd:cd11265  333 EAVQPITLEPLHHAKLE--RFSHIAVDVIPTKiHQSVHVLYVATTGGLIKKISVLPRTQE---TCLVEIWQPLPTPDsPI 407
                        490       500
                 ....*....|....*....|...
gi 341942018 521 KTMTISSKRQQLYVASAVGVTHL 543
Cdd:cd11265  408 KTMQYLKVTDSLYVGTELALMRI 430
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
53-534 1.88e-70

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: 238.01  E-value: 1.88e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  53 NTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINrepLI--IHWAASPQRIEECILSGKDGNgECGNFVRLIQPwNRTHL 130
Cdd:cd11263    5 NAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLS---LIqaVEWECDEATKKACYSKGKSKE-ECQNYIRVLLV-GGDRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 131 YVCGTGAYNPMCTyvnrGRRAQALPWTQMQVvrgrgsratdgadrptptaprqdyifylepekleSGKGKCPYDPKLDTA 210
Cdd:cd11263   80 FTCGTNAFTPICT----NRTLNNLTEIHDQI----------------------------------SGMARCPYSPQHNST 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 211 SALINE-ELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAernddklYFFFRERSAEAPQN 289
Cdd:cd11263  122 ALLTSSgELYAATAMDFPGRDPAIYRSLGILPPLRTAQYNSKWLNEPNFVSSYDIGNFT-------YFFFRENAVEHDCG 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 290 PAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEdgIETHFDELQDVFVQQTQDvrnpVIYAVFTSSGSVFRGS 369
Cdd:cd11263  195 KTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGE--IPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAAS 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 370 AVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFtpsMKSTKDYPDEVINFMrthpLMYQAVYPLQ 449
Cdd:cd11263  269 AVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPNPNFQCGTMDQGLY---VNLTERNLQDAQKFI----LMHEVVQPVT 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 450 RRPLVVRTGApyRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKviVLPKDDQEVEELMLEEVEVF--KEPAPVKTMTISS 527
Cdd:cd11263  342 PVPYFMEDNS--RFSHVAVDVVQGKDMLFHIIYLATDYGTIKK--VLAPLNQSSSSCLLEEIELFpkRQREPIRSLQILH 417

                 ....*..
gi 341942018 528 KRQQLYV 534
Cdd:cd11263  418 SQSVLFV 424
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
69-494 2.76e-64

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: 222.27  E-value: 2.76e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  69 MYVGSKDYVLSLDLHDINR-EPLI----IHWAAspQRIEECILSGKDGNgECGNFVRLIQPWNRTHLYVCGTGAYNPMCt 143
Cdd:cd11268   21 LLVAARDHVFSFDLQAEEEgEGLVpnkyLTWRS--QDVENCAVRGKLTD-ECYNYIRVLVPWDSQTLLACGTNSFSPVC- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 144 yvnrgrRAQALPWTQMqvvrgrgsratdgadrptptaprqdyifylEPEKLeSGKGKCPYDPKLDTASALINEELYAGVY 223
Cdd:cd11268   97 ------RSYGITSLQQ------------------------------EGEEL-SGQARCPFDATQSNVAIFAEGSLYSATA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 224 IDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHaelipdsAERNDDKLYFFFRERSAEAPQNPAV-YARIGRICLN 302
Cdd:cd11268  140 ADFQASDAVVYRSLGPQPPLRSAKYDSKWLREPHFVQ-------ALEHGDHVYFFFREVSVEDARLGRVqFSRVARVCKR 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 303 DDGGHCCLVNK-WSTFLKARLVCSVPGEDGIetHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFRGSAVCVYSMADIRM 381
Cdd:cd11268  213 DMGGSPRALDRhWTSFLKLRLNCSVPGDSTF--YFDVLQALTGPVNLHGRS-ALFGVFTTQTNSIPGSAVCAFYLDEIER 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 382 VFNGPFAHKEGPNYQWMPFS-GKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPLQRRPLVVRTGAP 460
Cdd:cd11268  290 GFEGKFKEQRSLDGAWTPVSeDRVPSPRPGSCAGVGGAALFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLTLTSRA 369
                        410       420       430
                 ....*....|....*....|....*....|....
gi 341942018 461 YrLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVI 494
Cdd:cd11268  370 L-LTQVAVDGMAGPHSNITVMFLGSNDGTVLKVL 402
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
57-545 1.70e-60

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: 210.09  E-value: 1.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  57 YRILLKDEDHDRMYVGSKDYVLSLDL---HDINREPLIIHWAASpqrieeciLSGKDGNGECGNFVRLIQPWNRThLYVC 133
Cdd:cd11243    4 YPVFFHEAGSSSVYVGGQGALYLLDFtgsAVIVKKIPDEKTEKD--------CKKRATLDDCENYITLIKKLDYR-LLVC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 134 GTGAYNPMCtyvnrgrraqalpWtqmqvvrgrgsratdgadrptptaprqdyifYLEPEKLES---GKGKCPYDPKLDTA 210
Cdd:cd11243   75 GTNAGSPKC-------------W-------------------------------FLVNQTLVTlsaDRGVAPFLPDENSL 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 211 SALINEELYAGvyIDFMGTDAAIFRTLGKQTAMRTDqynSRWLNDPSFIHAELIPdSAERNDDKLYFFFRERSAEA-PQN 289
Cdd:cd11243  111 VLIEGNNVYST--ISGKKGNIPRFRRYGGKKELYTS---DTVMQKPQFVKATLLP-EDEQYQDKIYYFFREDNEDKgPEA 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 290 PAVYARIGRICLNDDGGHCCL-VNKWSTFLKARLVCSVPGEDGietHFDELQDVFVQQTQDVRNPVIYAVFTSSgsvFRG 368
Cdd:cd11243  185 EPNISRVARLCKEDQGGTSSLsTSKWSTFLKARLVCGDPATPM---NFNRLQDVFLLPKEEWREAVVYGVFSNT---WGS 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 369 SAVCVYSMADIRMVFNgpfahkegpNYQWMPFSGKMPYPRPGTC-PGGTFTPSmkstkdypdEVINFMRTHPLMYQAVYP 447
Cdd:cd11243  259 SAVCSYSLGDIDKVFR---------TSSLKGYSGSLPNPRPGTCvPPEQTHPS---------ETFSFADEHPELDDRIEP 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 448 LQRRPLVVRTGApYRLTTVAVDQVDAADGR-YEVLFLGTDRGTVQKVIVLPKDDqeveeLMLEEVEVFKEPAPVKTMTIS 526
Cdd:cd11243  321 DEPRKLPVFQNK-DHYQKVVVDEVRASDGVsYDVLYLATDKGKIHKVVESKGQT-----HNIMEIQPFKEQEPIQSMILD 394
                        490
                 ....*....|....*....
gi 341942018 527 SKRQQLYVASAVGVTHLSL 545
Cdd:cd11243  395 AERSHLYVGTKAEVTRLPL 413
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
56-541 2.96e-45

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: 167.38  E-value: 2.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  56 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLII----HWAASPQRIEECILSGKDGNgECGNFVRLIQPWNR-THL 130
Cdd:cd09295    1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLSCIspelNFGFNEDQKAFCPLRRGKWT-ECINYIKVLQQKGDlDIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 131 YVCGTGAYNPMC-TYvnrgrraqalpwtqmqvvrgrgsratdgadrptptapRQDYIFYLEPEKLESGKGKCPYDPKLDT 209
Cdd:cd09295   80 AVCGSNAAQPSCgSY-------------------------------------RLDVLVELGKVRWPSGRPRCPIDNKHSN 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 210 ASALINEELYAGVYIDFM-GTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSaernDDKLYFFFRERSAEAPQ 288
Cdd:cd09295  123 MGVNVDSKLYSATDHDFKdGDRPALSRRSSNVHYLRIVVDSSTGLDEITFVYAFVSGDD----DDEVYFFFRQEPVEYLK 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 289 NPAVY-ARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDgieTHFDELQDVFVQQTQDVRNpVIYAVFTSSGSVFR 367
Cdd:cd09295  199 KGMVYvPRIARVCKLDVGGCHRLKKKLTSFLKADLNCSRPQSG---FAFNLLQDATGDTKNLIQD-VKFAIFSSCLNKSV 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 368 GSAVCVYSMADIRMVFNGPfahkegpnyqwmpfsgkmpyprpgtcpggtftpsmkstkdypdevinfmrthplmyqaVYP 447
Cdd:cd09295  275 ESAVCAYLFTDINNVFDDP----------------------------------------------------------VEA 296
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 448 LQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVlpkDDQEVEELMLEEVEVFKEPAPVKTMTISS 527
Cdd:cd09295  297 INNRPLYAHQNQRSRLTSIAVDATKQKSVGYQVVFLGLKLGSLGKALA---FFFLYKGHIIEEWKVFKDSSRITNLDLSR 373
                        490
                 ....*....|....
gi 341942018 528 KRQQLYVASAVGVT 541
Cdd:cd09295  374 PPLYLYVGSESGVL 387
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
608-697 1.30e-37

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: 135.55  E-value: 1.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 608 NAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPSDRRREIRAEDRFLRTEQGLLLRALQLGDRGLYSCTATENNFKH 687
Cdd:cd05871    1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                         90
                 ....*....|
gi 341942018 688 IVTRVQLHVL 697
Cdd:cd05871   81 TLVKIRLHVI 90
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
618-699 1.19e-12

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: 64.02  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 618 AGSAAFLECQPRSPQATVKWLFQRDPSDRRReirAEDRFLRTEQGLLLRALQLGDRGLYSCTATENNFKHIVTRVQLHVL 697
Cdd:cd04979   10 EGDTVILSCSVKSNNAPVTWIHNGKKVPRYR---SPRLVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSVTLHVL 86

                 ..
gi 341942018 698 GR 699
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 ...
462-588 1.48e-07

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


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 54.94  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 462 RLTTVAVDQVDAadgrYEVLFLGTDRGTVQKVIVlpkDDQEVEELMLEEVEVFKEPAPV-KTMTISSKRQQLYVASAVGV 540
Cdd:cd11272  394 RLTSVASYVYNG----YSVVFVGTKSGKLKKIRA---DGPPHGGVQYEMVSVFKDGSPIlRDMAFSIDHKYLYVMSERQV 466
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 341942018 541 THLSLHRCQAYgAACADCCLARDPYCAWdgqaCSRYTASSKR-RSRRQD 588
Cdd:cd11272  467 SRVPVESCEQY-TTCGECLSSGDPHCGW----CALHNMCSRRdKCQRAW 510
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
547-584 2.55e-07

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 47.92  E-value: 2.55e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 341942018   547 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRS 584
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
276-498 5.79e-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: 52.72  E-value: 5.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 276 YFFFRERSAEAPQNPaVYARIGRICLNDdgghcclvNKWSTFLKARLVCSvpGEDGieTHFDELQDVFV---------QQ 346
Cdd:cd11236  196 YFVTVQRKSVDDESP-YISRLVRVCQSD--------SNYYSYTEVPLQCT--GGDG--TNYNLLQAAYVgkagsdlarSL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 347 TQDVRNPVIYAVF----TSSGSVFRGSAVCVYSMADIRMVFNgpfahkegpnyqwmpfsgkmpyprpgtcpggtftpsmk 422
Cdd:cd11236  263 GISTDDDVLFGVFskskGPSAEPSSKSALCVFSMKDIEAAFN-------------------------------------- 304
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341942018 423 stkdypdevinfmRTHPLmyQAVYPLQRRPLVVRTgapyRLTTVAVDQVDaadgRYEVLFLGTDRGTVQKVIVLPK 498
Cdd:cd11236  305 -------------DNCPL--GGGVPITTSAVLSDS----LLTSVAVTTTR----NHTVAFLGTSDGQLKKVVLESS 357
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
612-696 1.57e-06

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: 46.73  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018   612 SVQYGVAGSAAFLECQPRS-PQATVKWLFQRDpsdrrREIRAEDRFLRTEQG----LLLRALQLGDRGLYSCTATENNFK 686
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGsPPPEVTWYKQGG-----KLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATNSSGS 76
                           90
                   ....*....|
gi 341942018   687 HIVTrVQLHV 696
Cdd:smart00410  77 ASSG-TTLTV 85
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
267-501 4.05e-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: 49.93  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 267 SAERNDDKLYFFFRERSAEAPQNPAVYarIGRICLNDdgghcclvNKWSTFLKARLVCsvpgEDGIETHFDELQDVFVQQ 346
Cdd:cd11245  188 YAFADNGYIYFLFSRRPGTADSTKRTY--ISRLCEND--------HHYYSYVELPLNC----TVNQENTYNLVQAAYLAK 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 347 TQDVRN-PVIYAVFTSSGSVFRG----SAVCVYSMADIRMVFN--------GPFAHKEGPNYQWMPFSGK-----MPYPR 408
Cdd:cd11245  254 PGKVLNgKVLFGVFSADEASTAApdgrSALCMYPLSSVDARFErtrescytGEGLEDDKPETAYIEYNVKsicktLPDKN 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 409 PGTCP-GGTFTPSmkstkdypdevinfmrthPLMYQavYPLQRRPLVVRtgaPYRLTTVAVdqvdAADGRYEVLFLGTDR 487
Cdd:cd11245  334 VKAYPcGAEHTPS------------------PLASR--YPLAAKPILTR---NDMLTAVAV----AVENGHTIAFLGDSG 386
                        250
                 ....*....|....
gi 341942018 488 GTVQKVIVLPKDDQ 501
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 ...
624-696 1.23e-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: 44.31  E-value: 1.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341942018 624 LECQPR-SPQATVKWLFQRDPSDRRREiraedRFLRTEQGLLLRALQLGDRGLYSCTATeNNFKHIVTRVQLHV 696
Cdd:cd20978   21 LPCQVTgVPQPKITWLHNGKPLQGPME-----RATVEDGTLTIINVQPEDTGYYGCVAT-NEIGDIYTETLLHV 88
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
272-493 3.62e-05

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


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 47.08  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 272 DDKLYFFFRERSAEAPQNPAVYarIGRICLNDDGGHcclvnkwsTFLKARLVCSVPgedgiETHFDELQDVFV------- 344
Cdd:cd11276  198 DNNYVYFLFNQQLGHPDKNRTL--IARLCENDHHYY--------SYTEMDLNCRDG-----ANAYNKCQAAYVstpgkel 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 345 -QQTQDVR--NPVIYAVFTSSGSVFRGSAVCVYSMADI--RMVFNGPFAH---KEGPNYQWMPFSGKMPyprpgtCPGGT 416
Cdd:cd11276  263 aQNYGNSIlsDKVLFAVFSRDEKDSGESALCMFPLKSInaKMEANREACYtgtIDDRDVFYKPFHSQKD------IICGS 336
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341942018 417 FTPsmKSTKDYP--DEVInfmrTHPLMYQAVYPLqRRPLVVRTGApyRLTTVAVdqvdAADGRYEVLFLGTDRGTVQKV 493
Cdd:cd11276  337 HQQ--KNSKSFPcgSEHL----PYPLGSRDELAL-TAPVLQRGGL--NLTAVTV----AVENGHTVAFLGTSDGRILKV 402
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
622-681 2.34e-04

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: 40.01  E-value: 2.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341942018 622 AFLECQPR-SPQATVKWLfqRDPSDRRREIRAEDRFLRTEQGLLLRALQLGDRGLYSCTAT 681
Cdd:cd00096    1 VTLTCSASgNPPPTITWY--KNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
619-697 5.84e-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: 39.41  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 619 GSAAFLECQPRSPQATVKWLFQRDPsdrrreIRAED-RFLRTEQGLLLRALQLGDRGLYSCTATEN-NFKHIVTRVQLHV 696
Cdd:cd05873   11 GGNAELKCSPKSNLARVVWKFQGKV------LKAESpKYGLYGDGLLIFNASEADAGRYQCLSVEKsKAKTFFQTVAKYV 84

                 .
gi 341942018 697 L 697
Cdd:cd05873   85 L 85
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
547-588 8.04e-04

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: 38.07  E-value: 8.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 341942018  547 RCQAYGAaCADCCLARDPYCAWD--GQACSRYTASSKRRSRRQD 588
Cdd:pfam01437   1 RCSQYTS-CSSCLAARDPYCGWCssEGRCVRRSACGAPEGNCEE 43
I-set pfam07679
Immunoglobulin I-set domain;
619-696 9.24e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.78  E-value: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018  619 GSAAFLECQPR-SPQATVKWLFQRDP--SDRRREIRAEDrflrTEQGLLLRALQLGDRGLYSCTATeNNFKHIVTRVQLH 695
Cdd:pfam07679  15 GESARFTCTVTgTPDPEVSWFKDGQPlrSSDRFKVTYEG----GTYTLTISNVQPDDSGKYTCVAT-NSAGEAEASAELT 89

                  .
gi 341942018  696 V 696
Cdd:pfam07679  90 V 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
612-681 3.41e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.16  E-value: 3.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341942018  612 SVQYGVAGSAAFLECQPR-SPQATVKWLFqrdPSDRRREIRAEDRFLRTEQGLL-LRALQLGDRGLYSCTAT 681
Cdd:pfam13927   9 SSVTVREGETVTLTCEATgSPPPTITWYK---NGEPISSGSTRSRSLSGSNSTLtISNVTRSDAGTYTCVAS 77
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
607-685 3.86e-03

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: 37.05  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341942018 607 KNAVESVQYGVAGSAAFLECQPR-SPQATVKWlfqrdpSDRRREIRAEDRFLRTEQG-LLLRALQLGDRGLYSCTAtENN 684
Cdd:cd04969    5 LNPVKKKILAAKGGDVIIECKPKaSPKPTISW------SKGTELLTNSSRICILPDGsLKIKNVTKSDEGKYTCFA-VNF 77

                 .
gi 341942018 685 F 685
Cdd:cd04969   78 F 78
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH