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Conserved domains on  [gi|21361914|ref|NP_071762|]
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semaphorin-4A isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
55-495 0e+00

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: 854.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  55 FFHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSY 134
Cdd:cd11256   1 RFRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTPGPIRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 135 NVTHLYTCGTFAFSPACTFIELQDSYLLP-ISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLG 213
Cdd:cd11256  81 NGTHLYTCGTYAFSPACTYIELDHFSLPPpNGTIITMDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 214 SQPVLKTDNFLRWLHHDASFVAAIPST--QVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQL 291
Cdd:cd11256 161 TKVSLKTDGFLRWLNADAVFVASFNPQgdSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 292 LCTQPGQLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRGPE 371
Cdd:cd11256 241 TCSQQGHFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 372 TNPRPGSCSVGPSSDKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVETAQGLDGHSHLVMYLGTTTGSLHKAVV 448
Cdd:cd11256 321 SDPRPGSCSGGKSSDKALNFMKDHFLMDEVVLpgaGRPLLVKSNVQYTRIAVDSVQGVSGHNYTVMFLGTDKGFLHKAVL 400
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 21361914 449 SGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRA 495
Cdd:cd11256 401 MGGSESHIIEEIELLTPPEPVENLLLAANEGVVYIGYSAGVWRVPLA 447
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
496-540 3.39e-10

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


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 56.18  E-value: 3.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 21361914   496 NCSVYESCVDCVLARDPHCAWDPESRTC-----CLLSAPNLNSWKQDMER 540
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCvrrsaCGAPEGNCEEWEQASSK 50
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
566-638 4.71e-08

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.


The actual alignment was detected with superfamily member cd05872:

Pssm-ID: 472250  Cd Length: 86  Bit Score: 50.90  E-value: 4.71e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361914 566 KEVLAVPNSILELPCPHLSALASYYWSH-GPAAVPEASSTVY--NGSLLLIVQDGVGGLYQCWATENGFSYPVISY 638
Cdd:cd05872   4 KFRTVVAGADVVLPCQLRSNLASPVWLFnGTPLNAQFSYLRLgtDGLLILVTSPEHSGTYRCYSEEEGFQQLVASY 79
 
Name Accession Description Interval E-value
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
55-495 0e+00

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: 854.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  55 FFHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSY 134
Cdd:cd11256   1 RFRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTPGPIRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 135 NVTHLYTCGTFAFSPACTFIELQDSYLLP-ISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLG 213
Cdd:cd11256  81 NGTHLYTCGTYAFSPACTYIELDHFSLPPpNGTIITMDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 214 SQPVLKTDNFLRWLHHDASFVAAIPST--QVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQL 291
Cdd:cd11256 161 TKVSLKTDGFLRWLNADAVFVASFNPQgdSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 292 LCTQPGQLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRGPE 371
Cdd:cd11256 241 TCSQQGHFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 372 TNPRPGSCSVGPSSDKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVETAQGLDGHSHLVMYLGTTTGSLHKAVV 448
Cdd:cd11256 321 SDPRPGSCSGGKSSDKALNFMKDHFLMDEVVLpgaGRPLLVKSNVQYTRIAVDSVQGVSGHNYTVMFLGTDKGFLHKAVL 400
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 21361914 449 SGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRA 495
Cdd:cd11256 401 MGGSESHIIEEIELLTPPEPVENLLLAANEGVVYIGYSAGVWRVPLA 447
Sema smart00630
semaphorin domain;
64-470 8.79e-128

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 385.95  E-value: 8.79e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914     64 FDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKnmIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTCG 143
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELK--TGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    144 TFAFSPACTFIELqdsyllpisedkvmegkgqspfdpahkhtavlvdGMLYSGTMNNFLGSEPILMRTLGSQPVLKTDNF 223
Cdd:smart00630  79 TNAFQPVCRLRNL----------------------------------GELYVGTVADFSGSDPAIPRSLSVRRLKGTSGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    224 --------LRWLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLCTQ 295
Cdd:smart00630 125 slrtvlydSKWLN-EPNFVYAFESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    296 PGQLP--FNVIRHAVLLPADSPTAPHIYAVFTSQWqvGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTY-RGPET 372
Cdd:smart00630 204 PGEDPfyFNELQAAFLLPPGSESDDVLYGVFSTSS--NPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYsRGKVP 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    373 NPRPGSCSVGPSS-----DKALTFMKDHFLMDEQVV---GTPLLVKSGVEY--TRLAVETAQGLDGHShlVMYLGTTTGS 442
Cdd:smart00630 282 YPRPGTCPNKPPSskdlpDETLNFIKSHPLMDEVVQpltGRPLFVKTDSNYllTSIAVDRVATDGNYT--VLFLGTSDGR 359
                          410       420       430
                   ....*....|....*....|....*....|.
gi 21361914    443 LHKAVVSGDSSAH---LVEEIQLFPDPEPVR 470
Cdd:smart00630 360 ILKVVLSESSSSSesvVLEEISVFPDGSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
304-474 3.37e-66

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: 217.14  E-value: 3.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914   304 IRHAVLLPADSPTA--PHIYAVFTSQWqVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRGPETNPRPGSCSV 381
Cdd:pfam01403   1 LQDVFVLKPGAGDAldTVLYGVFTTQW-SNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914   382 GPS----SDKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVETAQGLDGHsHLVMYLGTTTGSLHKAVVSGDSSA 454
Cdd:pfam01403  80 DPLrldlPDSVLNFVKDHPLMDEAVQpvgGRPLLVRTGVRLTSIAVDRVQALDGN-YTVLFLGTDDGRLHKVVLVGSEES 158
                         170       180
                  ....*....|....*....|
gi 21361914   455 HLVEEIQLFPDPEPVRNLQL 474
Cdd:pfam01403 159 HIIEEIQVFPEPQPVLNLLL 178
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
496-540 3.39e-10

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 56.18  E-value: 3.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 21361914   496 NCSVYESCVDCVLARDPHCAWDPESRTC-----CLLSAPNLNSWKQDMER 540
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCvrrsaCGAPEGNCEEWEQASSK 50
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
496-541 7.33e-09

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 52.16  E-value: 7.33e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 21361914    496 NCSVYESCVDCVLARDPHCAWDPESRTCclLSAPNLNSWKQDMERG 541
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRC--TSGERCDSRRQNWLSG 44
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
566-638 4.71e-08

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: 50.90  E-value: 4.71e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361914 566 KEVLAVPNSILELPCPHLSALASYYWSH-GPAAVPEASSTVY--NGSLLLIVQDGVGGLYQCWATENGFSYPVISY 638
Cdd:cd05872   4 KFRTVVAGADVVLPCQLRSNLASPVWLFnGTPLNAQFSYLRLgtDGLLILVTSPEHSGTYRCYSEEEGFQQLVASY 79
 
Name Accession Description Interval E-value
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
55-495 0e+00

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: 854.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  55 FFHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSY 134
Cdd:cd11256   1 RFRQENVHNYDQLLLSPDETTLYVGARDNILALGIRTPGPIRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 135 NVTHLYTCGTFAFSPACTFIELQDSYLLP-ISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLG 213
Cdd:cd11256  81 NGTHLYTCGTYAFSPACTYIELDHFSLPPpNGTIITMDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 214 SQPVLKTDNFLRWLHHDASFVAAIPST--QVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQL 291
Cdd:cd11256 161 TKVSLKTDGFLRWLNADAVFVASFNPQgdSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKWTTFLKAQL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 292 LCTQPGQLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRGPE 371
Cdd:cd11256 241 TCSQQGHFPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLGGRRSSAVCAYKLNDIEKVFNGKYKELNKESSRWTRYMGPV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 372 TNPRPGSCSVGPSSDKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVETAQGLDGHSHLVMYLGTTTGSLHKAVV 448
Cdd:cd11256 321 SDPRPGSCSGGKSSDKALNFMKDHFLMDEVVLpgaGRPLLVKSNVQYTRIAVDSVQGVSGHNYTVMFLGTDKGFLHKAVL 400
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 21361914 449 SGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRA 495
Cdd:cd11256 401 MGGSESHIIEEIELLTPPEPVENLLLAANEGVVYIGYSAGVWRVPLA 447
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
56-495 0e+00

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: 737.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGvPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYN 135
Cdd:cd11240   1 FSQEGIQNYSTLLLSEDEGTLYVGAREALFALNVSDIS-TELKDKIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 VTHLYTCGTFAFSPACTFIELQDSYLlpiSEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQ 215
Cdd:cd11240  80 STHLYVCGTFAFSPRCTYINLSDFSL---SSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHSEG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 216 PVLKTDNFLRWLHHDASFVAAIPST---------QVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTF 286
Cdd:cd11240 157 NVLKTENTLRWLNEPAFVGSAHIREsidspdgddDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGGQRTLQKKWTTF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 287 LKAQLLCTQPG-QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKETSRWT 365
Cdd:cd11240 237 LKAQLVCSQPDsGLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNV--SGLSAVCAYSLEDIKKVFSGKYKEFNRETSKWS 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 366 TYRGPETNPRPGSCSVG-----------PSSDKALTFMKDHFLMDEQV--VGTPLLVKSGVEYTRLAVETAQGLDGHSHL 432
Cdd:cd11240 315 RYTGPVPDPRPGACITNsarsqgitsslNLPDNVLTFVKDHPLMDEQVhpINRPLLVKSGVNYTRIAVHRVQALDGQTYT 394
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361914 433 VMYLGTTTGSLHKAvVSGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRA 495
Cdd:cd11240 395 VLFLGTEDGFLHKA-VSLDGGMHIIEEIQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPLS 456
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
56-495 2.41e-156

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: 462.41  E-value: 2.41e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYN 135
Cdd:cd11257   2 FEAEGVSNYTALLLSKDGNMLYVGARETLFALSSNDISPTGEQQELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRLN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 VTHLYTCGTFAFSPACTFIELQDSYLL------PISEDkvmeGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILM 209
Cdd:cd11257  82 STHLFTCGTYAFSPICTYIVMTNFSLErdekgePLLED----GKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 210 RTLGSQPVLKTDNFLRWLhHDASFVA------AIPSTQ----VVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLL 279
Cdd:cd11257 158 RSLGSGTPLKTENSLNWL-QDPAFVGsayiqeSLPKLVgdddKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGGERVL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 280 QKKWTTFLKAQLLCTQPGQ-LPFNVIRHAVLLPadsPTAPH-----IYAVFTSQWQVGGTRSSAVCAFSLLDIERVFKGK 353
Cdd:cd11257 237 QKRWTTFLKAQLLCSLPDDgFPFNVLQDVFVLT---PSPEDwkdtlFYGVFTSQWHKGTAGSSAVCVFTMDQVQRAFNGL 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 354 YKELNKETSRWTTYRGPETNPRPGSCSVGPSS-----------DKALTFMKDHFLMDEQVVGTPLLVKSGVEYTRLAVET 422
Cdd:cd11257 314 YKEVNRETQQWYTYTHPVPEPRPGACITNSARerkinsslhmpDRVLNFVKDHFLMDGQVRSQPLLLQPQVRYTQIAVHR 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361914 423 AQGLDgHSHLVMYLGTTTGSLHKAvVSGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRA 495
Cdd:cd11257 394 VKGLH-KTYDVLFLGTDDGRLHKA-VSVGPMVHIIEELQIFSEGQPVQNLLLDTHKGLLYASSHSGVVQVPVA 464
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
56-495 7.26e-131

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: 396.92  E-value: 7.26e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDpgVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYN 135
Cdd:cd11259  12 FHEPDVSNYSTLLLSEDKDVLYVGAREAVFALNALN--ISEKQHELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 VTHLYTCGTFAFSPACTFIELQDSYLLPISEDkvmeGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQ 215
Cdd:cd11259  90 DTFLYVCGTNAFQPTCDYLNLTSFRLLGKNED----GKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRNSSQS 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 216 PvLKTDNFLRWLHhDASFVAA--IPSTQ--------VVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTT 285
Cdd:cd11259 166 P-LRTEYAIPWLN-EPSFVFAdvIRADPdspdgeddKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTS 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 286 FLKAQLLCTQPGQ-LPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVGGTrsSAVCAFSLLDIERVF-KGKYKE---LNKE 360
Cdd:cd11259 244 FLKARLICSIPDKnLVFNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGL--SAVCAYNLSTVEEVFsKGKYMQsatVEQS 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 361 TSRWTTYRGPETNPRPGSC------SVGPSS-----DKALTFMKDHFLMDEQV--VGT-PLLVKSGVEYTRLAVETAQGL 426
Cdd:cd11259 322 HTKWVRYNGEVPKPRPGACinnearAANYTSslnlpDKTLQFVKDHPLMDDSVtpIGNrPRLIKKDVNYTQIVVDRVQAL 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361914 427 DGHSHLVMYLGTTTGSLHKAvVSGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGA--VFVGFSGGVWRVPRA 495
Cdd:cd11259 402 DGTIYDVMFISTDRGALHKA-ISLENEVHIIEETQLFPDFEPVQTLLLSSKKGRrfLYAGSNSGVVQSPLA 471
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
66-493 1.28e-130

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: 395.24  E-value: 1.28e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  66 TLLLSGDGNTLYVGAREAILALDIQDPgvpRLKNMIPWPASDRKKSECAFKKKSnETQCFNFIRVLVSYNVTHLYTCGTF 145
Cdd:cd11235   5 TKLLHEDRSTLYVGARDRVYLVDLDSL---YTEQKVAWPSSPDDVDTCYLKGKS-KDDCRNFIKVLEKNSDDSLLVCGTN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 146 AFSPACTFIELQDSYLlpisEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKT-DNFL 224
Cdd:cd11235  81 AFNPSCRNYNVETFEL----VGKEESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLGHNPPLRTeYHDS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 225 RWLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLCTQPGQLP--FN 302
Cdd:cd11235 157 KWLN-EPQFVGAFDIGDYVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKARLNCSVPGEFPfyFN 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 303 VIRHAVLLPADSPTAPHIYAVFTSQW-QVGGtrsSAVCAFSLLDIERVFKGKYKELNKETSRWT---TYRGPEtnPRPGS 378
Cdd:cd11235 236 ELQDVFDLPSPSNKEKIFYAVFTTPYnSIPG---SAVCAYSLSDIEAVFNGPFKEQHSSNSAWLpvpDERVPE--PRPGT 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 379 C--SVGPSSDKALTFMKDHFLMDEQV---VGTPLLVKSGVEY--TRLAVETAQGLDGHSHLVMYLGTTTGSLHKAVVSGD 451
Cdd:cd11235 311 CvdDSSPLPDDTLNFIKSHPLMDEAVtpiLNRPLFIKTDVNYrfTKIAVDRVQAKLGQTYDVLFVGTDRGIILKVVSLPE 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 21361914 452 SS---AHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11235 391 QGlqaSNILEEMPVGPPPEPIQTMQLSRKRRSLYVGSETGVLQVP 435
Sema smart00630
semaphorin domain;
64-470 8.79e-128

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 385.95  E-value: 8.79e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914     64 FDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKnmIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTCG 143
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELK--TGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    144 TFAFSPACTFIELqdsyllpisedkvmegkgqspfdpahkhtavlvdGMLYSGTMNNFLGSEPILMRTLGSQPVLKTDNF 223
Cdd:smart00630  79 TNAFQPVCRLRNL----------------------------------GELYVGTVADFSGSDPAIPRSLSVRRLKGTSGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    224 --------LRWLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLCTQ 295
Cdd:smart00630 125 slrtvlydSKWLN-EPNFVYAFESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLKARLECSV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    296 PGQLP--FNVIRHAVLLPADSPTAPHIYAVFTSQWqvGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTY-RGPET 372
Cdd:smart00630 204 PGEDPfyFNELQAAFLLPPGSESDDVLYGVFSTSS--NPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLPYsRGKVP 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914    373 NPRPGSCSVGPSS-----DKALTFMKDHFLMDEQVV---GTPLLVKSGVEY--TRLAVETAQGLDGHShlVMYLGTTTGS 442
Cdd:smart00630 282 YPRPGTCPNKPPSskdlpDETLNFIKSHPLMDEVVQpltGRPLFVKTDSNYllTSIAVDRVATDGNYT--VLFLGTSDGR 359
                          410       420       430
                   ....*....|....*....|....*....|.
gi 21361914    443 LHKAVVSGDSSAH---LVEEIQLFPDPEPVR 470
Cdd:smart00630 360 ILKVVLSESSSSSesvVLEEISVFPDGSPIS 390
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
56-484 3.15e-127

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: 387.24  E-value: 3.15e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPgvpRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYN 135
Cdd:cd11258   4 FSQVGVSNYTTLTLAEHRGLLYVGAREAIFALSLSNI---ELQPPISWEAPAEKKTECAQKGKSNQTECFNYIRFLQPYN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 VTHLYTCGTFAFSPACTFIELQDSYLlpiSEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQ 215
Cdd:cd11258  81 QSHLYTCGTYAFQPKCAYINMLTFTL---DRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 216 PVLKTDNFLRWLhHDASFV--AAIPST--------QVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTT 285
Cdd:cd11258 158 YSMKTEYLAFWL-NEPHFVgsAFVPESvgsftgddDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTT 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 286 FLKAQLLCTQPG-QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWqvGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRW 364
Cdd:cd11258 237 FLKARLLCSIPEwQLYFNQLKAVFTLEGASWRNTTFFAVFQARW--GDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKW 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 365 TTYRGPETNPRPGSC-----------SVGPSSDKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVETAQGLDGHS 430
Cdd:cd11258 315 GRYTDPVPSPRPGSCinnwhrdhgytSSLELPDNTLNFVKKHPLMEDRVKprlGRPLLVPCNSNFTHVVWTRVLGLDGET 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 21361914 431 HLVMYLGTTTGSLHKAVVSGdSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVG 484
Cdd:cd11258 395 YSVLFIGTLDGWLIKAVSLG-SWVHMIEELQVFDQEPPESLVVSQSSKKLLFAG 447
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
62-493 1.30e-122

The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and Sema4C genes are expressed in the developing cerebellar cortex. Sema4G and Sema4C proteins specifically bind to Plexin B2 expressed in the cerebellar granule cells. Sema4G and Sema4C are involved in neural tube closure and cerebellar granule cell development through Plexin B2.Sema4G belongs to the class 4 transmembrane semaphorin family of proteins. Semaphorins are regulatory molecules involved in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200523 [Multi-domain]  Cd Length: 457  Bit Score: 375.25  E-value: 1.30e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  62 QDFDTLLLSGDGNTLYVGAREAILALDIQDPGvPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYT 141
Cdd:cd11262   8 QNYSTLLLEDESGRLYVGARGAIFSLNASDIS-DSSALTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRFNSTHLYT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 142 CGTFAFSPACTFIELQDSYLLPISEdkvmEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLgSEPILMRTLgSQPVLKTD 221
Cdd:cd11262  87 CGTHAFRPLCAYIDAERFTLSSQFE----EGKEKCPYDPAKGYTGLIVDGQLYTASQYEFR-SFPDIRRNS-PQPTLRTE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 222 NF-LRWLhHDASFVAA----------IPSTQVVYFFFEETASE-FDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKA 289
Cdd:cd11262 161 EApTRWL-NDADFVGSvlvresmnssVGDDDKIYFFFTERSQEeTAYFSQSRVARVARVCKGDRGGKKTLQRKWTSFLKA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 290 QLLCTQPG-QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQvgGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYR 368
Cdd:cd11262 240 RLVCYIPEyEFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWK--NVKASAICRYSLSDIQTAFEGPYMEYQDSSSKWSRYT 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 369 GPETNPRPGSC------SVGPSS-----DKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVETAQGLDGHSHLVM 434
Cdd:cd11262 318 GKVPEPRPGSCitdehrSQGINSsqdlpDNVLDFVRRHPLMAEQVLpveGRPLLFKRNVIYTKIAVQTVRGLDGRVYDVL 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361914 435 YLGTTTGSLHKAVVSGdSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11262 398 FLGTDEGWLHKAVVIG-SAVHIIEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVP 455
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
56-493 4.43e-118

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: 363.46  E-value: 4.43e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRlkNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYN 135
Cdd:cd11260   1 FKEQGIWNYSTMLLREDLGLLVLGAREAVFALDLNDISVKR--AKVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 VTHLYTCGTFAFSPACTFIELQDSYLlpISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTlgSQ 215
Cdd:cd11260  79 DSRMYVCGTNAFSPTCDYISYDDGQL--TLEGKQEDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRS--SP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 216 PVLKTDNFLRWLHhDASFV--AAIPSTQ--------VVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTT 285
Cdd:cd11260 155 ITIRTEFKSSWLN-EPNFIymAAVPESEdspegdddKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQKKWTS 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 286 FLKAQLLCTQP-GQLPFnVIRHAVLLPADSPTAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVF-KGKYK-ELNKETS 362
Cdd:cd11260 234 FLKARLDCSVPePSLPY-VIQDVFHVCHQDWRKCVFYAVFTS--QSDSSQSSAVCAYNVTDISNVFsRGKFKtPVAVETS 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 363 --RWTTYRGPETNPRPGSC------SVGPSS-----DKALTFMKDHFLMDEQV---VGTPLLVKSGVEYTRLAVETAQGL 426
Cdd:cd11260 311 fvKWVMYSGELPVPRPGACinnaarTSGIKKslnlpDKTLQFVKDKPLMDQAVhpiTGKPLLVKRGALFTRIVVDMVTAA 390
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361914 427 DGHSHLVMYLGTTTGSLHKAvVSGDSSAHLVEEIQLFPDPEPVRNLQLAPTQgaVFVGFSGGVWRVP 493
Cdd:cd11260 391 DGQSYPVMFIGTANGYVLKA-VNYDGEMHIIEEVQLFEPEEPIDILRLSQNQ--LYAGSASGVVQMP 454
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
51-493 1.70e-114

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: 354.19  E-value: 1.70e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  51 RALSFFHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIqdPGVPRLKNMIPWPASDRKKSECAfKKKSNETQCFNFIRV 130
Cdd:cd11261   1 SALTRFSAPHTYNYSVLLVDPASHTLYVGARDAIFALTL--PFSGERPRRIDWMVPEAHRQNCR-KKGKKEAECHNFIRI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 131 LVSYNVTHLYTCGTFAFSPACTFIELQDSYllpiSEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMR 210
Cdd:cd11261  78 LAIANASHLLTCGTFAFDPKCGVIDVSSFQ----QVERLESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 211 TLG-SQPVLKTDNFLRWLHhDASFVAAIPSTQV----------VYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLL 279
Cdd:cd11261 154 AVGrAEEWIRTETLPSWLN-APAFVAAVFLSPAewgdedgddeIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 280 QKKWTTFLKAQLLCTQPGQ-LPFNVIRHAVLLPA-DSPTAPHIYAVFTSQWQvgGTRSSAVCAFSLLDIERVFKGKYKEL 357
Cdd:cd11261 233 QQRWTTFLKADLLCPGPEHgRASSILQDVTTLRPlPGAGTPIFYGIFSSQWE--GASISAVCAFRPQDIRRVMNGPFREF 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 358 NKETSRWTTYRGPET-NPRPGSC--------SVGPS---SDKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVET 422
Cdd:cd11261 311 KHDCNRGLPVMDSDVpQPRPGECitnnmkllGFGSSlslPDRVLTFVRDHPLMDRPVFpadGHPLLVTTDTAYLRVAAHR 390
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361914 423 AQGLDGHSHLVMYLGTTTGSLHKAVVSGdSSAHLVEEIQLFPDPEPVRNLQLapTQGAVFVGFSGGVWRVP 493
Cdd:cd11261 391 VTSLSGKEYDVLYLGTEDGHLHRAVRIG-AQLSVLEDLALFPEPQPVENLQL--HHNWLLVGSDTEVTQIN 458
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
63-497 3.28e-111

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: 345.88  E-value: 3.28e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  63 DFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKnmIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTC 142
Cdd:cd11239   9 DYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPKK--IYWPASPERIEECKMAGKDPNTECANFVRVLQPYNRTHLYAC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 143 GTFAFSPACTFIEL---QDSYLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLK 219
Cdd:cd11239  87 GTGAFHPICAFINVgrrLEDPIFKLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLGHRHYIR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 220 TDNF-LRWLhHDASFVAA--IPSTQ-----VVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQL 291
Cdd:cd11239 167 TEQYdSRWL-NEPKFVGAylIPDSDnpdddKVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGGQRSLVNKWSTFLKARL 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 292 LCTQPG----QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYkeLNKETS--RWT 365
Cdd:cd11239 246 VCSVPGpdgiDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNV--FKGSAVCVYSMADIRAAFNGPF--AHKEGPnyQWV 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 366 TYRGPETNPRPGSCsvgPSS-------------DKALTFMKDHFLMDEQVV---GTPLLVKSGVEY--TRLAVETAQGLD 427
Cdd:cd11239 322 EYQGKVPYPRPGTC---PSKtygplykstkdfpDDVISFARSHPLMYNPVYplhGRPLLIRTNVPYrlTQIAVDRVEAED 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361914 428 GHSHlVMYLGTTTGSLHKAVV--SGDSSAH--LVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11239 399 GQYD-VLFIGTDSGTVLKVVSlpKENWEMEevILEELQVFKHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
63-497 2.32e-97

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: 309.83  E-value: 2.32e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  63 DFDTLLLSGDGNTLYVGAREAILALDIQDpgVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTC 142
Cdd:cd11254   9 DYRILLKDEDHDRMYVGSKDYVLSLDLHD--INREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNRTHLYVC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 143 GTFAFSPACTFIEL---QDSYLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLK 219
Cdd:cd11254  87 GTGAYNPVCAYINRgrrAEDYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMGKQPAMR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 220 TDNF-LRWLhHDASFVAA--IPST-----QVVYFFFEETASEFDFFERLHtSRVARVCKNDVGGEKLLQKKWTTFLKAQL 291
Cdd:cd11254 167 TDQYnSRWL-NDPAFVHAhlIPDSsekndDKLYFFFREKSLEAPQSPAVL-SRIGRVCLNDDGGHCCLVNKWSTFLKARL 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 292 LCTQPGQ----LPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTY 367
Cdd:cd11254 245 VCSVPGAdgieTHFDELRDVFIQPTQDTKNPVIYAVFSTSGSV--FKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPY 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 368 RGPETNPRPGSCSVG---PS-------SDKALTFMKDHFLMDEQVVGT---PLLVKSGVEY--TRLAVETAQGLDGHsHL 432
Cdd:cd11254 323 TGKIPYPRPGTCPGGtftPSmkstkdyPDEVINFMRTHPLMYNAVYPVhrrPLVVRTNVNYrfTTIAVDQVDAADGR-YE 401
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361914 433 VMYLGTTTGSLHKAVV--SGDSSAH--LVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11254 402 VLFLGTDRGTVQKVIVlpKDDLETEelTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
68-497 1.58e-96

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: 306.95  E-value: 1.58e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  68 LLSGDGNTLYVGAREAILALDIQDPGVprlKNMIPWPASDRKKSECAFKKKSnETQCFNFIRVLVSYNVTHLYTCGTFAF 147
Cdd:cd11237   9 LLDQDGNSLLVGARNAVYNISLSDLTE---NQRIEWPSSDAHREMCLLKGKS-EDDCQNYIRVLAKKSAGRLLVCGTNAY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 148 SPAC-TFIELQDSYLLpiseDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRtlgsQPvLKTDNF-LR 225
Cdd:cd11237  85 KPLCrEYTVKDGGYRV----EREFDGQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYR----EP-LRTERYdLK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 226 WLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLCTQPGQLP--FNV 303
Cdd:cd11237 156 QLN-APNFVSSFAYGDYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLNCSVPGEYPfyFNE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 304 IRhAVLLPAD----SPTAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRG---PEtnPRP 376
Cdd:cd11237 235 IQ-STSDIVEggygGKSAKLIYGVFTT--PVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWLPVPSnkvPE--PRP 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 377 GSCsVGPS---SDKALTFMKDHFLMDEQV---VGTPLLVKSGVEY--TRLAVEtAQ--GLDGHSHLVMYLGTTTGSLHKA 446
Cdd:cd11237 310 GQC-VNDSrtlPDVTVNFIKSHPLMDEAVpsfFGRPILVRTSLQYrfTQIAVD-PQvkALDGKYYDVLFIGTDDGKVLKA 387
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361914 447 VVSGDSSAH------LVEEIQLFPDPEPVRNLQLAPT--QGAVFVGFSGGVWRVPRANC 497
Cdd:cd11237 388 VNIASADTVdkvspvVIEETQVFPRGVPIRNLLIVRGkdDGRLVVVSDDEIVSIPLHRC 446
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
64-497 2.63e-93

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: 299.13  E-value: 2.63e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  64 FDTLLLSGDGNTLYVGAREAILALDIQDpgVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTCG 143
Cdd:cd11250  10 YDALLLDEERGRLFVGAKNYLASLSLDN--ISKQEKKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHLYACG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 144 TFAFSPACTFIEL---QDSYLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKT 220
Cdd:cd11250  88 TGAFHPTCAFVEVgqrMEDHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGQRPSLRT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 221 DNF-LRWLHhDASFVAAI-------PSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLL 292
Cdd:cd11250 168 EQHdSRWLN-EPKFVKVFwipesenPDDDKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKARLV 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 293 CTQPG----QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYR 368
Cdd:cd11250 247 CSVPGneggDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSV--FQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQ 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 369 GPETNPRPGSC---------SVGPSSDKALTFMKDHFLMDEQVV---GTPLLVKSGVEY--TRLAVETAQGLDGHsHLVM 434
Cdd:cd11250 325 GKVPYPRPGMCpsktfgsfeSTKDFPDDVIQFARNHPLMFNPVLplgGRPLFLRTGIPYtfTQIAVDRVAAADGH-YDVM 403
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361914 435 YLGTTTGSLHKAVVSGDSSAH-----LVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11250 404 FIGTDVGSVLKVISVPKGSWPsneelLLEELHVFKDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
62-497 2.49e-92

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: 296.82  E-value: 2.49e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  62 QDFDTLLLSGDGNTLYVGAREAILALDIQDPGvprlKNM--IPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHL 139
Cdd:cd11252   8 LDFQTLLLDEERGRLLLGAKDHIYLLDLVDLN----KNPkkIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNRTHV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 140 YTCGTFAFSPACTFIEL---QDSYLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQP 216
Cdd:cd11252  84 YVCGTGAFHPTCGYIELgthKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLGPTP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 217 ---VLKTDNFLRWLHHDASFVAA--IPST-----QVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTF 286
Cdd:cd11252 164 dhhYIRTDISEHYWLNGAKFIGTfpIPDTynpddDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKWTTF 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 287 LKAQLLCTQPGQ----LPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKETS 362
Cdd:cd11252 244 LKARLVCSIPGPdgadTHFDELQDIFLLPTRDERNPVVYGVFTTTSSI--FKGSAVCVYSMADIRAVFNGPYAHKESPDH 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 363 RWTTYRGPETNPRPGSCsvgPSS-------------DKALTFMKDHFLMDEQV---VGTPLLVKSGVEY--TRLAVETAQ 424
Cdd:cd11252 322 RWVQYEGRIPYPRPGTC---PSKtydplikstkdfpDEVISFIKRHPLMYKSVyplTGGPVFTRINVDYrlTQIVVDHVA 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361914 425 GLDGHsHLVMYLGTTTGSLHKAV-VSGD---SSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11252 399 AEDGQ-YDVMFLGTDIGTVLKVVsITKEkwtMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
75-493 2.01e-90

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: 291.34  E-value: 2.01e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  75 TLYVGAREAILALDIQDPGVPRL--KNMIPWPASDRKKSECAFKKKsNETQCFNFIRVLVSYNVTHLYTCGTFAFSPACT 152
Cdd:cd11242  20 TLYIAARDHVYTVDLDASHTEEIvpSKKLTWRSRQADVENCRMKGK-HKDECHNFIKVLVPRNDETLFVCGTNAFNPVCR 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 153 FIELqdSYLLPISEDkvMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKTDNF-LRWLHhDA 231
Cdd:cd11242  99 NYRI--DTLEQDGEE--ISGMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRSLGDSPTLRTVKYdSKWLK-EP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 232 SFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGG-EKLLQKKWTTFLKAQLLCTQPGQ--LPFNVIRhAV 308
Cdd:cd11242 174 HFVHAVEYGDYVYFFFREIAVEYNTLGKVVFSRVARVCKNDMGGsPRVLEKQWTSFLKARLNCSVPGDshFYFDVLQ-AV 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 309 LLPADSPTAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYrgPET---NPRPGSCSvGPSS 385
Cdd:cd11242 253 TDVIRINGRPVVLGVFTT--QYNSIPGSAVCAFDMDDIEKVFEGRFKEQKSPDSAWTPV--PEDrvpKPRPGCCA-GSGS 327
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 386 -----------DKALTFMKDHFLMDEQV---VGTPLLVKSGVEY--TRLAVETAQGLDGhSHLVMYLGTTTGSLHKAVVS 449
Cdd:cd11242 328 aekyktsndfpDDTLNFIKTHPLMDEAVpsiINRPWFTRTMVRYrlTQIAVDNAAGPYQ-NYTVVFLGSEAGTVLKFLAR 406
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21361914 450 GDSSAH----LVEEIQLF-PDPEPVRN--------LQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11242 407 IGPSGSngsvFLEEIDVYnPAKCSYDGeedrriigLELDRASHALFVAFSGCVIRVP 463
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
64-497 2.82e-89

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: 289.59  E-value: 2.82e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  64 FDTLLLSGDGNTLYVGAREAILALDIQDPgvpRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTCG 143
Cdd:cd11249  32 YHTFLLDEERGRLYVGAKDHIFSFNLVNI---KDFQKIVWPVSPSRRDECKWAGKDILKECANFIKVLKAYNQTHLYACG 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 144 TFAFSPACTFIEL----QDSyLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLK 219
Cdd:cd11249 109 TGAFHPVCTYIEVghhpEDN-IFRLEDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIR 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 220 TDNF-LRWLhHDASFVAA--IPST-----QVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQL 291
Cdd:cd11249 188 TEQHdSRWL-NDPRFISAhlIPESdnpedDKIYFFFRENAIDGEHTGKATHARIGQLCKNDFGGHRSLVNKWTTFLKARL 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 292 LCTQPG----QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTY 367
Cdd:cd11249 267 ICSVPGpngiDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNI--FKGSAVCMYSMTDIRRVFLGPYAHRDGPNYQWVPF 344
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 368 RGPETNPRPGSC---------SVGPSSDKALTFMKDHFLMDEQVV---GTPLLVKSGVEY--TRLAVETAQGLDGHsHLV 433
Cdd:cd11249 345 QGRVPYPRPGTCpsktfggfdSTKDLPDDVITFARSHPAMYNPVFpinNRPIIIKTDVDYqfTQIVVDRVEAEDGQ-YDV 423
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361914 434 MYLGTTTGSLHKAVVSGDSSAH-----LVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11249 424 MFIGTDMGTVLKVVSIPKETWHdleevLLEEMTVFREPTAISAMELSTKQQQLYIGSAIGVSQLPLHRC 492
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
56-493 8.05e-86

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: 278.67  E-value: 8.05e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGvprLKNMIPWPASDRKKSECAFKKKSNEtQCFNFIRVLVSYN 135
Cdd:cd11241   1 FEIEYVSDFSRLVLDPTHDQLIVGARNYLFRLRLQSLS---LLQAVPWNSDEDTKRQCQSKGKSVE-ECQNYVRVLLVVG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 vTHLYTCGTFAFSPACTFIELqdSYLLPISEDkvMEGKGQSPFDPAHKHTAVLV-DGMLYSGTMNNFLGSEPILMRTLGS 214
Cdd:cd11241  77 -KNLFTCGTYAFSPVCTIRKL--SNLTQILDT--ISGVARCPYSPAHNSTALISaSGELYAGTVYDFSGRDPAIYRSLGG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 215 QPVLKTDNF-LRWLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLC 293
Cdd:cd11241 152 KPPLRTAQYnSKWLN-EPNFVGSYEIGNHTYFFFRENAVEHQDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKARLNC 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 294 TQPGQLPF--NVIRHAVLLPaDSPTaphIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTtyrgPE 371
Cdd:cd11241 231 SLPGEFPFyyNEIQGTFYLP-ETDL---IYAVFTT--NVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWL----PT 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 372 TNPRPGSCSVGPSSDKALTFMKDHFLMDEQ-----------VVGTPLLVKSGVEYTRLAVETAQGLDGHSHLVMYLGTTT 440
Cdd:cd11241 301 PNPHPNFQCTTSIDRGQPANTTERDLQDAQkyqlmaevvqpVTKIPLVTMDDVRFSKLAVDVVQGRGTQLVHIFYVGTDY 380
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21361914 441 GSLHKA-VVSGDSSAHLVEEIQLFPD--PEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11241 381 GTILKMyQPHRSQKSCTLEEIKILPAmkGEPITSLQFLKSEKSLFVGLETGVLRIP 436
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
56-493 1.32e-83

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: 272.63  E-value: 1.32e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGvprLKNMIPWPASDRKKSECAFKKKSnETQCFNFIRVLVSYN 135
Cdd:cd11264   1 FTYPGVRDFSQLALDLNRNQLIVGARNYLFRLSLHNVS---LIQATEWGSDEDTRRSCQSKGKT-EEECQNYVRVLIVYG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 vTHLYTCGTFAFSPACTFIELQDSyllpiseDKVME---GKGQSPFDPAHKHTAVLVD-GMLYSGTMNNFLGSEPILMRT 211
Cdd:cd11264  77 -KKVFTCGTNAFSPVCTSRQVGNL-------SKVIErinGVARCPYDPRHNSTAVITSrGELYAATVIDFSGRDPAIYRS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 212 LGSQPVLKTDNF-LRWLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHtSRVARVCKNDVGGEKLLQKKWTTFLKAQ 290
Cdd:cd11264 149 LGSVPPLRTAQYnSKWLN-EPNFIAAYDIGLFTYFFFRENAVEHDCGKTVY-SRVARVCKNDIGGRFLLEDTWTTFMKAR 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 291 LLCTQPGQLPF--NVIRHAVLLPADSptapHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTtyr 368
Cdd:cd11264 227 LNCSRPGEIPFyyNELQSTFYLPEQD----LIYGVFTT--NVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWL--- 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 369 gPETNPRPG-SCSV----GPS---SDKALTFMKDHFLMDE---QVVGTPLLVKSGVEYTRLAVETAQGLDGHSHlVMYLG 437
Cdd:cd11264 298 -PTANPIPNfQCGTlsddSPNenlTERSLQDAQRLFLMNDvvqPVTVDPLVTQDSVRFSKLVVDIVQGKDTLYH-VMYIG 375
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 438 TTTGSLHKAVVSGDSSAH--LVEEIQLFPD--PEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11264 376 TEYGTILKALSTTNRSLRscYLEEMQILPPgqREPIRSLQILHSDRSLFVGLNNGVLKIP 435
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
55-497 4.37e-79

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: 261.77  E-value: 4.37e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  55 FFHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIqDPGVPRLKNmIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSY 134
Cdd:cd11255   1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRL-DQTHPDAKE-IHWPPLPGQREECIRKGKDPETECANFVRVLQPF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 135 NVTHLYTCGTFAFSPACTFIEL--QDSYLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTL 212
Cdd:cd11255  79 NRTHLLACGTGAFQPVCALINVghRGEHVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 213 GSQPVLKTDNFLRWLHhDASFVAA--IPST-----QVVYFFFEETASEFDFFE-RLHTSRVARVCKNDVGGEKLLQKKWT 284
Cdd:cd11255 159 GTRSPLRTETDQRLLH-EPRFVAAhlIPDNadrdnDKVYFFFTERATETAEDDdGAIHSRVGRLCANDAGGQRVLVNKWS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 285 TFLKAQLLCTQPG----QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKE 360
Cdd:cd11255 238 TFIKARLVCSVPGphgiQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNV--FQGFAVCVYSMADIWEVFNGPFAHKDGP 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 361 TSRWTTYRGPETNPRPGSC-------------SVGPSSDKALTFMKDHFLMDEQVV---GTPLLVKSGVEY--TRLAVET 422
Cdd:cd11255 316 DHQWGPYEGKVPYPRPGVCpskitaqpgrafrSTKDYPDEVLQFARAHPLMWRPVYpshRRPVLVKTGLPYrlTQIVVDR 395
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 423 AQGLDGHsHLVMYLGTTTGSLHKAVV--SGDSSAH---LVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11255 396 VEAEDGY-YDVMFIGTDSGSVLKVIVlqKGNSAAGeevTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
63-497 3.26e-78

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: 259.44  E-value: 3.26e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  63 DFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKnmIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTC 142
Cdd:cd11251   9 DYRILFMDEDQDRIYVGSKDHILSLNINNISQDALS--IFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNRTHLYVC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 143 GTFAFSPACTFIELQDSyllpiSEDKVME-------GKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQ 215
Cdd:cd11251  87 GSGAFSPVCVYVNRGRR-----SEEQVFHidskaesGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 216 PVLKTDNF-LRWLHHDAsFVAAI-------PSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFL 287
Cdd:cd11251 162 NAVRTDQHnSKWLSEPI-FVDAHlipdgtdPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTFL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 288 KAQLLCTQPG----QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKETSR 363
Cdd:cd11251 241 KARLVCSVMDedgtETHFDELEDVFLLETDNPRTTLVYGIFTTSSSV--FKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQ 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 364 WTTYRGPETNPRPGSCSVGPSS----------DKALTFMKDHFLMDEQVVGT---PLLVKSGVEY--TRLAVETAQGLDG 428
Cdd:cd11251 319 LIAYQGRIPYPRPGTCPGGAFTpnmqstkefpDDVVTFIRNHPLMFNPIYPIgrrPLLVRTGTDYkyTKIAVDRVNAADG 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361914 429 HSHlVMYLGTTTGSLHKAVV-SGDSSAH---LVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11251 399 RYH-VLFLGTDKGTVQKVVVlPTNGSLSgelILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
56-493 5.03e-78

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: 257.65  E-value: 5.03e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGvprLKNMIPWPASDRKKSECAFKKKSNEtQCFNFIRVLVsYN 135
Cdd:cd11263   1 FRAENAVDFSQLTFDPGQKELIVGARNYLFRLQLEDLS---LIQAVEWECDEATKKACYSKGKSKE-ECQNYIRVLL-VG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 136 VTHLYTCGTFAFSPACTFIELQDsyLLPISEDkvMEGKGQSPFDPAHKHTAVLV-DGMLYSGTMNNFLGSEPILMRTLGS 214
Cdd:cd11263  76 GDRLFTCGTNAFTPICTNRTLNN--LTEIHDQ--ISGMARCPYSPQHNSTALLTsSGELYAATAMDFPGRDPAIYRSLGI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 215 QPVLKTDNF-LRWLHhDASFVAAIPSTQVVYFFFEETASEFDFfERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLC 293
Cdd:cd11263 152 LPPLRTAQYnSKWLN-EPNFVSSYDIGNFTYFFFRENAVEHDC-GKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNC 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 294 TQPGQLPF--NVIRHAVLLpadsPTAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRGPE 371
Cdd:cd11263 230 SRPGEIPFyyNELQSTFFL----PELDLIYGIFTT--NVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAWLPYPNPN 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 372 TNPRPGSCSVGPS---SDKALTFMKDHFLMDE---QVVGTPLLVKSGVEYTRLAVETAQGLDGHSHLVmYLGTTTGSLHK 445
Cdd:cd11263 304 PNFQCGTMDQGLYvnlTERNLQDAQKFILMHEvvqPVTPVPYFMEDNSRFSHVAVDVVQGKDMLFHII-YLATDYGTIKK 382
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 21361914 446 --AVVSGDSSAHLVEEIQLFPDP--EPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11263 383 vlAPLNQSSSSCLLEEIELFPKRqrEPIRSLQILHSQSVLFVGLQEHVIKIP 434
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
75-495 6.96e-75

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: 250.13  E-value: 6.96e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  75 TLYVGAREAILALDIQDPGVPRLK--NMIPWPASDRKKSECAFKKKsNETQCFNFIRVLVSYNVTHLYTCGTFAFSPACT 152
Cdd:cd11267  20 TLYIGDRDNLYRVELDPTAGTEMRyhKKLTWRSNKNDINVCRMKGK-HEGECRNFIKVLLLRDYGTLFVCGTNAFNPVCA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 153 FIELQDsyLLPISEDkvMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKTdnflrwLHHDAS 232
Cdd:cd11267  99 NYSIDT--LEPVGDN--ISGMARCPYDPKHANVALFADGMLFTATVTDFLAIDAVIYRSLGDSPALRT------VKHDSK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 233 ------FVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGG-EKLLQKKWTTFLKAQLLCTQPG--QLPFNV 303
Cdd:cd11267 169 wfkepyFVHAVEWGSHVYFFFREIAMEFNYLEKVVVSRVARVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGdsHFYFNV 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 304 IrHAVLLPADSPTAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYrgPET---NPRPGSCs 380
Cdd:cd11267 249 L-QAVSDILNLGGRPVVLAVFST--PTNSIPGSAVCAFDMTQVAAVFEGRFREQKSPESIWTPV--PEElvpRPRPGCC- 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 381 VGPSS---------DKALTFMKDHFLMDEQVV---GTPLLVKSGVEY--TRLAVETAQGLDGhSHLVMYLGTTTGSLHKA 446
Cdd:cd11267 323 AAPGMrynssstlpDEVLNFVKTHPLMDEAVPslgHAPWIVRTMTRYqlTHMVVDTEAGPHG-NHTVVFLGSTRGTVLKF 401
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361914 447 VV--SGDSSAH-----LVEEIQLFP-----DPEP----VRNLQLAPTQGAVFVGFSGGVWRVPRA 495
Cdd:cd11267 402 LIipNASSSEIsnqsvFLEELETYNpercgWDSPqaqkLLSLELDKGSGGLLLAFPSCVVRVPVA 466
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
63-493 4.92e-72

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: 242.63  E-value: 4.92e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  63 DFDTLLLSGDgnTLYVGAREAILALDIQDpgVPRlKNMIP-----WPASDRKKSECAFKKKSNEtQCFNFIRVLVSYNVT 137
Cdd:cd11269  10 DFQLMLKIRD--TLYIAGRDQVYTVNLNE--VPK-TEVTPsrkltWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRNDE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 138 HLYTCGTFAFSPACTFIELQDSYLlpisEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPV 217
Cdd:cd11269  84 MVFVCGTNAFNPMCRYYRLSTLEY----DGEEISGLARCPFDARQTNVALFADGKLYSATVADFLASDAVIYRSMGDGSA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 218 LKTDNF-LRWLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGG-EKLLQKKWTTFLKAQLLCTQ 295
Cdd:cd11269 160 LRTIKYdSKWIK-EPHFLHAIEYGNYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQRVLEKHWTSFLKARLNCSV 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 296 PGQ--LPFNVIRhAVLLPADSPTAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYrgPET- 372
Cdd:cd11269 239 PGDsfFYFDVLQ-SITDIIEINGIPTVVGVFTT--QLNSIPGSAVCAFSMDDIEKVFKGRFKEQKTPDSVWTAV--PEDk 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 373 --NPRPGSCSVGPSS----------DKALTFMKDHFLMDEQV---VGTPLLVKSGVEY--TRLAVETAQGlDGHSHLVMY 435
Cdd:cd11269 314 vpKPRPGCCAKHGLAeayktsidfpDETLSFIKSHPLMDSAVpsiIEEPWFTKTRVRYrlTAIAVDHAAG-PHQNYTVIF 392
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361914 436 LGTTTGSLHKAVVSGD----SSAHLVEEIQLF---------PDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11269 393 VGSEAGVVLKILAKTSpfslNDSVLLEEIEAYnhakcsaenEEDRRVISLQLDRDHHALFVAFSSCVVRIP 463
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
55-497 1.75e-71

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: 241.30  E-value: 1.75e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  55 FFHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKnmIPWPASDRKKSECAFKKKsNETQCFNFIRVLVSY 134
Cdd:cd11253   1 FHSPFGFLDLHTMLLDEYQERLFVGGRDLLYSLSLERISANYKE--IHWPSTQLQVEDCIMKGR-DKPECANYIRVLHHY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 135 NVTHLYTCGTFAFSPACTFIEL---QDSYLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRT 211
Cdd:cd11253  78 NRTHLLACGTGAFDPVCAFIRVgrgSEDHLFQLESDKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 212 LGSQPVLKTDNFLRWLHHDASFV--AAIPSTQ-----VVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWT 284
Cdd:cd11253 158 MNHLAHIRTEHDDERLLKEPKFVgsYMIPDNEdpddnKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRMLVNKWS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 285 TFLKAQLLCTQPG----QLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVggTRSSAVCAFSLLDIERVFKGKYKELNKE 360
Cdd:cd11253 238 TFLKTRLICSVPGpngiDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNI--FKGYAICVYHMASIRAAFNGPFAHKEGP 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 361 TSRWTTYRGPETNPRPGSC----------SVGPSSDKALTFMKDHFLMDEQVVGT---PLLVKSGVEY--TRLAVETAQG 425
Cdd:cd11253 316 EYHWSVYEGKVPYPRPGSCaskvngghygTTKDYPDEALRFARSHPLMYQAVKPVhkrPILVKTDGKYnlKQIAVDRVEA 395
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361914 426 LDGHSHlVMYLGTTTGSLHKAVVSGDSSAH-----LVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANC 497
Cdd:cd11253 396 EDGQYD-VLFIGTDNGIVLKVITIYNQETEtmeevILEELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
64-478 6.82e-71

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: 239.25  E-value: 6.82e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  64 FDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLK-NMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYN-VTHLYT 141
Cdd:cd11238   3 YRTLLLDEKRNALYVGAMDRVFRLNLYNINDTGNNcARDELTLSPSDVSECVSKGKDEEYECRNHVRVIQPMGdGQTLYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 142 CGTFAFSPACTFIELQDSYLLPISEDkVMEGKGQSPFDPAHKHTAVLVDG-------MLYSGTMNNFLGSEPILMRTlgs 214
Cdd:cd11238  83 CSTNAMNPKDRVLDANLLHLPEYVPG-PGNGIGKCPYDPDDNSTAVWVEWgnpgdlpALYSGTRTEFTKANTVIYRP--- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 215 qPVLKT-----DNFLRWLHHDA------SFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKW 283
Cdd:cd11238 159 -PLYNNtkgrhESFMRTLKYDSkwldepNFVGSFDIGDYVYFFFRETAVEYINCGKVVYSRVARVCKKDTGGKNVLRQNW 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 284 TTFLKAQLLCTQPGQLP--FNVIRHAVLLPADSPTapHIYAVFTSQwQVGGTrSSAVCAFSLLDIERVF-KGKYKELNKE 360
Cdd:cd11238 238 TTFLKARLNCSISGEFPfyFNEIQSVYKVPGRDDT--LFYATFTTS-ENGFT-GSAVCVFTLSDINAAFdTGKFKEQASS 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 361 TSRW---TTYRGPEtnPRPGSCSVGPS--SDKALTFMKDHFLMDEQV-VGTPLLVKSGVEYTRLAVETAQGLDGHsHLVM 434
Cdd:cd11238 314 SSAWlpvLSSEVPE--PRPGTCVNDSAtlSDTVLHFARTHPLMDDAVsHGPPLLYLRDVVFTHLVVDKLRIDDQE-YVVF 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 21361914 435 YLGTTTGSLHKAVV---SGDSSAHLVEEIQLFPdPEPVRNLQLAPTQ 478
Cdd:cd11238 391 YAGSNDGKVYKIVHwkdAGESKSNLLDVFELTP-GEPIRAMELLPGE 436
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
75-493 1.57e-69

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: 236.08  E-value: 1.57e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  75 TLYVGAREAILALDIQDPGVPRL--KNMIPWPASDRKKSECAFKKKSNEtQCFNFIRVLVSYNVTHLYTCGTFAFSPACT 152
Cdd:cd11266  20 TLYIAARDHIYTVDIDTSHTEEIyfSKKLTWKSRQADVDTCRMKGKHKD-ECHNFIKVLLKRNDDTLFVCGTNAFNPSCR 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 153 FIELQDSYLLpiseDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKTDNF-LRWLhHDA 231
Cdd:cd11266  99 NYKMDTLEFF----GDEFSGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHdSKWL-KEP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 232 SFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGG-EKLLQKKWTTFLKAQLLCTQPG--QLPFNVIRhAV 308
Cdd:cd11266 174 YFVQAVDYGDYIYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGsQRVLEKQWTSFLKARLNCSVPGdsHFYFNILQ-AV 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 309 LLPADSPTAPHIYAVFTSQWQvgGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTY---RGPEtnPRPGSCSvGPSS 385
Cdd:cd11266 253 TDVIHINGRDVVLATFSTPYN--SIPGSAVCAYDMLDIASVFTGRFKEQKSPDSTWTPVpdeRVPK--PRPGCCA-GSSS 327
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 386 -----------DKALTFMKDHFLMDEQV---VGTPLLVKSGVEY--TRLAVETAQGlDGHSHLVMYLGTTTGSLHKAVVS 449
Cdd:cd11266 328 lekyatsnefpDDTLNFIKTHPLMDEAVpsiINRPWFLRTMVRYrlTKIAVDNAAG-PYQNHTVVFLGSEKGIILKFLAR 406
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361914 450 GDSSAHL-----VEEIQLFpDPEP----------VRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11266 407 TGNSGFLndslfLEEMNVY-NSEKcsydgvedkrIMGMQLDKASSALYVAFSTCVIKVP 464
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
304-474 3.37e-66

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: 217.14  E-value: 3.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914   304 IRHAVLLPADSPTA--PHIYAVFTSQWqVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRGPETNPRPGSCSV 381
Cdd:pfam01403   1 LQDVFVLKPGAGDAldTVLYGVFTTQW-SNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914   382 GPS----SDKALTFMKDHFLMDEQVV---GTPLLVKSGVEYTRLAVETAQGLDGHsHLVMYLGTTTGSLHKAVVSGDSSA 454
Cdd:pfam01403  80 DPLrldlPDSVLNFVKDHPLMDEAVQpvgGRPLLVRTGVRLTSIAVDRVQALDGN-YTVLFLGTDDGRLHKVVLVGSEES 158
                         170       180
                  ....*....|....*....|
gi 21361914   455 HLVEEIQLFPDPEPVRNLQL 474
Cdd:pfam01403 159 HIIEEIQVFPEPQPVLNLLL 178
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
56-493 1.07e-65

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: 224.66  E-value: 1.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  56 FHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDpgvprLKNM--IPWPASDRKKSECAFKKKSNEtQCFNFIRVLVS 133
Cdd:cd11265   1 FSDPEVTSYSQMLFDVARNQVIVGARDNLYRLSLDG-----LELLerASWPAAESKVALCQNKGQSEE-DCHNYVKVLLS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 134 YNvTHLYTCGTFAFSPACTFIELQDsyLLPISEdkVMEGKGQSPFDPAHKHTAVL-VDGMLYSGTMNNFLGSEPILMRTL 212
Cdd:cd11265  75 YG-KQLFACGTNAFSPRCSWREMEN--LTSVTE--WDSGVAKCPYSPHANITALLsSSGQLFVGSPTDFSGSDSAIYRTL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 213 G--SQPVLKTDNF-LRWLHhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQK-KWTTFLK 288
Cdd:cd11265 150 GtsNKSFLRTKQYnSKWLN-EPQFVGSFETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLLKdNWTTFLK 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 289 AQLLCTQPGQLPF--NVIRHAVLLPADSPtaphIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTT 366
Cdd:cd11265 229 ARLNCSLPGEYPFyfDEIQGMTYLPDEGI----LYATFTT--PENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWER 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 367 YRGPETNPRPGSCSVGPSSdkaLTFMKDHFLMDEQVVGT---PLLVKSGVEYTRLAVE-TAQGLDGHSHlVMYLGTTTGS 442
Cdd:cd11265 303 VNVNHRDHFNQCSSSSSSH---LLESSRYQLMDEAVQPItlePLHHAKLERFSHIAVDvIPTKIHQSVH-VLYVATTGGL 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 21361914 443 LHKAVVSGDSSAH-LVEEIQLFPDPE-PVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11265 379 IKKISVLPRTQETcLVEIWQPLPTPDsPIKTMQYLKVTDSLYVGTELALMRIP 431
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
75-493 2.81e-63

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: 218.82  E-value: 2.81e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  75 TLYVGAREAILALDI---QDPGVPrlKNMIPWPASDRKKseCAFKKKSNEtQCFNFIRVLVSYNVTHLYTCGTFAFSPAC 151
Cdd:cd11270  20 MVYIAARDHVFAINLsasLERIVP--QQKLTWKTKDVEK--CTVRGKNSD-ECYNYIKVLVPRNDETLFACGTNAFNPTC 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 152 TfielqdSYLLPISEDKVMEGKGQS--PFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQ-PVLKTDNF-LRWL 227
Cdd:cd11270  95 R------NYKMSSLEQDGEEVIGQArcPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLGESsPVLRTVKYdSKWL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 228 HhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGE-KLLQKKWTTFLKAQLLCTQPGQ--LPFNVI 304
Cdd:cd11270 169 R-EPHFLHAIEYGNYVYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSpRVLERYWTSFLKARLNCSVPGDsfFYFDVL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 305 RHAV-LLPADSptAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYrgPET---NPRPGSCS 380
Cdd:cd11270 248 QSLTnVMQINH--RPAVLGVFTT--QANSITGSAVCAFYMDDIEKVFNGKFKEQRNSESAWTPV--PDEavpKPRPGSCA 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 381 -VGPSS---------DKALTFMKDHFLMDEQVVG---TPLLVKSGVEY--TRLAVETAQGLDGhSHLVMYLGTTTGSLHK 445
Cdd:cd11270 322 gDGPAAgyksstnfpDETLTFIKSYPLMDEAVPSvnnRPCFTRTTSRFklTQIAVDTAAGPYK-NYTVVFLGSENGHVLK 400
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361914 446 aVVSGDSSAH-----LVEEIQLF--------PDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11270 401 -VLASMHPNSsystqVLEDIDVYnpnkcnvrGEDRRILGLELDKDHHALFVAFTGCVIRVP 460
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
63-493 4.99e-61

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: 210.52  E-value: 4.99e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  63 DFDTLLLSGDGNTLYVGAREAILALDIqDPGVPRLKNMIP---WPASDRKKSECAfKKKSNETQCFNFIRVLVS-YNVTH 138
Cdd:cd09295   1 DDDKILVSFRKDTIYVGAIARIYKVDG-GGTRLLLSCISPelnFGFNEDQKAFCP-LRRGKWTECINYIKVLQQkGDLDI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 139 LYTCGTFAFSPACTFIELQDSYLLpiSEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFL-GSEPILMRTLGSQPV 217
Cdd:cd09295  79 LAVCGSNAAQPSCGSYRLDVLVEL--GKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNVHY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 218 LKTDNFLRWLHHDASFVAAIPSTQV---VYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLCT 294
Cdd:cd09295 157 LRIVVDSSTGLDEITFVYAFVSGDDddeVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTSFLKADLNCS 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 295 QPGQ-LPFNVIRHAVLLPADSpTAPHIYAVFTSQWQVGGtrSSAVCAFSLLDIERVFkgkykelnketsrwttyrgpetn 373
Cdd:cd09295 237 RPQSgFAFNLLQDATGDTKNL-IQDVKFAIFSSCLNKSV--ESAVCAYLFTDINNVF----------------------- 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 374 prpgscsvgpssdkaltfmkdhflmDEQVVGT---PLLVKSGVE--YTRLAVETAQGlDGHSHLVMYLGTTTGSLHKAVV 448
Cdd:cd09295 291 -------------------------DDPVEAInnrPLYAHQNQRsrLTSIAVDATKQ-KSVGYQVVFLGLKLGSLGKALA 344
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 21361914 449 SGDSSA-HLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd09295 345 FFFLYKgHIIEEWKVFKDSSRITNLDLSRPPLYLYVGSESGVLGVP 390
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
75-493 9.51e-58

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: 203.78  E-value: 9.51e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  75 TLYVGAREAILALDIQ--DPGVPRLKN-MIPWPASDRKKseCAFKKKSNEtQCFNFIRVLVSYNVTHLYTCGTFAFSPAC 151
Cdd:cd11268  20 TLLVAARDHVFSFDLQaeEEGEGLVPNkYLTWRSQDVEN--CAVRGKLTD-ECYNYIRVLVPWDSQTLLACGTNSFSPVC 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 152 T---FIELQdsyllpiSEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKTDNF-LRWL 227
Cdd:cd11268  97 RsygITSLQ-------QEGEELSGQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYdSKWL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 228 HhDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGE-KLLQKKWTTFLKAQLLCTQPGQLPFNV-IR 305
Cdd:cd11268 170 R-EPHFVQALEHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSpRALDRHWTSFLKLRLNCSVPGDSTFYFdVL 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 306 HAVLLPADSPTAPHIYAVFTSqwQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTY---RGPetNPRPGSCS-V 381
Cdd:cd11268 249 QALTGPVNLHGRSALFGVFTT--QTNSIPGSAVCAFYLDEIERGFEGKFKEQRSLDGAWTPVsedRVP--SPRPGSCAgV 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 382 GPSS---------DKALTFMKDHFLMDEQV---VGTPLL-VKSGVEYTRLAVETAQGldGHSHL-VMYLGTTTGSLHKAV 447
Cdd:cd11268 325 GGAAlfsssrdlpDDVLTFIKAHPLLDPAVppvTHQPLLtLTSRALLTQVAVDGMAG--PHSNItVMFLGSNDGTVLKVL 402
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361914 448 VSGDSSAH----LVEEIQLFpdpEPVR--------------NLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11268 403 PPGGRSGGpepiLLEEIDAY---SPARcsgkrtaqtarriiGLELDTEGHRLFVAFSGCIVYLP 463
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
55-493 9.81e-57

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: 199.69  E-value: 9.81e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  55 FFHQKGlqdfdtlllsgdGNTLYVGAREAILALDIqdpgvPRLKNMIPWPASDRKKSECafKKKSNETQCFNFIRVLVSY 134
Cdd:cd11243   7 FFHEAG------------SSSVYVGGQGALYLLDF-----TGSAVIVKKIPDEKTEKDC--KKRATLDDCENYITLIKKL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 135 NvTHLYTCGTFAFSPACTFIELQDsyLLPISEDKvmegkGQSPFDPaHKHTAVLVDGM-LYSgTMNNFLGSEPIlMRTLG 213
Cdd:cd11243  68 D-YRLLVCGTNAGSPKCWFLVNQT--LVTLSADR-----GVAPFLP-DENSLVLIEGNnVYS-TISGKKGNIPR-FRRYG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 214 SQPVLKT-DNFLRwlhhDASFVAA--IPSTQV----VYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQ-KKWTT 285
Cdd:cd11243 137 GKKELYTsDTVMQ----KPQFVKAtlLPEDEQyqdkIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLStSKWST 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 286 FLKAQLLCTQPGQ-LPFNVIRHAVLLPADSPTAPHIYAVFTSQWQvggtrSSAVCAFSLLDIERVFKgkykelnkeTSRW 364
Cdd:cd11243 213 FLKARLVCGDPATpMNFNRLQDVFLLPKEEWREAVVYGVFSNTWG-----SSAVCSYSLGDIDKVFR---------TSSL 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 365 TTYRGPETNPRPGSCSVG--PSSDKALTFMKDHFLMDEQV-----VGTPLLvKSGVEYTRLAVETAQGLDGHSHLVMYLG 437
Cdd:cd11243 279 KGYSGSLPNPRPGTCVPPeqTHPSETFSFADEHPELDDRIepdepRKLPVF-QNKDHYQKVVVDEVRASDGVSYDVLYLA 357
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21361914 438 TTTGSLHKAVVSGDSsAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11243 358 TDKGKIHKVVESKGQ-THNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLP 412
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
228-523 7.99e-13

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: 71.50  E-value: 7.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 228 HHDASFVAAIPSTQVVYFFF--EET------ASEFDFFerlHTSRVARVCKNDvggekllqKKWTTFLKAQLLCTQpGQL 299
Cdd:cd11272 201 HFDIFYIYGFASGNFVYFLTvqPETpegvsiNSAGDLF---YTSRIVRLCKDD--------PKFHSYVSLPFGCVR-GGV 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 300 PFNVIRHAVLLPADSPTAPH---------IYAVFTS-QWQVGGT-RSSAVCAFSLLDIERVFKGKYKelnketsrwTTYR 368
Cdd:cd11272 269 EYRLLQAAYLSKPGEVLARSlnitaqedvLFAIFSKgQKQYHHPpDDSALCAFPIRAINAQIKERLQ---------SCYQ 339
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 369 GP---ETNPRPG---SCSvgpssdKALTFMKDHF--LMDEQVVGTPLLVKSGVEYT----RLAVETAQGLDGHShlVMYL 436
Cdd:cd11272 340 GEgnlELNWLLGkdvQCT------KAPVPIDDNFcgLDINQPLGGSTPVEGVTLYTssrdRLTSVASYVYNGYS--VVFV 411
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 437 GTTTGSLHKavVSGDSSAH---LVEEIQLFPDPEPV-RNLQLAPTQGAVFVGFSGGVWRVPRANCSVYESCVDCVLARDP 512
Cdd:cd11272 412 GTKSGKLKK--IRADGPPHggvQYEMVSVFKDGSPIlRDMAFSIDHKYLYVMSERQVSRVPVESCEQYTTCGECLSSGDP 489
                       330
                ....*....|.
gi 21361914 513 HCAWDPESRTC 523
Cdd:cd11272 490 HCGWCALHNMC 500
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
496-540 3.39e-10

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 56.18  E-value: 3.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 21361914   496 NCSVYESCVDCVLARDPHCAWDPESRTC-----CLLSAPNLNSWKQDMER 540
Cdd:pfam01437   1 RCSQYTSCSSCLAARDPYCGWCSSEGRCvrrsaCGAPEGNCEEWEQASSK 50
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
228-483 9.20e-10

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


Pssm-ID: 200497 [Multi-domain]  Cd Length: 401  Bit Score: 61.19  E-value: 9.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 228 HHDASFVAAIPSTQVVYFFFEETASEFDffERLHTSRVARVCKNDvggekllqKKWTTFLKAQLLCTQPGQLPFNVIRHA 307
Cdd:cd11236 180 RYSIKYVYGFSSGGFSYFVTVQRKSVDD--ESPYISRLVRVCQSD--------SNYYSYTEVPLQCTGGDGTNYNLLQAA 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 308 VLLPADSPTAPHI---------YAVFTSQWQVGGTRS--SAVCAFSLLDIERVFKgkykelnketsrwttyrgpetnprp 376
Cdd:cd11236 250 YVGKAGSDLARSLgistdddvlFGVFSKSKGPSAEPSskSALCVFSMKDIEAAFN------------------------- 304
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 377 GSCSVGPSSDkaltfmkdhflmdeqVVGTPLLvkSGVEYTRLAVETAqgldgHSHLVMYLGTTTGSLHKAVVSGDSSAHL 456
Cdd:cd11236 305 DNCPLGGGVP---------------ITTSAVL--SDSLLTSVAVTTT-----RNHTVAFLGTSDGQLKKVVLESSSSATQ 362
                       250       260
                ....*....|....*....|....*..
gi 21361914 457 VEEIQLFPDPEPVRNLQLAPTQGAVFV 483
Cdd:cd11236 363 YETLLVDSGSPILPDMVFDPDGEHLYV 389
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
496-541 7.33e-09

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 52.16  E-value: 7.33e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 21361914    496 NCSVYESCVDCVLARDPHCAWDPESRTCclLSAPNLNSWKQDMERG 541
Cdd:smart00423   1 RCSKYTSCSECLLARDPYCAWCSSQGRC--TSGERCDSRRQNWLSG 44
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
228-493 1.47e-08

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


Pssm-ID: 200537 [Multi-domain]  Cd Length: 449  Bit Score: 57.86  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 228 HHDasFVAAIPSTQVVYFFFEET----ASEFDFferlhtsrVARVCKNDVGgekllqkkWTTFLKAQLLCTQPGQlPFNV 303
Cdd:cd11276 189 TQQ--FRYAFEDNNYVYFLFNQQlghpDKNRTL--------IARLCENDHH--------YYSYTEMDLNCRDGAN-AYNK 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 304 IRHA-------VLLPADSPTAPH---IYAVFTSQwqVGGTRSSAVCAFSLLDI----ERVFKGKYKELNKETSrwtTYRG 369
Cdd:cd11276 250 CQAAyvstpgkELAQNYGNSILSdkvLFAVFSRD--EKDSGESALCMFPLKSInakmEANREACYTGTIDDRD---VFYK 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 370 PETNPRPGSC-SVGPSSDKALTFMKDHF-----LMDEQVVGTPLLVKSGVEYTRLAVETAQGldghsHLVMYLGTTTGSL 443
Cdd:cd11276 325 PFHSQKDIICgSHQQKNSKSFPCGSEHLpyplgSRDELALTAPVLQRGGLNLTAVTVAVENG-----HTVAFLGTSDGRI 399
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361914 444 HKAVVSGDSSAHLVEEIQLfpdPEPV-RNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11276 400 LKVHLSPDPEEYNSILIEK---NKPVnKDLVLDKTLEHLYIMTEDKVFRLP 447
Ig_Sema4B_like cd05872
Immunoglobulin (Ig)-like domain of the class IV semaphorin Sema4B; The members here are ...
566-638 4.71e-08

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: 50.90  E-value: 4.71e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361914 566 KEVLAVPNSILELPCPHLSALASYYWSH-GPAAVPEASSTVY--NGSLLLIVQDGVGGLYQCWATENGFSYPVISY 638
Cdd:cd05872   4 KFRTVVAGADVVLPCQLRSNLASPVWLFnGTPLNAQFSYLRLgtDGLLILVTSPEHSGTYRCYSEEEGFQQLVASY 79
Sema_plexin_A4 cd11274
The Sema domain, a protein interacting module, of Plexin A4; Plexin A4 forms a receptor ...
130-498 1.38e-07

The Sema domain, a protein interacting module, of Plexin A4; Plexin A4 forms a receptor complex with neuropilins (NRPs) and transduces signals for class 3 semaphorins in the nervous system. It regulates facial nerve development by functioning as a receptor for Sema3A/NRP1. Both plexins A3 and A4 are essential for normal sympathetic development. They function both cooperatively, to regulate the migration of sympathetic neurons, and differentially, to guide sympathetic axons. Plexin A4 is also expressed in lymphoid tissues and functions in the immune system. It negatively regulates T lymphocyte responses. 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: 200535 [Multi-domain]  Cd Length: 473  Bit Score: 54.57  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 130 VLVSYNVTHLYTCGTFaFSPACTFIELQDSYLLPisedkvmegkgqspfDPAHKHTAVL--------VDGMLYSGTMNN- 200
Cdd:cd11274  80 LLIDYKENRLIACGSL-YQGICKLLRLDDLFKLG---------------EPFHKKEHYLsgvnesgsVFGVIVSYSNLDd 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 201 --FLGS----EPILMRTLGSQPVLK---TDNFLRWLHHDaSFVAA---IPSTQV-------VYFFFEETASEFDFF---- 257
Cdd:cd11274 144 klFIATavdgKPEYFPTISSRKLTKnseADGMFAYVFHD-EFVASmikIPSDTFtiipdfdIYYIYGFSSGNFVYFltlq 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 258 ------------ERLHTSRVARVCKNDVGgekllqkkWTTFLKAQLLCTQPGqLPFNVIRHAVLLPADS---------PT 316
Cdd:cd11274 223 pemisppgsttkEQVYTSKLVRLCKEDTA--------FNSYVEVPIGCEKNG-VEYRLLQAAYLSKAGAilarslgvgPD 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 317 APHIYAVFT--SQWQVGGTRSSAVCAFSLLDIERVFKGKYKelnketsrwTTYRGPET------NPRPGSCSvgpssdKA 388
Cdd:cd11274 294 DDILFTVFSkgQKRKMKSLDESALCIFVLKEINDRIKDRLQ---------SCYRGEGTldlawlKVKDIPCS------SA 358
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 389 LTFMKDHFL---------MDEQVVGTPLLVKSGVEYTRLAVETAQgldghSHLVMYLGTTTGSLHKAVVSGDSSAHLVEE 459
Cdd:cd11274 359 LLTIDDNFCgldmnaplgVSEMVRGLPVFTEDRDRMTSVIAYVYK-----NHSLAFVGTKSGKLKKIRVDGTTKNALQYE 433
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 21361914 460 IQLFPDPEPV-RNLQLAPTQGAVFVGFSGGVWRVPRANCS 498
Cdd:cd11274 434 TVQVVDTGPIlRDMAFSKDHEQLYIMSEKQLTRVPVESCG 473
Sema_plexin_A cd11244
The Sema domain, a protein interacting module, of Plexin A; Plexins serve as receptors of ...
130-493 2.41e-07

The Sema domain, a protein interacting module, of Plexin A; Plexins serve as receptors of semaphorins and may be the ancestor of semaphorins. Members of the Plexin A subfamily are receptors for Sema1s, Sema3s, and Sema6s, and they mediate diverse biological functions including axon guidance, cardiovascular development, and immune function. Guanylyl cyclase Gyc76C and Off-track kinase (OTK), a putative receptor tyrosine kinase, modulate Sema1a-Plexin A mediated axon repulsion. Sema3s do not interact directly with plexin A receptors, but instead bind Neuropilin-1 or Neuropilin-2 toactivate neuropilin-plexin A holoreceptor complexes. In contrast to Sema3s, Sema6s do not require neuropilins for plexin A binding. In the complex, plexin As serve as signal-transducing subunits. An increasing number of molecules that interact with the intracellular region of Plexin A have been identified; among them are IgCAMs (in axon guidance events) and Trem2-DAP12 (in immune responses). 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: 200505 [Multi-domain]  Cd Length: 470  Bit Score: 54.06  E-value: 2.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 130 VLVSYNVTHLYTCGTfAFSPACTFIELQDSYLLPisedkvmegkgqspfDPAHKHTAVLvDGMLYSGTMNN--------- 200
Cdd:cd11244  80 LLIDYSENRLIACGS-LYQGVCKLLRLEDLFKLG---------------EPHHKKEHYL-SGVNESGTMFGvivsysngd 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 201 ---FLGS----EPILMRTLGSQPVLK---TDNFLRWLHHDaSFVAA---IPS---TQV----VYFFFEETASEFDFF--- 257
Cdd:cd11244 143 dklFIGTavdgKSEYFPTLSSRKLTAdeeSDGMFAYVYHD-EFVSSqikIPSdtlSIIpdfdIYYVYGFSSGNFVYFltl 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 258 -------------ERLHTSRVARVCKNDvggekllqKKWTTFLKAQLLCTQPGqLPFNVIRHAVLLPAD---------SP 315
Cdd:cd11244 222 qpetqltpgdstgEQFYTSKIVRLCKDD--------TKFYSYVEFPIGCTRDG-VEYRLLQAAYLSKPGkalaqalgiSE 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 316 TAPHIYAVFtSQWQ---VGGTRSSAVCAFSLLDIERVFKGKYKelnketsrwTTYRGPETNPRPGSCSVGPSSDKALTFM 392
Cdd:cd11244 293 DEDVLFTIF-SKGQknrMKPPDESALCLFTLKQINLRIKERLQ---------SCYRGEGKLSLPWLLNKDLPCINAPLQI 362
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 393 KDHFLmdEQVVGTPLLVKSGVEYTRLAVETAQGL------DGHSHLVMYLGTTTGSLHKAVVSGDSSAHLVEEIQLFPDP 466
Cdd:cd11244 363 DDNFC--GLDMNQPLGGSDMVEGIPLFTDDRDRMtsvaayVYKGHSVVFVGTKSGKLKKIRVDGPPHNALQYETVQVVEG 440
                       410       420
                ....*....|....*....|....*...
gi 21361914 467 EPV-RNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11244 441 SPIlRDMAFSPDHQYLYIMSERQVTRVP 468
Sema_plexin_A3 cd11273
The Sema domain, a protein interacting module, of Plexin A3; Plexin-A3 forms a receptor ...
214-493 1.34e-06

The Sema domain, a protein interacting module, of Plexin A3; Plexin-A3 forms a receptor complex with neuropilin-2 and transduces signals for class 3 semaphorins in the nervous system. Both plexins A3 and A4 are essential for normal sympathetic neuron development. They function cooperatively to regulate the migration of sympathetic neurons, and differentially to guide sympathetic axons. Both plexins A3 and A4 are not required for guiding neural crest precursors prior to reaching the sympathetic anlagen. Plexin A3 is a major driving force for intraspinal motor growth cone guidance. 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: 200534 [Multi-domain]  Cd Length: 469  Bit Score: 51.47  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 214 SQPVLKTDNFLRWLHHDASFVAAIPSTQVVYFFFEETASEFDFF----ERLHTSRVARVCKNDVggekllqkKWTTFLKA 289
Cdd:cd11273 187 SQIKIPSDTLSLYPAFDIYYVYGFVSASFVYFLTLQLDTQQTLLdtagEKFFTSKIVRMCANDT--------EFYSYVEF 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 290 QLLCT---------QPGQL--PFNVIRHAVLLPADSPTaphIYAVFtSQWQ---VGGTRSSAVCAFSLLDIERVFKGKYK 355
Cdd:cd11273 259 PLGCSkdgveyrlvQAAHLakPGLLLAQALGVPEDEDV---LFTIF-SQGQknrASPPRETILCLFTLSNINAHIRERIQ 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 356 elnketsrwTTYRGPETNPRPG------SCSVGPS--SDKALTFMKDHFLMDEQVV-GTPLLVKSGVEYTRLAVETAQGl 426
Cdd:cd11273 335 ---------SCYRGEGTLSLPWllnkelPCINTPMqiNGNFCGLVLNQPLGGLHVIeGLPLLADSTDGMASVAAYTYRQ- 404
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361914 427 dghsHLVMYLGTTTGSLHKAVVSGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11273 405 ----HSVVFIGTRSGSLKKVRVDGFQDAHLYETVPVVDGSPILRDMVFSPDHRYIYLLSEKQVSQLP 467
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
75-493 1.73e-06

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


Pssm-ID: 200506 [Multi-domain]  Cd Length: 440  Bit Score: 51.09  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  75 TLYVGAREAILAL--DIQDPGV----PRLKNmiPWPASDRKKSECAfkkKSNETQCFNFIrVLVSYNVTHLYTCGTFaFS 148
Cdd:cd11245  13 RLYLGAVNGLFQLspNLQLESRadtgPKKDS--PQCLPPITAAECP---QAKETDNFNKL-LLVNSANGTLVVCGSL-FQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 149 PACTFIELQD-SYLLPISEDKvmegkGQSPFdPAHKHTAVLVDGMLYSGTMNNFL-------------GSEPILMRTL-- 212
Cdd:cd11245  86 GVCELRNLNSvNKPLYRPETP-----GDKQY-VAANEPSVSTVGLISYFKDGLSLlfvgrgytsslsgGIPPITTRLLqe 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 213 -GSQPV--------LKTDNFLRWLHHdasFVAAIPSTQVVYFFFEETASEFDffeRLHTSRVARVCKNDvggekllqKKW 283
Cdd:cd11245 160 hGEMDAfsneveakLVVGSASRYHHD---FVYAFADNGYIYFLFSRRPGTAD---STKRTYISRLCEND--------HHY 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 284 TTFLKAQLLCTQPGQLPFNVIRHAVLLPADSPTAPHI-YAVFTSQ--WQVGGTRSSAVCAFSLLDIERVFK--------G 352
Cdd:cd11245 226 YSYVELPLNCTVNQENTYNLVQAAYLAKPGKVLNGKVlFGVFSADeaSTAAPDGRSALCMYPLSSVDARFErtrescytG 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 353 KYKELNKETSRWTTY-------RGPETNPRPGSCSVG--PS---SDKALtfmkdhflmdeqvVGTPLLVKSgVEYTRLAV 420
Cdd:cd11245 306 EGLEDDKPETAYIEYnvksickTLPDKNVKAYPCGAEhtPSplaSRYPL-------------AAKPILTRN-DMLTAVAV 371
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361914 421 ETAQGldghsHLVMYLGTTTGSLHKaVVSGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVP 493
Cdd:cd11245 372 AVENG-----HTIAFLGDSGGQLHK-VYLDPNHTDFYSTIPGDQDSAVNKDLLFDSTLNHLYVMTGKKISKVP 438
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
260-528 7.75e-06

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: 49.13  E-value: 7.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 260 LHTSRVARVCKNDVGGEKLLqkkwttflkaqLLCTQPG-QLPFNVIRHAVLLPADSP-TAPHIYAVFTSQWqvGGTRSSA 337
Cdd:cd09295  14 IYVGAIARIYKVDGGGTRLL-----------LSCISPElNFGFNEDQKAFCPLRRGKwTECINYIKVLQQK--GDLDILA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 338 VCAFSLldiervFKGKYKELNKETsrwTTYRGPETNPRP-GSCSVGPSS-------DKALTFMKDHFLMDEQvvgTPLLV 409
Cdd:cd09295  81 VCGSNA------AQPSCGSYRLDV---LVELGKVRWPSGrPRCPIDNKHsnmgvnvDSKLYSATDHDFKDGD---RPALS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 410 K--SGVEYTRLAVETAQGLDGHSHLVMylgtttgslhkaVVSGDSsahlVEEIQLFPDPEPVRNLqlapTQGAVFVGFSG 487
Cdd:cd09295 149 RrsSNVHYLRIVVDSSTGLDEITFVYA------------FVSGDD----DDEVYFFFRQEPVEYL----KKGMVYVPRIA 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 21361914 488 GVWRVPRANCSVYESCVDCVLARDPHCAWDPESRTCCLLSA 528
Cdd:cd09295 209 RVCKLDVGGCHRLKKKLTSFLKADLNCSRPQSGFAFNLLQD 249
Sema_plexin_B3 cd11277
The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of ...
64-495 1.56e-05

The Sema domain, a protein interacting module, of Plexin B3; Plexin B3 is the receptor of semaphorin 5A. It is a highly potent stimulator of neurite outgrowth of primary murine cerebellar neurons. Plexin B3 has been linked to verbal performance and white matter volume in human brain. Furthermore, Sema5A and plexin B3 have been implicated in the progression of various types of cancer. They play an important role in the invasion and metastasis of gastric carcinoma. The stimulation of plexin B3 by Sema5A binding in human glioma cells results in the inhibition of cell migration and invasion. 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: 200538 [Multi-domain]  Cd Length: 434  Bit Score: 48.27  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914  64 FDTLLLSGDGNTLYVGAREAILAL--DIQDPGV----PRLKNMIPWPASDRKksECAFKKKSNETQCFnfirVLVSYNVT 137
Cdd:cd11277   8 FNHLALDPGSGTLYVGAVNRLYQLspDLQLLGEavtgPVLDSPDCLPFRDPA--DCPQARLTDNANKL----LLVSERAG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 138 HLYTCGTfAFSPACTFIELQD-SYLLPISEDKvmeGKGQ--SPFDP---------AHKHTAVLVDGMLYSGTMNNflGSE 205
Cdd:cd11277  82 ELVACGQ-VRQGVCEKRRLGNvAQVLYQAEDP---GDGQfvAANDPgvatvglvvEAPGRDLLLVGRGLTGKLSA--GIP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 206 PILMRTLGSQPVLKTDNFLRWLHHDAS-----FVAAIPSTQVVYFFFEETASEfdfFERLHTSRVARVCKNDVggekllq 280
Cdd:cd11277 156 PLTIRQLAGAQAFSSEGLGKLVVGDFSdynnsYVGAFAHNGYVYFLFRRRGAR---AQAEYRTYVARVCLGDT------- 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 281 kKWTTFLKAQLLCtQPGQlpfNVIRHAVLlpadSPTAPHIYAVFT-SQWQVGG-TRSSAVCAFSLLDIERVFkgkykeln 358
Cdd:cd11277 226 -NLYSYVEVPLVC-QGGY---NLAQAAYL----APGQGTLFVVFAaGQGSTPTpTDQTALCAYPLVELDSAM-------- 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361914 359 kETSRWTTY----RGPeTNPRPGSCSVGPSSdKALTFMKDHFLM----DEQ----------VVGTPLLvKSGVEYTRLAV 420
Cdd:cd11277 289 -ERARRLCYtaggGGP-NGKEEATIEYGVTS-RCVNLPKDSPESypcgDEHtpspiasrqpLEAEPLL-TLTPPLTAVAA 364
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361914 421 ETAQGldghsHLVMYLGTTTGSLHKAVVSGdSSAHLVEEIQLFPDPEPVRNLQLAPTQGA-VFVGFSGGVWRVPRA 495
Cdd:cd11277 365 LQEDG-----HTIAFLGDTQGQLHKVFLNG-SAGQVYSSQPVGPPGSAVNPDLLLDATGShLYVLTARQVTKVPVA 434
 
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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