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Conserved domains on  [gi|281182586|ref|NP_001094352|]
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semaphorin-3G precursor [Rattus norvegicus]

Protein Classification

semaphorin-3( domain architecture ID 10336818)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema super family cl15693
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
50-523 0e+00

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


The actual alignment was detected with superfamily member cd11255:

Pssm-ID: 472829 [Multi-domain]  Cd Length: 474  Bit Score: 940.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  50 FLGPRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNR 129
Cdd:cd11255    1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 130 THLLACGTGAFQPICTFITVGHRGEHVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGP 209
Cdd:cd11255   81 THLLACGTGAFQPVCALINVGHRGEHVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 210 RPALRSDSDQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETVPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFL 289
Cdd:cd11255  161 RSPLRTETDQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETAEDDDGAIHSRVGRLCANDAGGQRVLVNKWSTFI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 290 KARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWG 369
Cdd:cd11255  241 KARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 370 PYGGKVPFPRPGVCPSKMTAQPGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAED 449
Cdd:cd11255  321 PYEGKVPYPRPGVCPSKITAQPGRAFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEAED 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182586 450 GTYDVIFLGTDSGSVLKIIALQGSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11255  401 GYYDVMFIGTDSGSVLKVIVLQKGNSAAGEEVTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
591-676 2.75e-41

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: 145.57  E-value: 2.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 591 VFGTEHNSTFLECRPKSPQAAVRWFLQRPGDKGADQVKTDERVVQTDQGLLFRRLSRLDAGNYTCTTLEHGFSQTVVRFA 670
Cdd:cd05871    7 VYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQTLVKIR 86

                 ....*.
gi 281182586 671 LEVIAA 676
Cdd:cd05871   87 LHVIEP 92
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
522-568 1.75e-04

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 39.84  E-value: 1.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 281182586   522 QCETYGSaCAECCLARDPYCAWD--GTSCARYRPSSgkrrFRRQDIRHG 568
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCD----SRRQNWLSG 44
 
Name Accession Description Interval E-value
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
50-523 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: 940.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  50 FLGPRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNR 129
Cdd:cd11255    1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 130 THLLACGTGAFQPICTFITVGHRGEHVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGP 209
Cdd:cd11255   81 THLLACGTGAFQPVCALINVGHRGEHVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 210 RPALRSDSDQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETVPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFL 289
Cdd:cd11255  161 RSPLRTETDQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETAEDDDGAIHSRVGRLCANDAGGQRVLVNKWSTFI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 290 KARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWG 369
Cdd:cd11255  241 KARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 370 PYGGKVPFPRPGVCPSKMTAQPGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAED 449
Cdd:cd11255  321 PYEGKVPYPRPGVCPSKITAQPGRAFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEAED 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182586 450 GTYDVIFLGTDSGSVLKIIALQGSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11255  401 GYYDVMFIGTDSGSVLKVIVLQKGNSAAGEEVTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema smart00630
semaphorin domain;
59-495 8.00e-138

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 412.53  E-value: 8.00e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586    59 LQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGTG 138
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   139 AFQPICTFITVGhrgehvlhldpssiengrgrcphepsrpfastfvggELYTGLTADFLGREAMIFRSGGPRPaLRSDSD 218
Cdd:smart00630  81 AFQPVCRLRNLG------------------------------------ELYVGTVADFSGSDPAIPRSLSVRR-LKGTSG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   219 QSL---------LHDPRFVmaaripdNSDRDDDKVYFFFSETvPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFL 289
Cdd:smart00630 124 VSLrtvlydskwLNEPNFV-------YAFESGDFVYFFFRET-AVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFL 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   290 KARLVCSVPGPGGaeTHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWG 369
Cdd:smart00630 196 KARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWL 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   370 PY-GGKVPFPRPGVCPSKMtaqpgrpfGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVeAE 448
Cdd:smart00630 274 PYsRGKVPYPRPGTCPNKP--------PSSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-AT 344
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 281182586   449 DGTYDVIFLGTDSGSVLKIIALQGSGlpEPEEVVLEELQVFKVPTPI 495
Cdd:smart00630 345 DGNYTVLFLGTSDGRILKVVLSESSS--SSESVVLEEISVFPDGSPI 389
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
310-501 1.09e-61

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: 205.20  E-value: 1.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  310 LEDVFLLWPKAG--KNLEVYALFST-VSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGKVPFPRPGVCPSK 386
Cdd:pfam01403   1 LQDVFVLKPGAGdaLDTVLYGVFTTqWSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  387 MtaqpgrpfgSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLaqQLCQIVVDRVEAEDGTYDVIFLGTDSGSVLK 466
Cdd:pfam01403  81 P---------LRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGV--RLTSIAVDRVQALDGNYTVLFLGTDDGRLHK 149
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 281182586  467 IIALQGSGlpepeEVVLEELQVFKVPTPITEMEIS 501
Cdd:pfam01403 150 VVLVGSEE-----SHIIEEIQVFPEPQPVLNLLLS 179
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
591-676 2.75e-41

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: 145.57  E-value: 2.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 591 VFGTEHNSTFLECRPKSPQAAVRWFLQRPGDKGADQVKTDERVVQTDQGLLFRRLSRLDAGNYTCTTLEHGFSQTVVRFA 670
Cdd:cd05871    7 VYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQTLVKIR 86

                 ....*.
gi 281182586 671 LEVIAA 676
Cdd:cd05871   87 LHVIEP 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
591-668 9.43e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.19  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  591 VFGTEHNSTFLEC--RPKSPQAAVRWFLQRPGDKGADQVKTDERVvQTDQGLLFRRLSRLDAGNYTCTTLEHGFSQTVVR 668
Cdd:pfam00047   6 VTVLEGDSATLTCsaSTGSPGPDVTWSKEGGTLIESLKVKHDNGR-TTQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
522-568 1.75e-04

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 39.84  E-value: 1.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 281182586   522 QCETYGSaCAECCLARDPYCAWD--GTSCARYRPSSgkrrFRRQDIRHG 568
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCD----SRRQNWLSG 44
 
Name Accession Description Interval E-value
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
50-523 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: 940.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  50 FLGPRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNR 129
Cdd:cd11255    1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 130 THLLACGTGAFQPICTFITVGHRGEHVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGP 209
Cdd:cd11255   81 THLLACGTGAFQPVCALINVGHRGEHVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 210 RPALRSDSDQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETVPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFL 289
Cdd:cd11255  161 RSPLRTETDQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATETAEDDDGAIHSRVGRLCANDAGGQRVLVNKWSTFI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 290 KARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWG 369
Cdd:cd11255  241 KARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGPDHQWG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 370 PYGGKVPFPRPGVCPSKMTAQPGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAED 449
Cdd:cd11255  321 PYEGKVPYPRPGVCPSKITAQPGRAFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDRVEAED 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182586 450 GTYDVIFLGTDSGSVLKIIALQGSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11255  401 GYYDVMFIGTDSGSVLKVIVLQKGNSAAGEEVTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
50-523 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: 737.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  50 FLGPRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNR 129
Cdd:cd11239    1 FLGSMNSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPKKIYWPASPERIEECKMAGKDPNTECANFVRVLQPYNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 130 THLLACGTGAFQPICTFITVGHRGEH-VLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGG 208
Cdd:cd11239   81 THLYACGTGAFHPICAFINVGRRLEDpIFKLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 209 PRPALRSDSDQS-LLHDPRFVMAARIPDNSDRDDDKVYFFFSETvpSPDGGP-GHVTVSRVGRVCVNDAGGQRVLVNKWS 286
Cdd:cd11239  161 HRHYIRTEQYDSrWLNEPKFVGAYLIPDSDNPDDDKVYFFFREK--AVEAEGsGKAIYSRVGRICKNDVGGQRSLVNKWS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 287 TFLKARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQH 366
Cdd:cd11239  239 TFLKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPNY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 367 QWGPYGGKVPFPRPGVCPSKMTaqpGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVE 446
Cdd:cd11239  319 QWVEYQGKVPYPRPGTCPSKTY---GPLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPYRLTQIAVDRVE 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281182586 447 AEDGTYDVIFLGTDSGSVLKIIALQgSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11239  396 AEDGQYDVLFIGTDSGTVLKVVSLP-KENWEMEEVILEELQVFKHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
50-523 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: 632.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  50 FLGPRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPHNR 129
Cdd:cd11253    1 FHSPFGFLDLHTMLLDEYQERLFVGGRDLLYSLSLERISANYKEIHWPSTQLQVEDCIMKGRDK-PECANYIRVLHHYNR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 130 THLLACGTGAFQPICTFITVGHRGE-HVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGG 208
Cdd:cd11253   80 THLLACGTGAFDPVCAFIRVGRGSEdHLFQLESDKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 209 PRPALRSD-SDQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETVPSPDGGpGHVTVSRVGRVCVNDAGGQRVLVNKWST 287
Cdd:cd11253  160 HLAHIRTEhDDERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGG-NHAIYTRVGRVCANDQGGQRMLVNKWST 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 288 FLKARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQ 367
Cdd:cd11253  239 FLKTRLICSVPGPNGIDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYH 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 368 WGPYGGKVPFPRPGVCPSKMTaqpGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEA 447
Cdd:cd11253  319 WSVYEGKVPYPRPGSCASKVN---GGHYGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNLKQIAVDRVEA 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182586 448 EDGTYDVIFLGTDSGSVLKIIALQGSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11253  396 EDGQYDVLFIGTDNGIVLKVITIYNQETETMEEVILEELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
29-524 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: 564.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  29 TSVPRLRLSYRDLLTTNRSAIFLGPRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAwPDPREVLWPPQPGQKVECVR 108
Cdd:cd11249    2 NNVPRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNI-KDFQKIVWPVSPSRRDECKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 109 KGKDPLTECANFVRVLQPHNRTHLLACGTGAFQPICTFITVGHRGE-HVLHLDPSSIENGRGRCPHEPSRPFASTFVGGE 187
Cdd:cd11249   81 AGKDILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEdNIFRLEDSHFENGRGKSPYDPKLLTASLLIDGE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 188 LYTGLTADFLGREAMIFRSGGPRPALRSDS-DQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETvpSPDG-GPGHVTVS 265
Cdd:cd11249  161 LYSGTAADFMGRDFAIFRTLGHHHPIRTEQhDSRWLNDPRFISAHLIPESDNPEDDKIYFFFREN--AIDGeHTGKATHA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 266 RVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVY 345
Cdd:cd11249  239 RIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVCMY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 346 HMVDIWEVFNGPFAHRDGPQHQWGPYGGKVPFPRPGVCPSKMTAQpgrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGR 425
Cdd:cd11249  319 SMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGG----FDSTKDLPDDVITFARSHPAMYNPVFPINNR 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 426 PVLVKTHLAQQLCQIVVDRVEAEDGTYDVIFLGTDSGSVLKIIALQGSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQ 505
Cdd:cd11249  395 PIIIKTDVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETWHDLEEVLLEEMTVFREPTAISAMELSTKQQ 474
                        490
                 ....*....|....*....
gi 281182586 506 TLYVGSPLGVARLQLHQCE 524
Cdd:cd11249  475 QLYIGSAIGVSQLPLHRCD 493
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
60-523 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: 560.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  60 QVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGTGA 139
Cdd:cd11250   11 DALLLDEERGRLFVGAKNYLASLSLDNISKQEKKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHLYACGTGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 140 FQPICTFITVGHRGE-HVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRSDS- 217
Cdd:cd11250   91 FHPTCAFVEVGQRMEdHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRPSLRTEQh 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 218 DQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETVPSPDGGpGHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSV 297
Cdd:cd11250  171 DSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAGL-GKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLVCSV 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 298 PGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGKVPF 377
Cdd:cd11250  250 PGNEGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQGKVPY 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 378 PRPGVCPSKMTAQpgrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAEDGTYDVIFL 457
Cdd:cd11250  330 PRPGMCPSKTFGS----FESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPYTFTQIAVDRVAAADGHYDVMFI 405
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182586 458 GTDSGSVLKIIALQGSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11250  406 GTDVGSVLKVISVPKGSWPSNEELLLEELHVFKDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
58-523 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: 554.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  58 DLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGT 137
Cdd:cd11254    9 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNRTHLYVCGT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 138 GAFQPICTFITVGHRGE-HVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRSD 216
Cdd:cd11254   89 GAYNPVCAYINRGRRAEdYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMGKQPAMRTD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 217 S-DQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETvpSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVC 295
Cdd:cd11254  169 QyNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREK--SLEAPQSPAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARLVC 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 296 SVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGKV 375
Cdd:cd11254  247 SVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTGKI 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 376 PFPRPGVCPSKmTAQPGrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAEDGTYDVI 455
Cdd:cd11254  327 PYPRPGTCPGG-TFTPS--MKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGRYEVL 403
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281182586 456 FLGTDSGSVLKIIALQgSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11254  404 FLGTDRGTVQKVIVLP-KDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
50-523 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: 535.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  50 FLGPRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPgQKVE-CVRKGKDPLTECANFVRVLQPHN 128
Cdd:cd11252    1 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAK-ERVElCKLAGKDANTECANFIRVLHPYN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 129 RTHLLACGTGAFQPICTFITVG-HRGEHVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSG 207
Cdd:cd11252   80 RTHVYVCGTGAFHPTCGYIELGtHKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 208 GPRPA---LRSD-SDQSLLHDPRFVMAARIPDNSDRDDDKVYFFFSETvpSPDGGPGHVTV-SRVGRVCVNDAGGQRVLV 282
Cdd:cd11252  160 GPTPDhhyIRTDiSEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREA--SQDGSTSDKSVlSRVGRVCKNDVGGQRSLI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 283 NKWSTFLKARLVCSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRD 362
Cdd:cd11252  238 NKWTTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 363 GPQHQWGPYGGKVPFPRPGVCPSKmTAQPgrPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVV 442
Cdd:cd11252  318 SPDHRWVQYEGRIPYPRPGTCPSK-TYDP--LIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVV 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 443 DRVEAEDGTYDVIFLGTDSGSVLKIIALQGSgLPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQ 522
Cdd:cd11252  395 DHVAAEDGQYDVMFLGTDIGTVLKVVSITKE-KWTMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHR 473

                 .
gi 281182586 523 C 523
Cdd:cd11252  474 C 474
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
57-523 8.44e-167

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: 489.79  E-value: 8.44e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  57 LDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACG 136
Cdd:cd11251    8 LDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNRTHLYVCG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 137 TGAFQPICTFITVGHRGE-HVLHLDpSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRS 215
Cdd:cd11251   88 SGAFSPVCVYVNRGRRSEeQVFHID-SKAESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 216 DSDQS-LLHDPRFVMAARIPDNSDRDDDKVYFFFSETVPSPDGGPGHVTvSRVGRVCVNDAGGQRVLVNKWSTFLKARLV 294
Cdd:cd11251  167 DQHNSkWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTKQIH-SMIARVCPNDTGGQRSLVNKWTTFLKARLV 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 295 CSVPGPGGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGK 374
Cdd:cd11251  246 CSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQLIAYQGR 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 375 VPFPRPGVCPSKMTAQPGRpfgSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAEDGTYDV 454
Cdd:cd11251  326 IPYPRPGTCPGGAFTPNMQ---STKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGRYHV 402
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182586 455 IFLGTDSGSVLKIIALQGSGlPEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLHQC 523
Cdd:cd11251  403 LFLGTDKGTVQKVVVLPTNG-SLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
64-521 2.27e-139

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: 418.35  E-value: 2.27e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  64 LDEYRDRLFLGGRDALYSLRLDQAWPDpREVLWPPQPGQKVECVRKGKDpLTECANFVRVLQPHNRTHLLACGTGAFQPI 143
Cdd:cd11235    8 LHEDRSTLYVGARDRVYLVDLDSLYTE-QKVAWPSSPDDVDTCYLKGKS-KDDCRNFIKVLEKNSDDSLLVCGTNAFNPS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 144 CTFITVGHrgehvLHLDpSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRS-DSDQSLL 222
Cdd:cd11235   86 CRNYNVET-----FELV-GKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTeYHDSKWL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 223 HDPRFVMAARIPDnsdrdddKVYFFFSETvpSPDGGP-GHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVPGpg 301
Cdd:cd11235  160 NEPQFVGAFDIGD-------YVYFFFREI--AVEYINcGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPG-- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 302 GAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPY-GGKVPFPRP 380
Cdd:cd11235  229 EFPFYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVpDERVPEPRP 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 381 GVCpskmtaqpgrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEA-EDGTYDVIFLGT 459
Cdd:cd11235  309 GTC-----------VDDSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDVNYRFTKIAVDRVQAkLGQTYDVLFVGT 377
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281182586 460 DSGSVLKIIALQGSGlpEPEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQLH 521
Cdd:cd11235  378 DRGIILKVVSLPEQG--LQASNILEEMPVGPPPEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema smart00630
semaphorin domain;
59-495 8.00e-138

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 412.53  E-value: 8.00e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586    59 LQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGTG 138
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   139 AFQPICTFITVGhrgehvlhldpssiengrgrcphepsrpfastfvggELYTGLTADFLGREAMIFRSGGPRPaLRSDSD 218
Cdd:smart00630  81 AFQPVCRLRNLG------------------------------------ELYVGTVADFSGSDPAIPRSLSVRR-LKGTSG 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   219 QSL---------LHDPRFVmaaripdNSDRDDDKVYFFFSETvPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFL 289
Cdd:smart00630 124 VSLrtvlydskwLNEPNFV-------YAFESGDFVYFFFRET-AVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFL 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   290 KARLVCSVPGPGGaeTHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWG 369
Cdd:smart00630 196 KARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWL 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586   370 PY-GGKVPFPRPGVCPSKMtaqpgrpfGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVeAE 448
Cdd:smart00630 274 PYsRGKVPYPRPGTCPNKP--------PSSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-AT 344
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 281182586   449 DGTYDVIFLGTDSGSVLKIIALQGSGlpEPEEVVLEELQVFKVPTPI 495
Cdd:smart00630 345 DGNYTVLFLGTSDGRILKVVLSESSS--SSESVVLEEISVFPDGSPI 389
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
55-520 5.28e-136

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: 410.26  E-value: 5.28e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  55 GSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPD-PREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLL 133
Cdd:cd11240    5 GIQNYSTLLLSEDEGTLYVGAREALFALNVSDISTElKDKIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYNSTHLY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 134 ACGTGAFQPICTFITVGHrgehvLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPAL 213
Cdd:cd11240   85 VCGTFAFSPRCTYINLSD-----FSLSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEGNVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 214 RSDSDQSLLHDPRFVMAARIP---DNSDRDDDKVYFFFSETVPSPDgGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFLK 290
Cdd:cd11240  160 KTENTLRWLNEPAFVGSAHIResiDSPDGDDDKIYFFFTETAVEYD-FYEKVTVSRVARVCKGDLGGQRTLQKKWTTFLK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 291 ARLVCSVPgpgGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGP 370
Cdd:cd11240  239 AQLVCSQP---DSGLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWSR 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 371 YGGKVPFPRPGVCPSKMTAqpGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPrRGRPVLVKThlAQQLCQIVVDRVEAEDG 450
Cdd:cd11240  316 YTGPVPDPRPGACITNSAR--SQGITSSLNLPDNVLTFVKDHPLMDEQVHP-INRPLLVKS--GVNYTRIAVHRVQALDG 390
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182586 451 -TYDVIFLGTDSGSVLKIIALQGSglpepeEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd11240  391 qTYTVLFLGTEDGFLHKAVSLDGG------MHIIEEIQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
64-520 2.89e-112

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: 348.68  E-value: 2.89e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  64 LDEYRDRLFLGGRDALYSLRL-DQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGTGAFQP 142
Cdd:cd11262   15 LEDESGRLYVGARGAIFSLNAsDISDSSALTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRFNSTHLYTCGTHAFRP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 143 ICTFITVGhrgEHVLhldPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFlgREAMIFRSGGPRPALRS-DSDQSL 221
Cdd:cd11262   95 LCAYIDAE---RFTL---SSQFEEGKEKCPYDPAKGYTGLIVDGQLYTASQYEF--RSFPDIRRNSPQPTLRTeEAPTRW 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 222 LHDPRFVMAARIP---DNSDRDDDKVYFFFSETVPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVP 298
Cdd:cd11262  167 LNDADFVGSVLVResmNSSVGDDDKIYFFFTERSQEETAYFSQSRVARVARVCKGDRGGKKTLQRKWTSFLKARLVCYIP 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 299 gpgGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGKVPFP 378
Cdd:cd11262  247 ---EYEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYTGKVPEP 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 379 RPGVCPSKmtAQPGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLaqQLCQIVVDRVEAEDG-TYDVIFL 457
Cdd:cd11262  324 RPGSCITD--EHRSQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNV--IYTKIAVQTVRGLDGrVYDVLFL 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281182586 458 GTDSGSVLKIIALqGSGlpepeEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd11262  400 GTDEGWLHKAVVI-GSA-----VHIIEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
62-520 8.09e-97

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: 308.37  E-value: 8.09e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  62 MYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGTGAFQ 141
Cdd:cd11260   12 MLLREDLGLLVLGAREAVFALDLNDISVKRAKVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMNDSRMYVCGTNAFS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 142 PICTFITVghrGEHVLHLDpSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGgpRPALRSDSDQSL 221
Cdd:cd11260   92 PTCDYISY---DDGQLTLE-GKQEDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRSS--PITIRTEFKSSW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 222 LHDPRFVMAARIP---DNSDRDDDKVYFFFSETVPSPDgGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVP 298
Cdd:cd11260  166 LNEPNFIYMAAVPeseDSPEGDDDKIYLFFSETAVEYD-FYNKLVVSRVARVCKGDLGGQRTLQKKWTSFLKARLDCSVP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 299 gpggaETHFDQL-EDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFN-----GPFAhRDGPQHQWGPYG 372
Cdd:cd11260  245 -----EPSLPYViQDVFHVCHQDWRKCVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrgkfkTPVA-VETSFVKWVMYS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 373 GKVPFPRPGVCPSKMTAQPGrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAqqLCQIVVDRVEAEDGT- 451
Cdd:cd11260  319 GELPVPRPGACINNAARTSG--IKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGAL--FTRIVVDMVTAADGQs 394
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182586 452 YDVIFLGTDSGSVLKIIALQGSglpepeEVVLEELQVFKVPTPITEMEISVKrqTLYVGSPLGVARLQL 520
Cdd:cd11260  395 YPVMFIGTANGYVLKAVNYDGE------MHIIEEVQLFEPEEPIDILRLSQN--QLYAGSASGVVQMPV 455
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
62-515 1.79e-95

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: 305.63  E-value: 1.79e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  62 MYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLACGTGAFQ 141
Cdd:cd11259   23 LLLSEDKDVLYVGAREAVFALNALNISEKQHELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLNDTFLYVCGTNAFQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 142 PICTFITVGHrgehvLHLDPSSiENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSgGPRPALRSDSDQSL 221
Cdd:cd11259  103 PTCDYLNLTS-----FRLLGKN-EDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRN-SSQSPLRTEYAIPW 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 222 LHDPRFVMAARI---PDNSDRDDDKVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVP 298
Cdd:cd11259  176 LNEPSFVFADVIradPDSPDGEDDKIYFFFTE-VSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSIP 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 299 GPGGAethFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFN-GPFAHR---DGPQHQWGPYGGK 374
Cdd:cd11259  255 DKNLV---FNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHTKWVRYNGE 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 375 VPFPRPGVCPSKMTAQPGrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLaqQLCQIVVDRVEAEDGT-YD 453
Cdd:cd11259  332 VPKPRPGACINNEARAAN--YTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDV--NYTQIVVDRVQALDGTiYD 407
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281182586 454 VIFLGTDSGSVLKIIALQGSglpepeEVVLEELQVFKVPTPITEMEISVK--RQTLYVGSPLGV 515
Cdd:cd11259  408 VMFISTDRGALHKAISLENE------VHIIEETQLFPDFEPVQTLLLSSKkgRRFLYAGSNSGV 465
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
53-520 8.19e-95

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: 303.32  E-value: 8.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  53 PRGSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDP--REVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRT 130
Cdd:cd11257    4 AEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISPTGeqQELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRLNST 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 131 HLLACGTGAFQPICTFITVGH-------RGEHVLhldpssiENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMI 203
Cdd:cd11257   84 HLFTCGTYAFSPICTYIVMTNfslerdeKGEPLL-------EDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPII 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 204 FRSGGPRPALRSDSDQSLLHDPRFVMAARIPDN---SDRDDDKVYFFFSETVPSPDGGPGHVtVSRVGRVCVNDAGGQRV 280
Cdd:cd11257  157 YRSLGSGTPLKTENSLNWLQDPAFVGSAYIQESlpkLVGDDDKIYFFFSETGKEFDFFENTI-VSRIARVCKGDEGGERV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 281 LVNKWSTFLKARLVCSVPGPGGAethFDQLEDVFLLWP--KAGKNLEVYALFStvSAVFRGF----AVCVYHMVDIWEVF 354
Cdd:cd11257  236 LQKRWTTFLKAQLLCSLPDDGFP---FNVLQDVFVLTPspEDWKDTLFYGVFT--SQWHKGTagssAVCVFTMDQVQRAF 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 355 NGPFAHRDGPQHQWGPYGGKVPFPRPGVCPSKMTAQpgRPFGSTKDYPDEVLQFVRGHPLMFQPVrprRGRPVLVKTHLA 434
Cdd:cd11257  311 NGLYKEVNRETQQWYTYTHPVPEPRPGACITNSARE--RKINSSLHMPDRVLNFVKDHFLMDGQV---RSQPLLLQPQVR 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 435 QQlcQIVVDRVEAEDGTYDVIFLGTDSGSVLKIIALQGsglpepEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLG 514
Cdd:cd11257  386 YT--QIAVHRVKGLHKTYDVLFLGTDDGRLHKAVSVGP------MVHIIEELQIFSEGQPVQNLLLDTHKGLLYASSHSG 457

                 ....*.
gi 281182586 515 VARLQL 520
Cdd:cd11257  458 VVQVPV 463
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
55-520 4.38e-94

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: 301.34  E-value: 4.38e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  55 GSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPrEVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLA 134
Cdd:cd11258    8 GVSNYTTLTLAEHRGLLYVGAREAIFALSLSNIELQP-PISWEAPAEKKTECAQKGKSNQTECFNYIRFLQPYNQSHLYT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 135 CGTGAFQPICTFITVGHrgehvLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALR 214
Cdd:cd11258   87 CGTYAFQPKCAYINMLT-----FTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQHYSMK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 215 SDSDQSLLHDPRFVMAARIPD--NSDR-DDDKVYFFFSETVPSPDGGPGHVtVSRVGRVCVNDAGGQRVLVNKWSTFLKA 291
Cdd:cd11258  162 TEYLAFWLNEPHFVGSAFVPEsvGSFTgDDDKIYFFFSERAVEYDCDSEQV-VARVARVCKGDLGGARTLQKKWTTFLKA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 292 RLVCSVPgpgGAETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPY 371
Cdd:cd11258  241 RLLCSIP---EWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKWGRY 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 372 GGKVPFPRPGVCPSKMTAQPGrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKThlAQQLCQIVVDRVEAEDG- 450
Cdd:cd11258  318 TDPVPSPRPGSCINNWHRDHG--YTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPC--NSNFTHVVWTRVLGLDGe 393
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 451 TYDVIFLGTDSGSVLKIIALqGSGlpepeEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd11258  394 TYSVLFIGTLDGWLIKAVSL-GSW-----VHMIEELQVFDQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
64-523 9.15e-88

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: 284.22  E-value: 9.15e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  64 LDEYRDRLFLGGRDALYSLRLDQAWPDPReVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPHNRTHLLACGTGAFQPI 143
Cdd:cd11237   10 LDQDGNSLLVGARNAVYNISLSDLTENQR-IEWPSSDAHREMCLLKGKSE-DDCQNYIRVLAKKSAGRLLVCGTNAYKPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 144 CTFITVgHRGEHVLHLDpssiENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRsgGPRPALRSDSDQslLH 223
Cdd:cd11237   88 CREYTV-KDGGYRVERE----FDGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYR--EPLRTERYDLKQ--LN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 224 DPRFVmaaripdNSDRDDDKVYFFFSET-VPSPDGGPghVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVPGpgg 302
Cdd:cd11237  159 APNFV-------SSFAYGDYVYFFFRETaVEYINCGK--AIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPG--- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 303 aET--HFDQLEDVFLLWPKAGKNLE---VYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPY-GGKVP 376
Cdd:cd11237  227 -EYpfYFNEIQSTSDIVEGGYGGKSaklIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVpSNKVP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 377 FPRPGVCPSKmtaqpgrpfgSTKdYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVD-RVEAEDG-TYDV 454
Cdd:cd11237  306 EPRPGQCVND----------SRT-LPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQYRFTQIAVDpQVKALDGkYYDV 374
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281182586 455 IFLGTDSGSVLKII-ALQGSGLPEPEEVVLEELQVFKVPTPITEMEISVKRQT--LYVGSPLGVARLQLHQC 523
Cdd:cd11237  375 LFIGTDDGKVLKAVnIASADTVDKVSPVVIEETQVFPRGVPIRNLLIVRGKDDgrLVVVSDDEIVSIPLHRC 446
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
58-517 4.71e-86

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: 279.87  E-value: 4.71e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  58 DLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPdPR---EVLWPPQPGQKVECVRKGKDPLTECANFVRVLQPHNRTHLLA 134
Cdd:cd11256    9 NYDQLLLSPDETTLYVGARDNILALGIRTPGP-IRlkhQIPWPANDSKISECAFKKKSNETECFNFIRVLVPVNGTHLYT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 135 CGTGAFQPICTFITVGHrgehvLHLDPSSIE----NGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPR 210
Cdd:cd11256   88 CGTYAFSPACTYIELDH-----FSLPPPNGTiitmDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLGTK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 211 PALRSDSDQSLLH-DPRFVMAARIPdnsdrDDDKVYFFFSETVPSPDGGPgHVTVSRVGRVCVNDAGGQRVLVNKWSTFL 289
Cdd:cd11256  163 VSLKTDGFLRWLNaDAVFVASFNPQ-----GDSKVYFFFEETAREFDFFE-KLTVARVARVCKNDVGGEKLLQKKWTTFL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 290 KARLVCSVPGpggaETHFDQLEDVFLLWPKAGKNLEVYALFSTVSAV--FRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQ 367
Cdd:cd11256  237 KAQLTCSQQG----HFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLggRRSSAVCAYKLNDIEKVFNGKYKELNKESSR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 368 WGPYGGKVPFPRPGVCpskmtaqpgrpfgSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLaqQLCQIVVDRVEA 447
Cdd:cd11256  313 WTRYMGPVSDPRPGSC-------------SGGKSSDKALNFMKDHFLMDEVVLPGAGRPLLVKSNV--QYTRIAVDSVQG 377
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182586 448 EDG-TYDVIFLGTDSGSVLKIIALQGSglpepEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVAR 517
Cdd:cd11256  378 VSGhNYTVMFLGTDKGFLHKAVLMGGS-----ESHIIEEIELLTPPEPVENLLLAANEGVVYIGYSAGVWR 443
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
57-473 9.49e-86

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: 279.79  E-value: 9.49e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  57 LDLQVMYldEYRDRLFLGGRDALYSLRLDQAWPD----PREVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPHNRTHL 132
Cdd:cd11242    9 LDFQRML--RINRTLYIAARDHVYTVDLDASHTEeivpSKKLTWRSRQADVENCRMKGKHK-DECHNFIKVLVPRNDETL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 133 LACGTGAFQPICtfitvghRGEHVLHLDPSSIE-NGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRP 211
Cdd:cd11242   86 FVCGTNAFNPVC-------RNYRIDTLEQDGEEiSGMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSLGDSP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 212 ALRS-DSDQSLLHDPRFVMAARIpdnsdrdDDKVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGG-QRVLVNKWSTFL 289
Cdd:cd11242  159 TLRTvKYDSKWLKEPHFVHAVEY-------GDYVYFFFRE-IAVEYNTLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 290 KARLVCSVPGpgGAETHFDQLEDVFLLWPKAGKNLeVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWG 369
Cdd:cd11242  231 KARLNCSVPG--DSHFYFDVLQAVTDVIRINGRPV-VLGVFTTQYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWT 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 370 PYG-GKVPFPRPGVCpskmtAQPG--RPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVE 446
Cdd:cd11242  308 PVPeDRVPKPRPGCC-----AGSGsaEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYRLTQIAVDNAA 382
                        410       420
                 ....*....|....*....|....*..
gi 281182586 447 AEDGTYDVIFLGTDSGSVLKIIALQGS 473
Cdd:cd11242  383 GPYQNYTVVFLGSEAGTVLKFLARIGP 409
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
55-468 1.80e-84

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: 276.00  E-value: 1.80e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  55 GSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPREVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPHNRTHLLA 134
Cdd:cd11261   10 HTYNYSVLLVDPASHTLYVGARDAIFALTLPFSGERPRRIDWMVPEAHRQNCRKKGKKE-AECHNFIRILAIANASHLLT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 135 CGTGAFQPICTFITVGhRGEHVLHLdpssiENGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRS-GGPRPAL 213
Cdd:cd11261   89 CGTFAFDPKCGVIDVS-SFQQVERL-----ESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAvGRAEEWI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 214 RSDSDQSLLHDPRFVMAA--RIPDNSDRD-DDKVYFFFSETVPSPDGGPgHVTVSRVGRVCVNDAGGQRVLVNKWSTFLK 290
Cdd:cd11261  163 RTETLPSWLNAPAFVAAVflSPAEWGDEDgDDEIYFFFTETAREYDSYE-RIKVPRVARVCAGDLGGRKTLQQRWTTFLK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 291 ARLVCSVPGPGGAethFDQLEDVFLLWPKAGKNLEV-YALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWG 369
Cdd:cd11261  242 ADLLCPGPEHGRA---SSILQDVTTLRPLPGAGTPIfYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGL 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 370 PY-GGKVPFPRPGVCPSKMTAqpGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQlcQIVVDRVEAE 448
Cdd:cd11261  319 PVmDSDVPQPRPGECITNNMK--LLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLLVTTDTAYL--RVAAHRVTSL 394
                        410       420
                 ....*....|....*....|.
gi 281182586 449 DGT-YDVIFLGTDSGSVLKII 468
Cdd:cd11261  395 SGKeYDVLYLGTEDGHLHRAV 415
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
71-468 2.51e-80

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: 265.16  E-value: 2.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  71 LFLGGRDALYSLRLDQAWPDP----REVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPHNRTHLLACGTGAFQPICTF 146
Cdd:cd11267   21 LYIGDRDNLYRVELDPTAGTEmryhKKLTWRSNKNDINVCRMKGKHE-GECRNFIKVLLLRDYGTLFVCGTNAFNPVCAN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 147 ITVghrgeHVLHL--DPSSienGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRS-DSDQSLLH 223
Cdd:cd11267  100 YSI-----DTLEPvgDNIS---GMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRTvKHDSKWFK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 224 DPRFVMAARIPDNsdrdddkVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGG-QRVLVNKWSTFLKARLVCSVPGpgG 302
Cdd:cd11267  172 EPYFVHAVEWGSH-------VYFFFRE-IAMEFNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPG--D 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 303 AETHFDQLEDVFLLWPKAGKNLeVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGK-VPFPRPG 381
Cdd:cd11267  242 SHFYFNVLQAVSDILNLGGRPV-VLAVFSTPTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPVPEElVPRPRPG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 382 VCpskmtAQPGRPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAEDGTYDVIFLGTDS 461
Cdd:cd11267  321 CC-----AAPGMRYNSSSTLPDEVLNFVKTHPLMDEAVPSLGHAPWIVRTMTRYQLTHMVVDTEAGPHGNHTVVFLGSTR 395

                 ....*..
gi 281182586 462 GSVLKII 468
Cdd:cd11267  396 GTVLKFL 402
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
56-469 1.69e-75

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: 252.26  E-value: 1.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  56 SLDLQVMYldEYRDRLFLGGRDALYSLRLDQAWPDP----REVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPHNRTH 131
Cdd:cd11269    8 RLDFQLML--KIRDTLYIAGRDQVYTVNLNEVPKTEvtpsRKLTWRSRQQDRENCAMKGKHK-DECHNFIKVFVPRNDEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 132 LLACGTGAFQPICTFI---TVGHRGEHVlhldpssieNGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGG 208
Cdd:cd11269   85 VFVCGTNAFNPMCRYYrlsTLEYDGEEI---------SGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 209 PRPALRS-DSDQSLLHDPRFVMAARIpdnsdrdDDKVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGG-QRVLVNKWS 286
Cdd:cd11269  156 DGSALRTiKYDSKWIKEPHFLHAIEY-------GNYVYFFFRE-IAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWT 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 287 TFLKARLVCSVPGPggAETHFDQLEDVFLLWPKAGKNlEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQH 366
Cdd:cd11269  228 SFLKARLNCSVPGD--SFFYFDVLQSITDIIEINGIP-TVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDS 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 367 QWGPY-GGKVPFPRPGVCPSKMTAQPgrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRV 445
Cdd:cd11269  305 VWTAVpEDKVPKPRPGCCAKHGLAEA---YKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTAIAVDHA 381
                        410       420
                 ....*....|....*....|....
gi 281182586 446 EAEDGTYDVIFLGTDSGSVLKIIA 469
Cdd:cd11269  382 AGPHQNYTVIFVGSEAGVVLKILA 405
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
57-520 1.24e-70

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: 238.86  E-value: 1.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  57 LDLQVMYLDEYRDRLFLGGRDALYSLRL----DQAWPDPREVLwPPQPGQKVECVRKGKDPLTECANFVRVLQPHN-RTH 131
Cdd:cd11238    1 LYYRTLLLDEKRNALYVGAMDRVFRLNLyninDTGNNCARDEL-TLSPSDVSECVSKGKDEEYECRNHVRVIQPMGdGQT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 132 LLACGTGAFQPICTFITVG--HRGEHVlhldpSSIENGRGRCPHEPSRPFASTFVGG-------ELYTGLTADFLGREAM 202
Cdd:cd11238   80 LYVCSTNAMNPKDRVLDANllHLPEYV-----PGPGNGIGKCPYDPDDNSTAVWVEWgnpgdlpALYSGTRTEFTKANTV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 203 IFRS-------GGPRPALRS-DSDQSLLHDPRFVMAARIpdnsdrdDDKVYFFFSETVPSPDGGpGHVTVSRVGRVCVND 274
Cdd:cd11238  155 IYRPplynntkGRHESFMRTlKYDSKWLDEPNFVGSFDI-------GDYVYFFFRETAVEYINC-GKVVYSRVARVCKKD 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 275 AGGQRVLVNKWSTFLKARLVCSVPG--PggaeTHFDQLEDVFLLwPKAGKNLeVYALFSTVSAVFRGFAVCVYHMVDIWE 352
Cdd:cd11238  227 TGGKNVLRQNWTTFLKARLNCSISGefP----FYFNEIQSVYKV-PGRDDTL-FYATFTTSENGFTGSAVCVFTLSDINA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 353 VFN-GPFAHRDGPQHQWGPY-GGKVPFPRPGVCpskmtaqpgrpFGSTKDYPDEVLQFVRGHPLMFQPVrpRRGRPVLVK 430
Cdd:cd11238  301 AFDtGKFKEQASSSSAWLPVlSSEVPEPRPGTC-----------VNDSATLSDTVLHFARTHPLMDDAV--SHGPPLLYL 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 431 THLAqqLCQIVVDRVEAEDGTYDVIFLGTDSGSVLKIIALQGSGlpepeEVVLEELQVFKV--PTPITEMEISvKRQTLY 508
Cdd:cd11238  368 RDVV--FTHLVVDKLRIDDQEYVVFYAGSNDGKVYKIVHWKDAG-----ESKSNLLDVFELtpGEPIRAMELL-PGEFLY 439
                        490
                 ....*....|..
gi 281182586 509 VGSPLGVARLQL 520
Cdd:cd11238  440 VASDHRVSQIDL 451
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
54-473 3.77e-70

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: 238.01  E-value: 3.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  54 RGSLDLQVMYLDEyrDRLFLGGRDALYSLRLDQAWPD----PREVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPHNR 129
Cdd:cd11266    6 RHRLDIQMIMIMN--RTLYIAARDHIYTVDIDTSHTEeiyfSKKLTWKSRQADVDTCRMKGKHK-DECHNFIKVLLKRND 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 130 THLLACGTGAFQPICTFI---TVGHRGEHVlhldpssieNGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRS 206
Cdd:cd11266   83 DTLFVCGTNAFNPSCRNYkmdTLEFFGDEF---------SGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 207 GGPRPALRS-DSDQSLLHDPRFVMAARIpdnsdrdDDKVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGG-QRVLVNK 284
Cdd:cd11266  154 LGDSPTLRTvKHDSKWLKEPYFVQAVDY-------GDYIYFFFRE-IAVEYNSMGKVVFPRVAQVCKNDMGGsQRVLEKQ 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 285 WSTFLKARLVCSVPGpgGAETHFDQLEDVFLLWPKAGKNLeVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGP 364
Cdd:cd11266  226 WTSFLKARLNCSVPG--DSHFYFNILQAVTDVIHINGRDV-VLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQKSP 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 365 QHQWGPY-GGKVPFPRPGVCPSKMTAQPgrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVD 443
Cdd:cd11266  303 DSTWTPVpDERVPKPRPGCCAGSSSLEK---YATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVD 379
                        410       420       430
                 ....*....|....*....|....*....|
gi 281182586 444 RVEAEDGTYDVIFLGTDSGSVLKIIALQGS 473
Cdd:cd11266  380 NAAGPYQNHTVVFLGSEKGIILKFLARTGN 409
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
57-469 1.56e-65

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: 225.37  E-value: 1.56e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  57 LDLQVMYldEYRDRLFLGGRDALYSLRLDQA----WPDpREVLWPPQPGQKveCVRKGKdPLTECANFVRVLQPHNRTHL 132
Cdd:cd11270    9 LDFQRML--RINHMVYIAARDHVFAINLSASleriVPQ-QKLTWKTKDVEK--CTVRGK-NSDECYNYIKVLVPRNDETL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 133 LACGTGAFQPICtfitvghRGEHVLHLDPSSIE-NGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPR- 210
Cdd:cd11270   83 FACGTNAFNPTC-------RNYKMSSLEQDGEEvIGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLGESs 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 211 PALRS-DSDQSLLHDPRFVMAARIpdnsdrdDDKVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGGQ-RVLVNKWSTF 288
Cdd:cd11270  156 PVLRTvKYDSKWLREPHFLHAIEY-------GNYVYFFLSE-IAVEYTTLGKVVFSRVARVCKNDNGGSpRVLERYWTSF 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 289 LKARLVCSVPGpgGAETHFDQLEDVFLLWPKAGKNlEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQW 368
Cdd:cd11270  228 LKARLNCSVPG--DSFFYFDVLQSLTNVMQINHRP-AVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAW 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 369 GPY-GGKVPFPRPGVCPSKMTAQPgrpFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEA 447
Cdd:cd11270  305 TPVpDEAVPKPRPGSCAGDGPAAG---YKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFKLTQIAVDTAAG 381
                        410       420
                 ....*....|....*....|..
gi 281182586 448 EDGTYDVIFLGTDSGSVLKIIA 469
Cdd:cd11270  382 PYKNYTVVFLGSENGHVLKVLA 403
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
64-520 2.43e-65

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: 223.97  E-value: 2.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  64 LDEYRDRLFLGGRDALYSLRLdQAWPDPREVLWPPQPGQKVECVRKGKDpLTECANFVRVLQPHNRThLLACGTGAFQPI 143
Cdd:cd11241   14 LDPTHDQLIVGARNYLFRLRL-QSLSLLQAVPWNSDEDTKRQCQSKGKS-VEECQNYVRVLLVVGKN-LFTCGTYAFSPV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 144 CTFITVGHrgehvLHLDPSSIeNGRGRCPHEPSRP-FASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRSD-SDQSL 221
Cdd:cd11241   91 CTIRKLSN-----LTQILDTI-SGVARCPYSPAHNsTALISASGELYAGTVYDFSGRDPAIYRSLGGKPPLRTAqYNSKW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 222 LHDPRFVMAARIpdnsdrdDDKVYFFFSET-VPSPDGGpgHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKARLVCSVPGP 300
Cdd:cd11241  165 LNEPNFVGSYEI-------GNHTYFFFRENaVEHQDCG--KTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNCSLPGE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 301 ggAETHFDQLEDVFLLwPKAGKnleVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYggkvPFPRP 380
Cdd:cd11241  236 --FPFYYNEIQGTFYL-PETDL---IYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPT----PNPHP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 381 GVCPSKMTAQpGRPFGSTKdypdEVLQFVRGHPLMFQPVRPRRGRPVLVKThlAQQLCQIVVDRVEAEDGT-YDVIFLGT 459
Cdd:cd11241  306 NFQCTTSIDR-GQPANTTE----RDLQDAQKYQLMAEVVQPVTKIPLVTMD--DVRFSKLAVDVVQGRGTQlVHIFYVGT 378
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182586 460 DSGSVLKIIALQGSGLPEPEEVVLEELQVFKvpTPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd11241  379 DYGTILKMYQPHRSQKSCTLEEIKILPAMKG--EPITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
310-501 1.09e-61

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: 205.20  E-value: 1.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  310 LEDVFLLWPKAG--KNLEVYALFST-VSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGGKVPFPRPGVCPSK 386
Cdd:pfam01403   1 LQDVFVLKPGAGdaLDTVLYGVFTTqWSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  387 MtaqpgrpfgSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLaqQLCQIVVDRVEAEDGTYDVIFLGTDSGSVLK 466
Cdd:pfam01403  81 P---------LRLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVRTGV--RLTSIAVDRVQALDGNYTVLFLGTDDGRLHK 149
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 281182586  467 IIALQGSGlpepeEVVLEELQVFKVPTPITEMEIS 501
Cdd:pfam01403 150 VVLVGSEE-----SHIIEEIQVFPEPQPVLNLLLS 179
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
71-472 5.96e-59

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: 207.63  E-value: 5.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  71 LFLGGRDALYSLRLDQAwpDPREVLWPPQ----PGQKVE-CVRKGKdpLT-ECANFVRVLQPHNRTHLLACGTGAFQPIC 144
Cdd:cd11268   21 LLVAARDHVFSFDLQAE--EEGEGLVPNKyltwRSQDVEnCAVRGK--LTdECYNYIRVLVPWDSQTLLACGTNSFSPVC 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 145 T---FITVGHRGEHVlhldpssieNGRGRCPHEPSRPFASTFVGGELYTGLTADFLGREAMIFRSGGPRPALRSDS-DQS 220
Cdd:cd11268   97 RsygITSLQQEGEEL---------SGQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKyDSK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 221 LLHDPRFVMAAripdnsdRDDDKVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGGQ-RVLVNKWSTFLKARLVCSVpg 299
Cdd:cd11268  168 WLREPHFVQAL-------EHGDHVYFFFRE-VSVEDARLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSV-- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 300 PGGAETHFDQLEDVFLLWPKAGKNlEVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYG-GKVPFP 378
Cdd:cd11268  238 PGDSTFYFDVLQALTGPVNLHGRS-ALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVSeDRVPSP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 379 RPGVCPSKMTAQpgrPFGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLAqQLCQIVVDRVEAEDGTYDVIFLG 458
Cdd:cd11268  317 RPGSCAGVGGAA---LFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLTLTSRA-LLTQVAVDGMAGPHSNITVMFLG 392
                        410
                 ....*....|....
gi 281182586 459 TDSGSVLKIIALQG 472
Cdd:cd11268  393 SNDGTVLKVLPPGG 406
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
55-520 7.88e-59

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: 206.37  E-value: 7.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  55 GSLDLQVMYLDEYRDRLFLGGRDALYSLRLD-----QAwpdpreVLWPPQPGQKVECVRKGKDPLtECANFVRVLQPhNR 129
Cdd:cd11264    5 GVRDFSQLALDLNRNQLIVGARNYLFRLSLHnvsliQA------TEWGSDEDTRRSCQSKGKTEE-ECQNYVRVLIV-YG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 130 THLLACGTGAFQPICTFITVGHRGEHVLHLdpssieNGRGRCPHEPSRpfASTFV---GGELYTGLTADFLGREAMIFRS 206
Cdd:cd11264   77 KKVFTCGTNAFSPVCTSRQVGNLSKVIERI------NGVARCPYDPRH--NSTAVitsRGELYAATVIDFSGRDPAIYRS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 207 GGPRPALRSDSDQS-LLHDPRFVMAARIPDNSdrdddkvYFFFSETVPSPDGGpgHVTVSRVGRVCVNDAGGQRVLVNKW 285
Cdd:cd11264  149 LGSVPPLRTAQYNSkWLNEPNFIAAYDIGLFT-------YFFFRENAVEHDCG--KTVYSRVARVCKNDIGGRFLLEDTW 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 286 STFLKARLVCSVPGPggAETHFDQLEDVFLLwPKagKNLeVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQ 365
Cdd:cd11264  220 TTFMKARLNCSRPGE--IPFYYNELQSTFYL-PE--QDL-IYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPR 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 366 HQWGPYGGKVPFPRPGVCPSKmtaqpgrpfGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHLaqQLCQIVVDRV 445
Cdd:cd11264  294 SAWLPTANPIPNFQCGTLSDD---------SPNENLTERSLQDAQRLFLMNDVVQPVTVDPLVTQDSV--RFSKLVVDIV 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 446 EAEDGTYDVIFLGTDSGSVLKIIA-----LQGSGLPEPEEVVLEELQvfkvptPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd11264  363 QGKDTLYHVMYIGTEYGTILKALSttnrsLRSCYLEEMQILPPGQRE------PIRSLQILHSDRSLFVGLNNGVLKIPL 436
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
61-520 4.21e-58

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: 203.54  E-value: 4.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  61 VMYLDEYRDRLFLGGRDALYSLrldqAWPDPRE-VLWPPQPGQKVECVRKGkdPLTECANFVRVLQPHNRThLLACGTGA 139
Cdd:cd11243    6 VFFHEAGSSSVYVGGQGALYLL----DFTGSAViVKKIPDEKTEKDCKKRA--TLDDCENYITLIKKLDYR-LLVCGTNA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 140 FQPICTFITVGHRgehvlhldpSSIENGRGRCPHEPSRPFASTFVGGELYTGLTadflGRE--AMIFRSGGPRPALRSdS 217
Cdd:cd11243   79 GSPKCWFLVNQTL---------VTLSADRGVAPFLPDENSLVLIEGNNVYSTIS----GKKgnIPRFRRYGGKKELYT-S 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 218 DqSLLHDPRFVMAARIPDNSDRDDdKVYFFFSETvpSPDGGP-GHVTVSRVGRVCVNDAGGQRVL-VNKWSTFLKARLVC 295
Cdd:cd11243  145 D-TVMQKPQFVKATLLPEDEQYQD-KIYYFFRED--NEDKGPeAEPNISRVARLCKEDQGGTSSLsTSKWSTFLKARLVC 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 296 SVPGPGGaetHFDQLEDVFLLWPKAGKNLEVYALFSTvsaVFRGFAVCVYHMVDIWEVFNgpfahrdgPQHQWGpYGGKV 375
Cdd:cd11243  221 GDPATPM---NFNRLQDVFLLPKEEWREAVVYGVFSN---TWGSSAVCSYSLGDIDKVFR--------TSSLKG-YSGSL 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 376 PFPRPGVCpskmtAQPGRPfgstkdYPDEVLQFVRGHPLMFQPVRPRRGR--PVLVKTHLAQqlcQIVVDRVEAEDG-TY 452
Cdd:cd11243  286 PNPRPGTC-----VPPEQT------HPSETFSFADEHPELDDRIEPDEPRklPVFQNKDHYQ---KVVVDEVRASDGvSY 351
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281182586 453 DVIFLGTDSGSVLKIIALQGsglpepEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd11243  352 DVLYLATDKGKIHKVVESKG------QTHNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
55-520 2.28e-57

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: 202.18  E-value: 2.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  55 GSLDLQVMYLDEYRDRLFLGGRDALYSLRLDQAwPDPREVLWPPQPGQKVECVRKGKDPlTECANFVRVLQPhNRTHLLA 134
Cdd:cd11263    5 NAVDFSQLTFDPGQKELIVGARNYLFRLQLEDL-SLIQAVEWECDEATKKACYSKGKSK-EECQNYIRVLLV-GGDRLFT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 135 CGTGAFQPICTFITVGHRGEhvLHLDPSsienGRGRCPHEPSRPFASTFVG-GELYTGLTADFLGREAMIFRSGGPRPAL 213
Cdd:cd11263   82 CGTNAFTPICTNRTLNNLTE--IHDQIS----GMARCPYSPQHNSTALLTSsGELYAATAMDFPGRDPAIYRSLGILPPL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 214 RSDSDQS-LLHDPRFVMAARIpdnsdrdDDKVYFFFSETVPSPDGGpgHVTVSRVGRVCVNDAGGQRVLVNKWSTFLKAR 292
Cdd:cd11263  156 RTAQYNSkWLNEPNFVSSYDI-------GNFTYFFFRENAVEHDCG--KTVFSRAARVCKNDIGGRFLLEDTWTTFMKAR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 293 LVCSVPGPggAETHFDQLEDVFLLwpkagKNLE-VYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPY 371
Cdd:cd11263  227 LNCSRPGE--IPFYYNELQSTFFL-----PELDlIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPY 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 372 ggkvPFPRPGVCPSKMTAqpgrpfGSTKDYPDEVLQFVRGHPLMFQPVRPRRGRPVLVKTHlaQQLCQIVVDRVEAEDGT 451
Cdd:cd11263  300 ----PNPNPNFQCGTMDQ------GLYVNLTERNLQDAQKFILMHEVVQPVTPVPYFMEDN--SRFSHVAVDVVQGKDML 367
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281182586 452 YDVIFLGTDSGSVLKIIAL--QGSGlpepeEVVLEELQVF--KVPTPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd11263  368 FHIIYLATDYGTIKKVLAPlnQSSS-----SCLLEEIELFpkRQREPIRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
62-518 1.10e-50

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: 183.44  E-value: 1.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  62 MYLDEYRDRLFLGGRDALYSLRLDQAwPDPREVLWPPQPGQKVECVRKGKDpLTECANFVRVLQPHNRtHLLACGTGAFQ 141
Cdd:cd11265   12 MLFDVARNQVIVGARDNLYRLSLDGL-ELLERASWPAAESKVALCQNKGQS-EEDCHNYVKVLLSYGK-QLFACGTNAFS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 142 PICTFitvghrgEHVLHLDP-SSIENGRGRCPHEPSRPFASTFV-GGELYTGLTADFLGREAMIFRSGGP--RPALRSDS 217
Cdd:cd11265   89 PRCSW-------REMENLTSvTEWDSGVAKCPYSPHANITALLSsSGQLFVGSPTDFSGSDSAIYRTLGTsnKSFLRTKQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 218 -DQSLLHDPRFVmaaripdNSDRDDDKVYFFFSETVpSPDGGPGHVTVSRVGRVCVNDAGGQRVLV-NKWSTFLKARLVC 295
Cdd:cd11265  162 yNSKWLNEPQFV-------GSFETGNFVYFLFRESA-VEYMNCGKVIYSRIARVCKNDVGGGTMLLkDNWTTFLKARLNC 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 296 SVPG--PggaeTHFDQLEDVFLLwPKAGKnleVYALFSTVSAVFRGFAVCVYHMVDIWEVFNGPFAHRDGPQHQWGPYGg 373
Cdd:cd11265  234 SLPGeyP----FYFDEIQGMTYL-PDEGI---LYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVN- 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 374 kvpfprpgvcpskmTAQPGRPFGSTKDYPDEVLQFVRgHPLMFQPVRPRRGRPVLVKThlAQQLCQIVVDRVEAE-DGTY 452
Cdd:cd11265  305 --------------VNHRDHFNQCSSSSSSHLLESSR-YQLMDEAVQPITLEPLHHAK--LERFSHIAVDVIPTKiHQSV 367
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281182586 453 DVIFLGTDSGSVLKIIALQGSglpePEEVVLEELQVFKVP-TPITEMEISVKRQTLYVGSPLGVARL 518
Cdd:cd11265  368 HVLYVATTGGLIKKISVLPRT----QETCLVEIWQPLPTPdSPIKTMQYLKVTDSLYVGTELALMRI 430
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
58-520 1.44e-50

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: 182.02  E-value: 1.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  58 DLQVMYLDEYRDRLFLGGRDALYSLRLDQAWPDPR----EVLWPPQPGQKVECvRKGKDPLTECANFVRVLQPHNR-THL 132
Cdd:cd09295    1 DDDKILVSFRKDTIYVGAIARIYKVDGGGTRLLLScispELNFGFNEDQKAFC-PLRRGKWTECINYIKVLQQKGDlDIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 133 LACGTGAFQPICtfitvGH-RGEHVLHLDPSSIENGRGRCPHEPSRPFASTFVGGELYTGLTADFL-GREAMIFRSGGPR 210
Cdd:cd09295   80 AVCGSNAAQPSC-----GSyRLDVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 211 PALRSDSDQS-LLHDPRFVMAaripDNSDRDDDKVYFFFSEtVPSPDGGPGHVTVSRVGRVCVNDAGGQRVLVNKWSTFL 289
Cdd:cd09295  155 HYLRIVVDSStGLDEITFVYA----FVSGDDDDEVYFFFRQ-EPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTSFL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 290 KARLVCSVPGPGGAethFDQLEDVFLLWPKAGKNLeVYALFSTVSAVFRGFAVCVYHMVDIWEVFngpfahrdgpqhqwg 369
Cdd:cd09295  230 KADLNCSRPQSGFA---FNLLQDATGDTKNLIQDV-KFAIFSSCLNKSVESAVCAYLFTDINNVF--------------- 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 370 pyggkvpfprpgvcpskmtaqpgrpfgstkdypdevlqfvrghplmFQPVRPRRGRPVLVKTHLAQQLCQIVVDRVEAED 449
Cdd:cd09295  291 ----------------------------------------------DDPVEAINNRPLYAHQNQRSRLTSIAVDATKQKS 324
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281182586 450 GTYDVIFLGTDSGSVLKIIALQGSglpePEEVVLEELQVFKVPTPITEMEISVKRQTLYVGSPLGVARLQL 520
Cdd:cd09295  325 VGYQVVFLGLKLGSLGKALAFFFL----YKGHIIEEWKVFKDSSRITNLDLSRPPLYLYVGSESGVLGVPV 391
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
591-676 2.75e-41

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: 145.57  E-value: 2.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 591 VFGTEHNSTFLECRPKSPQAAVRWFLQRPGDKGADQVKTDERVVQTDQGLLFRRLSRLDAGNYTCTTLEHGFSQTVVRFA 670
Cdd:cd05871    7 VYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQTLVKIR 86

                 ....*.
gi 281182586 671 LEVIAA 676
Cdd:cd05871   87 LHVIEP 92
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
452-564 3.61e-10

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: 63.03  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 452 YDVIFLGTDSGSVLKIIA---LQGSglpepeeVVLEELQVFKVPTPI-TEMEISVKRQTLYVGSPLGVARLQLHQCETYg 527
Cdd:cd11272  406 YSVVFVGTKSGKLKKIRAdgpPHGG-------VQYEMVSVFKDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQY- 477
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 281182586 528 SACAECCLARDPYCAWdgtsCARYRPSSGKRRFRRQD 564
Cdd:cd11272  478 TTCGECLSSGDPHCGW----CALHNMCSRRDKCQRAW 510
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
598-674 2.48e-09

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: 54.77  E-value: 2.48e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281182586 598 STFLECRPKSPQAAVRWFLQRPGDKGADQVKTderVVQTDQGLLFRRLSRLDAGNYTCTTLEHGFSQTVVRFALEVI 674
Cdd:cd04979   13 TVILSCSVKSNNAPVTWIHNGKKVPRYRSPRL---VLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSVTLHVL 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
591-668 9.43e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 47.19  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586  591 VFGTEHNSTFLEC--RPKSPQAAVRWFLQRPGDKGADQVKTDERVvQTDQGLLFRRLSRLDAGNYTCTTLEHGFSQTVVR 668
Cdd:pfam00047   6 VTVLEGDSATLTCsaSTGSPGPDVTWSKEGGTLIESLKVKHDNGR-TTQSSLLISNVTKEDAGTYTCVVNNPGGSATLST 84
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
601-656 1.74e-05

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: 43.99  E-value: 1.74e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 281182586 601 LECRPK-SPQAAVRWflqrpgDKGADQVKTDERVVQTDQGLLF-RRLSRLDAGNYTCT 656
Cdd:cd04969   22 IECKPKaSPKPTISW------SKGTELLTNSSRICILPDGSLKiKNVTKSDEGKYTCF 73
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
597-673 3.90e-05

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


Pssm-ID: 409457  Cd Length: 87  Bit Score: 42.88  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182586 597 NSTFLECRPKSPQAAVRWflqrpgdKGADQVKTDE--RVVQTDQGLLFRRLSRLDAGNYTCTTLEHG----FSQTVVRFA 670
Cdd:cd05873   12 GNAELKCSPKSNLARVVW-------KFQGKVLKAEspKYGLYGDGLLIFNASEADAGRYQCLSVEKSkaktFFQTVAKYV 84

                 ...
gi 281182586 671 LEV 673
Cdd:cd05873   85 LEV 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
601-656 1.11e-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: 41.16  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 281182586 601 LECRPK-SPQAAVRWFlqRPGDKGADQVKTDERVVQTDQGLLFRRLSRLDAGNYTCT 656
Cdd:cd00096    3 LTCSASgNPPPTITWY--KNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCV 57
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
522-568 1.75e-04

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 39.84  E-value: 1.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 281182586   522 QCETYGSaCAECCLARDPYCAWD--GTSCARYRPSSgkrrFRRQDIRHG 568
Cdd:smart00423   1 RCSKYTS-CSECLLARDPYCAWCssQGRCTSGERCD----SRRQNWLSG 44
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
601-675 3.11e-04

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


Pssm-ID: 409456  Cd Length: 86  Bit Score: 40.12  E-value: 3.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281182586 601 LECRPKSPQAAVRWFLQrpgdkGADQVKTDERVVQTDQGLLFRRLSRLDAGNYTCTTLEHGFSQTVVRFALEVIA 675
Cdd:cd05872   16 LPCQLRSNLASPVWLFN-----GTPLNAQFSYLRLGTDGLLILVTSPEHSGTYRCYSEEEGFQQLVASYSLNVVE 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
589-656 1.99e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182586  589 TRVFGTEHNSTFLECRPK-SPQAAVRWFlqRPGDKGADQVKTDERVVQTDQGLLFRRLSRLDAGNYTCT 656
Cdd:pfam13927   9 SSVTVREGETVTLTCEATgSPPPTITWY--KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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