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Conserved domains on  [gi|1863909954|ref|NP_001371829|]
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semaphorin-3D precursor [Homo sapiens]

Protein Classification

semaphorin-3( domain architecture ID 10181348)

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

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List of domain hits

Name Accession Description Interval E-value
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
61-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted semaphorin expressed during the development of the nervous system. In zebrafish, Sema3D is expressed in the ventral tectum. It guides retinal axons along the dorsoventral axis of the tectum and guides the laterality of retinal ganglion cell (RGC) projections. Both Sema3D knockdown or its ubiquitous overexpression induced aberrant ipsilateral projections. Proper balance of Sema3D is needed at the midline for the progression of RGC axons from the chiasm midline into the contralateral optic tract. Sema3D is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


:

Pssm-ID: 200513 [Multi-domain]  Cd Length: 474  Bit Score: 1056.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  61 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNK 140
Cdd:cd11252     1 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 141 THIYVCGTGAFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLG 220
Cdd:cd11252    81 THVYVCGTGAFHPTCGYIELGTHKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 221 PTHDHHYIRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKW 300
Cdd:cd11252   161 PTPDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 301 TTFLKARLICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESAD 380
Cdd:cd11252   241 TTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 381 HRWVQYDGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAE 460
Cdd:cd11252   321 HRWVQYEGRIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVAAE 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863909954 461 DGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11252   401 DGQYDVMFLGTDIGTVLKVVSITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
595-686 1.12e-48

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


:

Pssm-ID: 409455  Cd Length: 92  Bit Score: 166.37  E-value: 1.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 595 TADEKVIFGIEFNSTFLECIPKSQQATIKWYIQRSGDEHREELKPDERIIKTEYGLLIRSLQKKDSGMYYCKAQEHTFIH 674
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|..
gi 1863909954 675 TIVKLTLNVIEN 686
Cdd:cd05871    81 TLVKIRLHVIEP 92
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
533-570 2.33e-08

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 50.62  E-value: 2.33e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1863909954  533 RCDTYgKACADCCLARDPYCAWD--GNACSRYAPTSKRRA 570
Cdd:smart00423   1 RCSKY-TSCSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
 
Name Accession Description Interval E-value
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
61-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted semaphorin expressed during the development of the nervous system. In zebrafish, Sema3D is expressed in the ventral tectum. It guides retinal axons along the dorsoventral axis of the tectum and guides the laterality of retinal ganglion cell (RGC) projections. Both Sema3D knockdown or its ubiquitous overexpression induced aberrant ipsilateral projections. Proper balance of Sema3D is needed at the midline for the progression of RGC axons from the chiasm midline into the contralateral optic tract. Sema3D is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200513 [Multi-domain]  Cd Length: 474  Bit Score: 1056.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  61 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNK 140
Cdd:cd11252     1 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 141 THIYVCGTGAFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLG 220
Cdd:cd11252    81 THVYVCGTGAFHPTCGYIELGTHKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 221 PTHDHHYIRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKW 300
Cdd:cd11252   161 PTPDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 301 TTFLKARLICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESAD 380
Cdd:cd11252   241 TTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 381 HRWVQYDGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAE 460
Cdd:cd11252   321 HRWVQYEGRIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVAAE 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863909954 461 DGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11252   401 DGQYDVMFLGTDIGTVLKVVSITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema smart00630
semaphorin domain;
70-507 2.39e-165

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 483.02  E-value: 2.39e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954   70 FQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVCGTG 149
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  150 AFHPICGYIDLGvykediifkldthnlesgrlkcpfdpqqpfasvmtdeYLYSGTASDFLGKDTAFTRSLGPTHDH---- 225
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRLKgtsg 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  226 HYIRTDISEHYWLNGAKFIGTFfipdtynPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLK 305
Cdd:smart00630 124 VSLRTVLYDSKWLNEPNFVYAF-------ESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLK 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  306 ARLICSIPGSDGadTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQ 385
Cdd:smart00630 197 ARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  386 Y-DGRIPYPRPGTCPSKTYdplikSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHViAEDGQY 464
Cdd:smart00630 275 YsRGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNY 348
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1863909954  465 DVMFLGTDIGTVLKVVSISKEKWNmEEVVLEELQIFKHSSIIL 507
Cdd:smart00630 349 TVLFLGTSDGRILKVVLSESSSSS-ESVVLEEISVFPDGSPIS 390
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
325-512 1.09e-78

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: 250.65  E-value: 1.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 325 LQDIYLLP--TRDERNPVVYGVFTTT-SSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYDGRIPYPRPGTCPSK 401
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 402 TYdpliksTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRinVDYRLTQIVVDHVIAEDGQYDVMFLGTDIGTVLKVVS 481
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVR--TGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1863909954 482 ISKEkwnmEEVVLEELQIFKHSSIILNMELS 512
Cdd:pfam01403 153 VGSE----ESHIIEEIQVFPEPQPVLNLLLS 179
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
595-686 1.12e-48

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


Pssm-ID: 409455  Cd Length: 92  Bit Score: 166.37  E-value: 1.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 595 TADEKVIFGIEFNSTFLECIPKSQQATIKWYIQRSGDEHREELKPDERIIKTEYGLLIRSLQKKDSGMYYCKAQEHTFIH 674
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|..
gi 1863909954 675 TIVKLTLNVIEN 686
Cdd:cd05871    81 TLVKIRLHVIEP 92
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
533-570 2.33e-08

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 50.62  E-value: 2.33e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1863909954  533 RCDTYgKACADCCLARDPYCAWD--GNACSRYAPTSKRRA 570
Cdd:smart00423   1 RCSKY-TSCSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
533-561 9.98e-04

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 37.69  E-value: 9.98e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1863909954 533 RCDTYGkACADCCLARDPYCAWD--GNACSR 561
Cdd:pfam01437   1 RCSQYT-SCSSCLAARDPYCGWCssEGRCVR 30
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
611-680 1.31e-03

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 38.26  E-value: 1.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863909954  611 LECIPKSQ-QATIKWYIQRsgdehREELKPDERIIKTEYG----LLIRSLQKKDSGMYYCKAQ-EHTFIHTIVKLT 680
Cdd:smart00410  14 LSCEASGSpPPEVTWYKQG-----GKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATnSSGSASSGTTLT 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
611-667 3.15e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.16  E-value: 3.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1863909954 611 LEC-IPKSQQATIKWYiqRSGDEHREELKPDERIIKTEYGLLIRSLQKKDSGMYYCKA 667
Cdd:pfam13927  21 LTCeATGSPPPTITWY--KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
 
Name Accession Description Interval E-value
Sema_3D cd11252
The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted ...
61-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3D (Sema3D); Sema3D is a secreted semaphorin expressed during the development of the nervous system. In zebrafish, Sema3D is expressed in the ventral tectum. It guides retinal axons along the dorsoventral axis of the tectum and guides the laterality of retinal ganglion cell (RGC) projections. Both Sema3D knockdown or its ubiquitous overexpression induced aberrant ipsilateral projections. Proper balance of Sema3D is needed at the midline for the progression of RGC axons from the chiasm midline into the contralateral optic tract. Sema3D is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200513 [Multi-domain]  Cd Length: 474  Bit Score: 1056.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  61 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNK 140
Cdd:cd11252     1 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIYLLDLVDLNKNPKKIYWPAAKERVELCKLAGKDANTECANFIRVLHPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 141 THIYVCGTGAFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLG 220
Cdd:cd11252    81 THVYVCGTGAFHPTCGYIELGTHKEDRIFLLDTQNLESGRLKCPFDPQQPFASVMTDEYLYAGTASDFLGKDTTFTRSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 221 PTHDHHYIRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKW 300
Cdd:cd11252   161 PTPDHHYIRTDISEHYWLNGAKFIGTFPIPDTYNPDDDKIYFFFREASQDGSTSDKSVLSRVGRVCKNDVGGQRSLINKW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 301 TTFLKARLICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESAD 380
Cdd:cd11252   241 TTFLKARLVCSIPGPDGADTHFDELQDIFLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESPD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 381 HRWVQYDGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAE 460
Cdd:cd11252   321 HRWVQYEGRIPYPRPGTCPSKTYDPLIKSTKDFPDEVISFIKRHPLMYKSVYPLTGGPVFTRINVDYRLTQIVVDHVAAE 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863909954 461 DGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11252   401 DGQYDVMFLGTDIGTVLKVVSITKEKWTMEEVVLEELQIFKHPSPILNMELSLKQQQLYIGSRDGLVQLSLHRC 474
Sema_3 cd11239
The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins ...
61-534 0e+00

The Sema domain, a protein interacting module, of class 3 semaphorins; Class 3 semaphorins (Sema3s) are secreted regulator molecules involved in the development of the nervous system, vasculogenesis, angiogenesis,and tumorigenesis. There are 7 distinct subfamilies named Sema3A to 3G. Sema3s function as repellent signals during axon guidance by repelling neurons away from the source of Sema3s. However, Sema3s that are secreted by tumor cells play an inhibitory role in tumor growth and angiogenesis (specifically Sema3B and Sema3F). Sema3s functions by forming complexes with neuropilins and A-type plexins, where neuropilins serve as the ligand binding moiety and the plexins function as signal transduction component. Sema3s primarily inhibit the cell motility and migration of tumor and endothelial cells by inducing collapse of the actin cytoskeleton via neuropilins and plexins. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200500 [Multi-domain]  Cd Length: 471  Bit Score: 941.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  61 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNK 140
Cdd:cd11239     1 FLGSMNSLDYRSLLLDEDRDRLYVGGKDHILSLSLDNINQDPKKIYWPASPERIEECKMAGKDPNTECANFVRVLQPYNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 141 THIYVCGTGAFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLG 220
Cdd:cd11239    81 THLYACGTGAFHPICAFINVGRRLEDPIFKLDDSSLESGRGKCPFDPNQPFASVLIDGELYSGTAIDFMGRDAAIFRSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 221 PthdHHYIRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKW 300
Cdd:cd11239   161 H---RHYIRTEQYDSRWLNEPKFVGAYLIPDSDNPDDDKVYFFFREKAVEAEGSGKAIYSRVGRICKNDVGGQRSLVNKW 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 301 TTFLKARLICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESAD 380
Cdd:cd11239   238 STFLKARLVCSVPGPDGIDTYFDELEDVFLLPTRDPKNPLIYGVFTTSSNVFKGSAVCVYSMADIRAAFNGPFAHKEGPN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 381 HRWVQYDGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAE 460
Cdd:cd11239   318 YQWVEYQGKVPYPRPGTCPSKTYGPLYKSTKDFPDDVISFARSHPLMYNPVYPLHGRPLLIRTNVPYRLTQIAVDRVEAE 397
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863909954 461 DGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11239   398 DGQYDVLFIGTDSGTVLKVVSLPKENWEMEEVILEELQVFKHPSPITSMEISSKRQQLYVGSAEGVVQLPLHRC 471
Sema_3A cd11249
The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been ...
39-535 0e+00

The Sema domain, a protein interacting module, of semaphorin 3A (Sema3A); Sema3A has been reported to inhibit the growth of certain experimental tumors and to regulate endothelial cell migration and apoptosis in vitro, as well as arteriogenesis in the muscle, skin vessel permeability, and tumor angiogenesis in vivo. The function of Sema3A is mediated through receptors neuropilin-1 (NP1) and plexins, although little is known about the requirement of specific plexins in its receptor complex. It is known however that Plexin-A4 is the receptor for Sema3A in the Toll-like receptor- and sepsis-induced cytokine storm during immune response. Sema3A is a member of the Class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200510 [Multi-domain]  Cd Length: 493  Bit Score: 700.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  39 KQNIPRLKLTYKDLLLSNSCIPFLGSSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDLnKNFKKIYWPAAKERVELCK 118
Cdd:cd11249     1 KNNVPRLKLSYKEMLESNNLITFNGLANSSSYHTFLLDEERGRLYVGAKDHIFSFNLVNI-KDFQKIVWPVSPSRRDECK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 119 LAGKDANTECANFIRVLQPYNKTHIYVCGTGAFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDE 198
Cdd:cd11249    80 WAGKDILKECANFIKVLKAYNQTHLYACGTGAFHPVCTYIEVGHHPEDNIFRLEDSHFENGRGKSPYDPKLLTASLLIDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 199 YLYSGTASDFLGKDTAFTRSLGpthDHHYIRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTI 278
Cdd:cd11249   160 ELYSGTAADFMGRDFAIFRTLG---HHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKIYFFFRENAIDGEHTGKAT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 279 LSRVGRVCKNDVGGQRSLINKWTTFLKARLICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVC 358
Cdd:cd11249   237 HARIGQLCKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYAVFTTSSNIFKGSAVC 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 359 VYSMADIRAVFNGPYAHKESADHRWVQYDGRIPYPRPGTCPSKTYDPLiKSTRDFPDDVISFIKRHSVMYKSVYPVAGGP 438
Cdd:cd11249   317 MYSMTDIRRVFLGPYAHRDGPNYQWVPFQGRVPYPRPGTCPSKTFGGF-DSTKDLPDDVITFARSHPAMYNPVFPINNRP 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 439 TFKRINVDYRLTQIVVDHVIAEDGQYDVMFLGTDIGTVLKVVSISKEKW-NMEEVVLEELQIFKHSSIILNMELSLKQQQ 517
Cdd:cd11249   396 IIIKTDVDYQFTQIVVDRVEAEDGQYDVMFIGTDMGTVLKVVSIPKETWhDLEEVLLEEMTVFREPTAISAMELSTKQQQ 475
                         490
                  ....*....|....*...
gi 1863909954 518 LYIGSRDGLVQLSLHRCD 535
Cdd:cd11249   476 LYIGSAIGVSQLPLHRCD 493
Sema_3B cd11250
The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is ...
70-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3B (Sema3B); Sema3B is coexpressed with semaphorin 3F and both proteins are candidate tumor suppressors. Both Sema3B and Sema3F show high levels of expression in normal tissues and low-grade tumors but are down-regulated in highly metastatic tumors in the lung, melanoma cells, bladder carcinoma cells and prostate carcinoma. They are upregulated by estrogen and inhibit cell motility and invasiveness through decreased FAK phosphorylation and inhibition of MMP-2 and MMP-9 expression. Two receptor families, the neuropilins (NP) and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3B is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200511 [Multi-domain]  Cd Length: 471  Bit Score: 659.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  70 FQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVCGTG 149
Cdd:cd11250    10 YDALLLDEERGRLFVGAKNYLASLSLDNISKQEKKIYWPAPVEWREECNWAGKDINTDCMNYVKILHHYNRTHLYACGTG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 150 AFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLG--PThdhhy 227
Cdd:cd11250    90 AFHPTCAFVEVGQRMEDHVFRLDPSRVEDGKGKSPYDPRHTAASVLVGDELYSGVATDLMGRDFTIFRSLGqrPS----- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 228 IRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLKAR 307
Cdd:cd11250   165 LRTEQHDSRWLNEPKFVKVFWIPESENPDDDKIYFFFRETAVEAAGLGKQSYSRIGQICRNDMGGQRSLVNKWTTFLKAR 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 308 LICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYD 387
Cdd:cd11250   245 LVCSVPGNEGGDTHFDELRDVFLLQTRDKRNPLIYAVFSTSSSVFQGSAVCVYTMNDVRRAFLGPFAHKEGPNYQWVSYQ 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 388 GRIPYPRPGTCPSKTYDPLiKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAEDGQYDVM 467
Cdd:cd11250   325 GKVPYPRPGMCPSKTFGSF-ESTKDFPDDVIQFARNHPLMFNPVLPLGGRPLFLRTGIPYTFTQIAVDRVAAADGHYDVM 403
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863909954 468 FLGTDIGTVLKVVSISKEKW-NMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11250   404 FIGTDVGSVLKVISVPKGSWpSNEELLLEELHVFKDSSPITSMQISSKRQQLYVGSRSGVSQLPLHRC 471
Sema_3F cd11254
The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is ...
69-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3F (Sema3F); Sema3F is coexpressed with semaphorin3B. Both Sema3B and Sema3F proteins are candidate tumor suppressors that are down-regulated in highly metastatic tumors. Two receptor families, the neuropilins and plexins, have been implicated in mediating the actions of semaphorins 3B and 3F. Sema3F is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200515 [Multi-domain]  Cd Length: 470  Bit Score: 625.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVCGT 148
Cdd:cd11254     9 DYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWPASPQRIEECILSGKGSNGECGNFIRLIQPWNRTHLYVCGT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 149 GAFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGPthdHHYI 228
Cdd:cd11254    89 GAYNPVCAYINRGRRAEDYMFRLEPDKLESGKGKCPYDPKQDSVSALINGELYAGVYIDFMGTDAAIFRTMGK---QPAM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 229 RTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSdKTILSRVGRVCKNDVGGQRSLINKWTTFLKARL 308
Cdd:cd11254   166 RTDQYNSRWLNDPAFVHAHLIPDSSEKNDDKLYFFFREKSLEAPQS-PAVLSRIGRVCLNDDGGHCCLVNKWSTFLKARL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 309 ICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYDG 388
Cdd:cd11254   245 VCSVPGADGIETHFDELRDVFIQPTQDTKNPVIYAVFSTSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPYTG 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 389 RIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAEDGQYDVMF 468
Cdd:cd11254   325 KIPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYNAVYPVHRRPLVVRTNVNYRFTTIAVDQVDAADGRYEVLF 404
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863909954 469 LGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11254   405 LGTDRGTVQKVIVLPKDDLETEELTLEEVEVFKVPAPIKTMKISSKRQQLYVSSAVGVTHLSLHRC 470
Sema_3G cd11255
The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is ...
61-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3G (Sema3G); Semaphorin 3G is identified as a primarily endothelial cell- expressed class 3 semaphorin that controls endothelial and smooth muscle cell functions in autocrine and paracrine manners, respectively. It is mainly expressed in the lung and kidney, and a little in the brain. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200516 [Multi-domain]  Cd Length: 474  Bit Score: 584.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  61 FLGSSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNK 140
Cdd:cd11255     1 FLGLHGDLHLSAVYLDEYRDRLFLGGKDVLYSLRLDQTHPDAKEIHWPPLPGQREECIRKGKDPETECANFVRVLQPFNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 141 THIYVCGTGAFHPICGYIDLGvYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLG 220
Cdd:cd11255    81 THLLACGTGAFQPVCALINVG-HRGEHVFSLDPTTVESGRGRCPHEPKRPFASTFTGGELYTGLTADFLGRDSVIFRGFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 221 PTHDhhyIRTDiSEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQE-GSTSDKTILSRVGRVCKNDVGGQRSLINK 299
Cdd:cd11255   160 TRSP---LRTE-TDQRLLHEPRFVAAHLIPDNADRDNDKVYFFFTERATEtAEDDDGAIHSRVGRLCANDAGGQRVLVNK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 300 WTTFLKARLICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESA 379
Cdd:cd11255   236 WSTFIKARLVCSVPGPHGIQTHFDQLEDVFLLRTKDGKSPEIYALFSTISNVFQGFAVCVYSMADIWEVFNGPFAHKDGP 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 380 DHRWVQYDGRIPYPRPGTCPSK-TYDP--LIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDH 456
Cdd:cd11255   316 DHQWGPYEGKVPYPRPGVCPSKiTAQPgrAFRSTKDYPDEVLQFARAHPLMWRPVYPSHRRPVLVKTGLPYRLTQIVVDR 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863909954 457 VIAEDGQYDVMFLGTDIGTVLKVVSISKEKW-NMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11255   396 VEAEDGYYDVMFIGTDSGSVLKVIVLQKGNSaAGEEVTLEELQVFKVPTPITEMEISVKRQMLYVGSRTGVAQVPLHRC 474
Sema_3C cd11251
The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted ...
64-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3C (Sema3C); Sema3C is a secreted semaphorin expressed in and adjacent to cardiac neural crest cells, and causes impaired migration of neural crest cells to the developing cardiac outflow tract, resulting in the interruption of the aortic arch and persistent truncus arteriosus. It has been proposed that Sema3C acts as a guidance molecule, regulating migration of neural crest cells that express semaphorin receptors such as plexin A2. Sema3C may also participate in tumor progression. The cleavage of Sema3C induced by ADAMTS1 promotes the migration of breast cancer cells. Sema3C is a member of the class 3 semaphorin family of secreted proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200512 [Multi-domain]  Cd Length: 470  Bit Score: 571.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  64 SSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHI 143
Cdd:cd11251     4 SERPLDYRILFMDEDQDRIYVGSKDHILSLNINNISQDALSIFWPASASKVEECKMAGKDPTHGCGNFVRVIQPYNRTHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 144 YVCGTGAFHPICGYIDLGVYKEDIIFKLDTHNlESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGpth 223
Cdd:cd11251    84 YVCGSGAFSPVCVYVNRGRRSEEQVFHIDSKA-ESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLT--- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 224 DHHYIRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTF 303
Cdd:cd11251   160 KRNAVRTDQHNSKWLSEPIFVDAHLIPDGTDPNDAKLYFFLKERLTDNSGSTKQIHSMIARVCPNDTGGQRSLVNKWTTF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 304 LKARLICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRW 383
Cdd:cd11251   240 LKARLVCSVMDEDGTETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHMSDIQTVFNGPFAHKEGPNHQL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 384 VQYDGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAEDGQ 463
Cdd:cd11251   320 IAYQGRIPYPRPGTCPGGAFTPNMQSTKEFPDDVVTFIRNHPLMFNPIYPIGRRPLLVRTGTDYKYTKIAVDRVNAADGR 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863909954 464 YDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11251   400 YHVLFLGTDKGTVQKVVVLPTNGSLSGELILEELEVFKNHAPITNMKISSKKQQLYVSSEEGISQVSLHRC 470
Sema_3E cd11253
The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted ...
68-534 0e+00

The Sema domain, a protein interacting module, of semaphorin 3E (Sema3E); Sema3E is a secreted molecule implicated in axonal path finding and inhibition of developmental and postischemic angiogenesis. It is also highly expressed in metastatic cancer cells. Sema3E signaling, through its high affinity functional receptor Plexin D1, drives cancer cell invasiveness and metastatic spreading. Sema3E is a member of the class 3 semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200514 [Multi-domain]  Cd Length: 471  Bit Score: 568.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  68 LDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANtECANFIRVLQPYNKTHIYVCG 147
Cdd:cd11253     8 LDLHTMLLDEYQERLFVGGRDLLYSLSLERISANYKEIHWPSTQLQVEDCIMKGRDKP-ECANYIRVLHHYNRTHLLACG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 148 TGAFHPICGYIDLGVYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGptHDHHy 227
Cdd:cd11253    87 TGAFDPVCAFIRVGRGSEDHLFQLESDKFERGRGRCPFDPNSSFISTLIGGELFVGLYSDYWGRDAAIFRTMN--HLAH- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 228 IRTDISEHYWLNGAKFIGTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLKAR 307
Cdd:cd11253   164 IRTEHDDERLLKEPKFVGSYMIPDNEDPDDNKVYFFFTEKALEAEGGNHAIYTRVGRVCANDQGGQRMLVNKWSTFLKTR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 308 LICSIPGSDGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYD 387
Cdd:cd11253   244 LICSVPGPNGIDTHFDELEDVFLLRTRDNKNPEIFGLFSTTSNIFKGYAICVYHMASIRAAFNGPFAHKEGPEYHWSVYE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 388 GRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAEDGQYDVM 467
Cdd:cd11253   324 GKVPYPRPGSCASKVNGGHYGTTKDYPDEALRFARSHPLMYQAVKPVHKRPILVKTDGKYNLKQIAVDRVEAEDGQYDVL 403
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863909954 468 FLGTDIGTVLKVVSI-SKEKWNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11253   404 FIGTDNGIVLKVITIyNQETETMEEVILEELQVFKVPVPIISMEISSKRQQLYIGSESGVAQIRFHQC 471
Sema_semaphorin cd11235
The Sema domain, a protein interacting module, of semaphorins; Semaphorins are regulator ...
68-532 2.07e-170

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: 497.70  E-value: 2.07e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  68 LDFQTLLLDEERGRLLLGAKDHIFLLSLVDLnKNFKKIYWPAAKERVELCKLAGKDAnTECANFIRVLQPYNKTHIYVCG 147
Cdd:cd11235     1 LKYHTKLLHEDRSTLYVGARDRVYLVDLDSL-YTEQKVAWPSSPDDVDTCYLKGKSK-DDCRNFIKVLEKNSDDSLLVCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 148 TGAFHPICGYIDLGVykediiFKLDTHNlESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGpthDHHY 227
Cdd:cd11235    79 TNAFNPSCRNYNVET------FELVGKE-ESGRGKCPYDPDHNSTALFADGELYSGTSADFLGTDPVIYRTLG---HNPP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 228 IRTDISEHYWLNGAKFIGTFFIPDtynpdddKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLKAR 307
Cdd:cd11235   149 LRTEYHDSKWLNEPQFVGAFDIGD-------YVYFFFREIAVEYINCGKAVYSRVARVCKNDQGGSRSLEKKWTTFLKAR 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 308 LICSIPGSDgaDTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQY- 386
Cdd:cd11235   222 LNCSVPGEF--PFYFNELQDVFDLPSPSNKEKIFYAVFTTPYNSIPGSAVCAYSLSDIEAVFNGPFKEQHSSNSAWLPVp 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 387 DGRIPYPRPGTCpsktydplIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAEDGQ-YD 465
Cdd:cd11235   300 DERVPEPRPGTC--------VDDSSPLPDDTLNFIKSHPLMDEAVTPILNRPLFIKTDVNYRFTKIAVDRVQAKLGQtYD 371
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863909954 466 VMFLGTDIGTVLKVVSISKEKWNmEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSLH 532
Cdd:cd11235   372 VLFVGTDRGIILKVVSLPEQGLQ-ASNILEEMPVGPPPEPIQTMQLSRKRRSLYVGSETGVLQVPLA 437
Sema smart00630
semaphorin domain;
70-507 2.39e-165

semaphorin domain;


Pssm-ID: 214747 [Multi-domain]  Cd Length: 390  Bit Score: 483.02  E-value: 2.39e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954   70 FQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVCGTG 149
Cdd:smart00630   1 LQHLLLDEDNGTLYVGARNRLYQLSLNLILEAELKTGPVLSSPDCEECVSKGKDPPTDCVNYIRLLLDYNEDRLLVCGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  150 AFHPICGYIDLGvykediifkldthnlesgrlkcpfdpqqpfasvmtdeYLYSGTASDFLGKDTAFTRSLGPTHDH---- 225
Cdd:smart00630  81 AFQPVCRLRNLG-------------------------------------ELYVGTVADFSGSDPAIPRSLSVRRLKgtsg 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  226 HYIRTDISEHYWLNGAKFIGTFfipdtynPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLK 305
Cdd:smart00630 124 VSLRTVLYDSKWLNEPNFVYAF-------ESGDFVYFFFRETAVEDDNCGKAVHSRVARVCKNDVGGPRSLDKKWTSFLK 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  306 ARLICSIPGSDGadTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQ 385
Cdd:smart00630 197 ARLECSVPGEDP--FYFNELQAAFLLPPGSESDDVLYGVFSTSSNPIPGSAVCAFSLSDINAVFNGPFKECETSTSQWLP 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  386 Y-DGRIPYPRPGTCPSKTYdplikSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHViAEDGQY 464
Cdd:smart00630 275 YsRGKVPYPRPGTCPNKPP-----SSKDLPDETLNFIKSHPLMDEVVQPLTGRPLFVKTDSNYLLTSIAVDRV-ATDGNY 348
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1863909954  465 DVMFLGTDIGTVLKVVSISKEKWNmEEVVLEELQIFKHSSIIL 507
Cdd:smart00630 349 TVLFLGTSDGRILKVVLSESSSSS-ESVVLEEISVFPDGSPIS 390
Sema_4 cd11240
The Sema domain, a protein interacting module, of class 4 semaphorins (Sema4); Class 4 ...
64-531 1.10e-156

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: 463.42  E-value: 1.10e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  64 SSEGL-DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFK-KIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKT 141
Cdd:cd11240     2 SQEGIqNYSTLLLSEDEGTLYVGAREALFALNVSDISTELKdKIKWEASEDKKKECANKGKDNQTDCFNFIRILQFYNST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 142 HIYVCGTGAFHPICGYIDLgvykEDiiFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGp 221
Cdd:cd11240    82 HLYVCGTFAFSPRCTYINL----SD--FSLSSIKFEDGKGRCPFDPAQRYTAIMVDGELYSATVNNFLGSEPVISRNHS- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 222 thDHHYIRTDISEhYWLNGAKFIGTFFIP---DTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLIN 298
Cdd:cd11240   155 --EGNVLKTENTL-RWLNEPAFVGSAHIResiDSPDGDDDKIYFFFTETAVEYDFYEKVTVSRVARVCKGDLGGQRTLQK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 299 KWTTFLKARLICSIPGSdgaDTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKES 378
Cdd:cd11240   232 KWTTFLKAQLVCSQPDS---GLPFNVLRDVFVLSPDSWDATIFYGVFTSQWNVSGLSAVCAYSLEDIKKVFSGKYKEFNR 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 379 ADHRWVQYDGRIPYPRPGTC-PSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRiNVDYrlTQIVVDHV 457
Cdd:cd11240   309 ETSKWSRYTGPVPDPRPGACiTNSARSQGITSSLNLPDNVLTFVKDHPLMDEQVHPINRPLLVKS-GVNY--TRIAVHRV 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863909954 458 IAEDGQ-YDVMFLGTDIGTVLKVVSISKEKwnmeeVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11240   386 QALDGQtYTVLFLGTEDGFLHKAVSLDGGM-----HIIEEIQLFDQPQPVKNLLLSSSKGVLYVGSSSGVVQVPL 455
Sema_4G cd11262
The Sema domain, a protein interacting module, of semaphorin 4G (Sema4G); The Sema4G and ...
64-531 3.12e-130

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: 395.28  E-value: 3.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  64 SSEGLDFQTLLLDEERGRLLLGAKDHIFLLSLVDL-NKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTH 142
Cdd:cd11262     4 RGPAQNYSTLLLEDESGRLYVGARGAIFSLNASDIsDSSALTIDWEASPEQKHQCLKKGKNNQTECFNHVRFLQRFNSTH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 143 IYVCGTGAFHPICGYIDlgvyKEDiiFKLDTHnLESGRLKCPFDPQQPFASVMTDEYLYsgTASDFLGKDTAFTRSLGPT 222
Cdd:cd11262    84 LYTCGTHAFRPLCAYID----AER--FTLSSQ-FEEGKEKCPYDPAKGYTGLIVDGQLY--TASQYEFRSFPDIRRNSPQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 223 HDhhyIRTDISEHYWLNGAKFIGTFFIPDTYNP---DDDKIYFFFRESSQEGSTS-DKTILSRVGRVCKNDVGGQRSLIN 298
Cdd:cd11262   155 PT---LRTEEAPTRWLNDADFVGSVLVRESMNSsvgDDDKIYFFFTERSQEETAYfSQSRVARVARVCKGDRGGKKTLQR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 299 KWTTFLKARLICSIPGSdgaDTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKES 378
Cdd:cd11262   232 KWTSFLKARLVCYIPEY---EFLFNVLRSVFVLWGSTPQDTVFYGIFGLEWKNVKASAICRYSLSDIQTAFEGPYMEYQD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 379 ADHRWVQYDGRIPYPRPGTCPSKTY-DPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYrlTQIVVDHV 457
Cdd:cd11262   309 SSSKWSRYTGKVPEPRPGSCITDEHrSQGINSSQDLPDNVLDFVRRHPLMAEQVLPVEGRPLLFKRNVIY--TKIAVQTV 386
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863909954 458 IAEDGQ-YDVMFLGTDIGTVLKVVSISKEKWnmeevVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11262   387 RGLDGRvYDVLFLGTDEGWLHKAVVIGSAVH-----IIEELQVFREPQPVENLVISKKQNSLYVGARSGVVQVPL 456
Sema_4D cd11259
The Sema domain, a protein interacting module, of semaphorin 4D (Sema4D, also known as CD100); ...
69-528 1.26e-116

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: 360.71  E-value: 1.26e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVCGT 148
Cdd:cd11259    19 NYSTLLLSEDKDVLYVGAREAVFALNALNISEKQHELYWKVSEDKRTKCAVKGKSKQTECRNYIRVLQPLNDTFLYVCGT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 149 GAFHPICGYIDLgvykedIIFKLDTHNlESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLgpthDHHYI 228
Cdd:cd11259    99 NAFQPTCDYLNL------TSFRLLGKN-EDGKGRCPFDPAQSYTSVMVDGELYSGTSYNFLGSEPIISRNS----SQSPL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 229 RTDISEHyWLNGAKFIGTFFI---PDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLK 305
Cdd:cd11259   168 RTEYAIP-WLNEPSFVFADVIradPDSPDGEDDKIYFFFTEVSVEYEFVGKLLIPRIARVCKGDQGGLRTLQKKWTSFLK 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 306 ARLICSIPGSdgaDTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFN-GPYAHK---ESADH 381
Cdd:cd11259   247 ARLICSIPDK---NLVFNVVNDVFILKSPTLKEPVIYGVFTPQLNNVGLSAVCAYNLSTVEEVFSkGKYMQSatvEQSHT 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 382 RWVQYDGRIPYPRPGTCPSKTYDPL-IKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYrlTQIVVDHVIAE 460
Cdd:cd11259   324 KWVRYNGEVPKPRPGACINNEARAAnYTSSLNLPDKTLQFVKDHPLMDDSVTPIGNRPRLIKKDVNY--TQIVVDRVQAL 401
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1863909954 461 DGQ-YDVMFLGTDIGTVLKVVSISKEKWnmeevVLEELQIFKHSSIILNMELSLKQQQ--LYIGSRDGLVQ 528
Cdd:cd11259   402 DGTiYDVMFISTDRGALHKAISLENEVH-----IIEETQLFPDFEPVQTLLLSSKKGRrfLYAGSNSGVVQ 467
Sema_1A cd11237
The Sema domain, a protein interacting module, of semaphorin 1A (Sema1A); Sema1A is a ...
70-534 1.59e-115

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: 356.64  E-value: 1.59e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  70 FQTLLLDEERgrLLLGAKDHIFLLSLVDLNKNfKKIYWPAAKERVELCKLAGKDaNTECANFIRVLQPYNKTHIYVCGTG 149
Cdd:cd11237     7 FKLLDQDGNS--LLVGARNAVYNISLSDLTEN-QRIEWPSSDAHREMCLLKGKS-EDDCQNYIRVLAKKSAGRLLVCGTN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 150 AFHPICGYIDLGVYKEDIIFKLDthnlesGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRslGPthdhhyIR 229
Cdd:cd11237    83 AYKPLCREYTVKDGGYRVEREFD------GQGLCPYDPKHNSTAVYADGQLYSATVADFSGADPLIYR--EP------LR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 230 TDISEHYWLNGAKFIGTFfipdTYNpddDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLKARLI 309
Cdd:cd11237   149 TERYDLKQLNAPNFVSSF----AYG---DYVYFFFRETAVEYINCGKAIYSRVARVCKNDKGGPHPFRDRWTSFLKARLN 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 310 CSIPGsdgaDT--YFDELQDIY-LLPTRD--ERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWV 384
Cdd:cd11237   222 CSVPG----EYpfYFNEIQSTSdIVEGGYggKSAKLIYGVFTTPVNSISGSAVCAFSLQDILEVFDGSFKEQQDINSNWL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 385 QY-DGRIPYPRPGTCpsktydplIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVD-HVIAEDG 462
Cdd:cd11237   298 PVpSNKVPEPRPGQC--------VNDSRTLPDVTVNFIKSHPLMDEAVPSFFGRPILVRTSLQYRFTQIAVDpQVKALDG 369
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863909954 463 Q-YDVMFLGTDIGTVLKVVSISK--EKWNMEEVVLEELQIFKHSSIILNMEL--SLKQQQLYIGSRDGLVQLSLHRC 534
Cdd:cd11237   370 KyYDVLFIGTDDGKVLKAVNIASadTVDKVSPVVIEETQVFPRGVPIRNLLIvrGKDDGRLVVVSDDEIVSIPLHRC 446
Sema_4E cd11260
The Sema domain, a protein interacting module, of semaphorin 4E (Sema4E); Sema4E is expressed ...
69-531 3.60e-112

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: 348.43  E-value: 3.60e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVCGT 148
Cdd:cd11260     8 NYSTMLLREDLGLLVLGAREAVFALDLNDISVKRAKVLWEVTEEKQKDCTNKGKHADIDCHNYIRILHKMNDSRMYVCGT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 149 GAFHPICGYIDlgvYKEDiifKLDTH-NLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGPThdhhy 227
Cdd:cd11260    88 NAFSPTCDYIS---YDDG---QLTLEgKQEDGKGKCPFDPFQRYSSVMVDQDLYSATSMNFLGSEPVIMRSSPIT----- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 228 IRTDISEHyWLNGAKFIGTFFIPDTY-NP--DDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFL 304
Cdd:cd11260   157 IRTEFKSS-WLNEPNFIYMAAVPESEdSPegDDDKIYLFFSETAVEYDFYNKLVVSRVARVCKGDLGGQRTLQKKWTSFL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 305 KARLICSIPGSDGAdtYFdeLQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFN-GPYAHK---ESAD 380
Cdd:cd11260   236 KARLDCSVPEPSLP--YV--IQDVFHVCHQDWRKCVFYAVFTSQSDSSQSSAVCAYNVTDISNVFSrGKFKTPvavETSF 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 381 HRWVQYDGRIPYPRPGTC-PSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVdyRLTQIVVDHVIA 459
Cdd:cd11260   312 VKWVMYSGELPVPRPGACiNNAARTSGIKKSLNLPDKTLQFVKDKPLMDQAVHPITGKPLLVKRGA--LFTRIVVDMVTA 389
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863909954 460 EDGQ-YDVMFLGTDIGTVLKVVSiskekWNMEEVVLEELQIFKHSSIILNMELSlkQQQLYIGSRDGLVQLSL 531
Cdd:cd11260   390 ADGQsYPVMFIGTANGYVLKAVN-----YDGEMHIIEEVQLFEPEEPIDILRLS--QNQLYAGSASGVVQMPV 455
Sema_4C cd11258
The Sema domain, a protein interacting module, of semaphorin 4C (Sema4C); Sema4C acts as a ...
69-531 9.65e-112

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: 347.56  E-value: 9.65e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNfKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVCGT 148
Cdd:cd11258    11 NYTTLTLAEHRGLLYVGAREAIFALSLSNIELQ-PPISWEAPAEKKTECAQKGKSNQTECFNYIRFLQPYNQSHLYTCGT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 149 GAFHPICGYIDLGVykediiFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGPthdHHYI 228
Cdd:cd11258    90 YAFQPKCAYINMLT------FTLDRAEFEDGKGKCPYDPAKGHTGLIVDGELYSATLNNFLGTEPVILRNLGQ---HYSM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 229 RTdisEH--YWLNGAKFIGTFFIPDT---YNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTF 303
Cdd:cd11258   161 KT---EYlaFWLNEPHFVGSAFVPESvgsFTGDDDKIYFFFSERAVEYDCDSEQVVARVARVCKGDLGGARTLQKKWTTF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 304 LKARLICSIPgsdGADTYFDELQDIYLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRW 383
Cdd:cd11258   238 LKARLLCSIP---EWQLYFNQLKAVFTLEGASWRNTTFFAVFQARWGDMDVSAVCEYQLGEIQQVFEGPYKEYSEQAQKW 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 384 VQYDGRIPYPRPGTCPSKTY-DPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDyrLTQIVVDHVIAEDG 462
Cdd:cd11258   315 GRYTDPVPSPRPGSCINNWHrDHGYTSSLELPDNTLNFVKKHPLMEDRVKPRLGRPLLVPCNSN--FTHVVWTRVLGLDG 392
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 463 Q-YDVMFLGTDIGTVLKVVSISKEKWnmeevVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11258   393 EtYSVLFIGTLDGWLIKAVSLGSWVH-----MIEELQVFDQEPPESLVVSQSSKKLLFAGSRSELLQLPW 457
Sema_4B cd11257
The Sema domain, a protein interacting module, of semaphorin 4B (Sema4B); Sema4B, expressed in ...
69-531 2.48e-103

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: 325.66  E-value: 2.48e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKN--FKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVC 146
Cdd:cd11257     9 NYTALLLSKDGNMLYVGARETLFALSSNDISPTgeQQELTWSADEEKKQECSFKGKDPQRDCQNYIKILLRLNSTHLFTC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 147 GTGAFHPICGYIDLgvykEDIIFKLDTHN---LESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGPTH 223
Cdd:cd11257    89 GTYAFSPICTYIVM----TNFSLERDEKGeplLEDGKGRCPFDPEYKSTAIMVDGELYTGTVSNFQGNDPIIYRSLGSGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 224 DhhyIRTDiSEHYWLNGAKFIGTFFIPDTYNP---DDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKW 300
Cdd:cd11257   165 P---LKTE-NSLNWLQDPAFVGSAYIQESLPKlvgDDDKIYFFFSETGKEFDFFENTIVSRIARVCKGDEGGERVLQKRW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 301 TTFLKARLICSIPGsDGADtyFDELQDIYLLP--TRDERNPVVYGVFttTSSIFKG----SAVCVYSMADIRAVFNGPYA 374
Cdd:cd11257   241 TTFLKAQLLCSLPD-DGFP--FNVLQDVFVLTpsPEDWKDTLFYGVF--TSQWHKGtagsSAVCVFTMDQVQRAFNGLYK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 375 HKESADHRWVQYDGRIPYPRPGTCPSKTYDPL-IKSTRDFPDDVISFIKRHSVMYKsvyPVAGGPTFKRINVDYrlTQIV 453
Cdd:cd11257   316 EVNRETQQWYTYTHPVPEPRPGACITNSARERkINSSLHMPDRVLNFVKDHFLMDG---QVRSQPLLLQPQVRY--TQIA 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863909954 454 VDHVIAEDGQYDVMFLGTDIGTVLKVVSISKEKWnmeevVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11257   391 VHRVKGLHKTYDVLFLGTDDGRLHKAVSVGPMVH-----IIEELQIFSEGQPVQNLLLDTHKGLLYASSHSGVVQVPV 463
Sema_6 cd11242
The Sema domain, a protein interacting module, of class 6 semaphorins (Sema6); Class 6 ...
64-520 3.25e-103

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: 325.62  E-value: 3.25e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  64 SSEGLDFQTLLldEERGRLLLGAKDHIFLLSLVDLNKN----FKKIYWPAAKERVELCKLAGKDANtECANFIRVLQPYN 139
Cdd:cd11242     5 ARHRLDFQRML--RINRTLYIAARDHVYTVDLDASHTEeivpSKKLTWRSRQADVENCRMKGKHKD-ECHNFIKVLVPRN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 140 KTHIYVCGTGAFHPICGYidlgvYKEDiifKLDTHNLE-SGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRS 218
Cdd:cd11242    82 DETLFVCGTNAFNPVCRN-----YRID---TLEQDGEEiSGMARCPFDAKQANVALFADGKLYSATVTDFLASDAVIYRS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 219 LGPT-------HDHHYIRtdisEHYWLNGAKFigtffipdtynpdDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVG 291
Cdd:cd11242   154 LGDSptlrtvkYDSKWLK----EPHFVHAVEY-------------GDYVYFFFREIAVEYNTLGKVVFSRVARVCKNDMG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 292 G-QRSLINKWTTFLKARLICSIPGSdgADTYFDELQDIyLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFN 370
Cdd:cd11242   217 GsPRVLEKQWTSFLKARLNCSVPGD--SHFYFDVLQAV-TDVIRINGRPVVLGVFTTQYNSIPGSAVCAFDMDDIEKVFE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 371 GPYAHKESADHRWVQY-DGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRL 449
Cdd:cd11242   294 GRFKEQKSPDSAWTPVpEDRVPKPRPGCCAGSGSAEKYKTSNDFPDDTLNFIKTHPLMDEAVPSIINRPWFTRTMVRYRL 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 450 TQIVVDHVIAEDGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSI---------ILNMELSLKQQQLYI 520
Cdd:cd11242   374 TQIAVDNAAGPYQNYTVVFLGSEAGTVLKFLARIGPSGSNGSVFLEEIDVYNPAKCsydgeedrrIIGLELDRASHALFV 453
Sema_4F cd11261
The Sema domain, a protein interacting module, of semaphorin 4F (Sema4F); Sema4F plays role in ...
69-529 2.82e-100

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: 317.60  E-value: 2.82e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIYWPAAKERVELCKLAGKDaNTECANFIRVLQPYNKTHIYVCGT 148
Cdd:cd11261    13 NYSVLLVDPASHTLYVGARDAIFALTLPFSGERPRRIDWMVPEAHRQNCRKKGKK-EAECHNFIRILAIANASHLLTCGT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 149 GAFHPICGYIDLGVYKEdiifkldTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGPTHDhhYI 228
Cdd:cd11261    92 FAFDPKCGVIDVSSFQQ-------VERLESGRGKCPFEPAQRSAAIMAGGVLYAATVKNFLGTEPIISRAVGRAEE--WI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 229 RTDISEHyWLNGAKFIGTFFIPDTYNPD---DDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLK 305
Cdd:cd11261   163 RTETLPS-WLNAPAFVAAVFLSPAEWGDedgDDEIYFFFTETAREYDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 306 ARLICSIPGSdgaDTYFDELQDIYLLPTRDERN-PVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWV 384
Cdd:cd11261   242 ADLLCPGPEH---GRASSILQDVTTLRPLPGAGtPIFYGIFSSQWEGASISAVCAFRPQDIRRVMNGPFREFKHDCNRGL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 385 QY-DGRIPYPRPGTC-PSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFkrINVDYRLTQIVVDHVIAEDG 462
Cdd:cd11261   319 PVmDSDVPQPRPGECiTNNMKLLGFGSSLSLPDRVLTFVRDHPLMDRPVFPADGHPLL--VTTDTAYLRVAAHRVTSLSG 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863909954 463 Q-YDVMFLGTDIGTVLKVVSISKEKwnmeeVVLEELQIFKHSSIILNMElsLKQQQLYIGSRDGLVQL 529
Cdd:cd11261   397 KeYDVLYLGTEDGHLHRAVRIGAQL-----SVLEDLALFPEPQPVENLQ--LHHNWLLVGSDTEVTQI 457
Sema_4A cd11256
The Sema domain, a protein interacting module, of semaphorin 4A (Sema4A); Sema4A is expressed ...
69-521 5.36e-96

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: 306.07  E-value: 5.36e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLN--KNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYNKTHIYVC 146
Cdd:cd11256     9 NYDQLLLSPDETTLYVGARDNILALGIRTPGpiRLKHQIPWPANDSKISECAFKKKSNETECFNFIRVLVPVNGTHLYTC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 147 GTGAFHPICGYIDLGVYKedIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGpthDHH 226
Cdd:cd11256    89 GTYAFSPACTYIELDHFS--LPPPNGTIITMDGKGQSPFDPQHNYTAILVDGELYTGTMNNFRGNEPIIFRNLG---TKV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 227 YIRTDISeHYWLNG-AKFIGTFFIPDtynpdDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLK 305
Cdd:cd11256   164 SLKTDGF-LRWLNAdAVFVASFNPQG-----DSKVYFFFEETAREFDFFEKLTVARVARVCKNDVGGEKLLQKKWTTFLK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 306 ARLICSIPGSdgadTYFDELQDIYLLPTRDERNPVVYGVFTTTSSI--FKGSAVCVYSMADIRAVFNGPYAHKESADHRW 383
Cdd:cd11256   238 AQLTCSQQGH----FPFNVIHHVALLNQPDPNNSVFYAVFTSQWQLggRRSSAVCAYKLNDIEKVFNGKYKELNKESSRW 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 384 VQYDGRIPYPRPGTCpsktydplikSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYrlTQIVVDHVIAEDGQ 463
Cdd:cd11256   314 TRYMGPVSDPRPGSC----------SGGKSSDKALNFMKDHFLMDEVVLPGAGRPLLVKSNVQY--TRIAVDSVQGVSGH 381
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1863909954 464 -YDVMFLGTDIGTVLKVVSISKEkwnmEEVVLEELQIFKHSSIILNMELSLKQQQLYIG 521
Cdd:cd11256   382 nYTVMFLGTDKGFLHKAVLMGGS----ESHIIEEIELLTPPEPVENLLLAANEGVVYIG 436
Sema_6D cd11269
The Sema domain, a protein interacting module, of semaphorin 6D (Sema6D); Sema6D is expressed ...
64-531 3.12e-95

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: 304.64  E-value: 3.12e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  64 SSEGLDFQTLLldEERGRLLLGAKDHIFLLSLVDLNKN----FKKIYWPAAKERVELCKLAGKDANtECANFIRVLQPYN 139
Cdd:cd11269     5 SQHRLDFQLML--KIRDTLYIAGRDQVYTVNLNEVPKTevtpSRKLTWRSRQQDRENCAMKGKHKD-ECHNFIKVFVPRN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 140 KTHIYVCGTGAFHPICGYidlgvykediiFKLDTHNLE----SGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAF 215
Cdd:cd11269    82 DEMVFVCGTNAFNPMCRY-----------YRLSTLEYDgeeiSGLARCPFDARQTNVALFADGKLYSATVADFLASDAVI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 216 TRSLGpthDHHYIRTDISEHYWLNGAKFIGTFfipdTYNpddDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGG-QR 294
Cdd:cd11269   151 YRSMG---DGSALRTIKYDSKWIKEPHFLHAI----EYG---NYVYFFFREIAVEHNNLGKAVYSRVARICKNDMGGsQR 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 295 SLINKWTTFLKARLICSIPGSdgADTYFDELQDIYLLPtrdERN--PVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGP 372
Cdd:cd11269   221 VLEKHWTSFLKARLNCSVPGD--SFFYFDVLQSITDII---EINgiPTVVGVFTTQLNSIPGSAVCAFSMDDIEKVFKGR 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 373 YAHKESADHRWVQY-DGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQ 451
Cdd:cd11269   296 FKEQKTPDSVWTAVpEDKVPKPRPGCCAKHGLAEAYKTSIDFPDETLSFIKSHPLMDSAVPSIIEEPWFTKTRVRYRLTA 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 452 IVVDHVIAEDGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIFKHSSI---------ILNMELSLKQQQLYIGS 522
Cdd:cd11269   376 IAVDHAAGPHQNYTVIFVGSEAGVVLKILAKTSPFSLNDSVLLEEIEAYNHAKCsaeneedrrVISLQLDRDHHALFVAF 455

                  ....*....
gi 1863909954 523 RDGLVQLSL 531
Cdd:cd11269   456 SSCVVRIPL 464
Sema_2A cd11238
The Sema domain, a protein interacting module, of semaphorin 2A (Sema2A); Sema2A, a secreted ...
68-531 3.86e-90

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: 290.87  E-value: 3.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  68 LDFQTLLLDEERGRLLLGAKDHIFLLSLVDLN---KNFKKIYWPAAKERVELCKLAGKDANTECANFIRVLQPYN-KTHI 143
Cdd:cd11238     1 LYYRTLLLDEKRNALYVGAMDRVFRLNLYNINdtgNNCARDELTLSPSDVSECVSKGKDEEYECRNHVRVIQPMGdGQTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 144 YVCGTGAFHPicgyidlgvyKEDIIFKLDTHNLE------SGRLKCPFDPQQPFASVMTDE-------YLYSGTASDFLG 210
Cdd:cd11238    81 YVCSTNAMNP----------KDRVLDANLLHLPEyvpgpgNGIGKCPYDPDDNSTAVWVEWgnpgdlpALYSGTRTEFTK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 211 KDTAFTRS---LGPTHDHH-YIRTDISEHYWLNGAKFIGTFFIpdtynpdDDKIYFFFRESSQEGSTSDKTILSRVGRVC 286
Cdd:cd11238   151 ANTVIYRPplyNNTKGRHEsFMRTLKYDSKWLDEPNFVGSFDI-------GDYVYFFFRETAVEYINCGKVVYSRVARVC 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 287 KNDVGGQRSLINKWTTFLKARLICSIPGSdgADTYFDELQDIYLLPTRDErnPVVYGVFTTTSSIFKGSAVCVYSMADIR 366
Cdd:cd11238   224 KKDTGGKNVLRQNWTTFLKARLNCSISGE--FPFYFNEIQSVYKVPGRDD--TLFYATFTTSENGFTGSAVCVFTLSDIN 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 367 AVFN-GPYAHKESADHRWVQY-DGRIPYPRPGTCpsktydplIKSTRDFPDDVISFIKRHSVMYKSVYpvAGGPTF-KRi 443
Cdd:cd11238   300 AAFDtGKFKEQASSSSAWLPVlSSEVPEPRPGTC--------VNDSATLSDTVLHFARTHPLMDDAVS--HGPPLLyLR- 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 444 nvDYRLTQIVVDHVIAEDGQYDVMFLGTDIGTVLKVVSIsKEKWNMEEVVLEELQIfKHSSIILNMELSlKQQQLYIGSR 523
Cdd:cd11238   369 --DVVFTHLVVDKLRIDDQEYVVFYAGSNDGKVYKIVHW-KDAGESKSNLLDVFEL-TPGEPIRAMELL-PGEFLYVASD 443

                  ....*...
gi 1863909954 524 DGLVQLSL 531
Cdd:cd11238   444 HRVSQIDL 451
Sema_5 cd11241
The Sema domain, a protein interacting module, of semaphorin 5 (Sema5); Class 5 semaphorins ...
69-531 4.49e-89

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: 287.53  E-value: 4.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNkNFKKIYWPAAKERVELCKLAGKDANtECANFIRVLQPYNKThIYVCGT 148
Cdd:cd11241     8 DFSRLVLDPTHDQLIVGARNYLFRLRLQSLS-LLQAVPWNSDEDTKRQCQSKGKSVE-ECQNYVRVLLVVGKN-LFTCGT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 149 GAFHPICGYIDLgvykEDIIFKLDTHnleSGRLKCPFDPQQPFASVMT-DEYLYSGTASDFLGKDTAFTRSLGPTHDhhy 227
Cdd:cd11241    85 YAFSPVCTIRKL----SNLTQILDTI---SGVARCPYSPAHNSTALISaSGELYAGTVYDFSGRDPAIYRSLGGKPP--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 228 IRTDISEHYWLNGAKFIGTFFIpdtynpdDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTTFLKAR 307
Cdd:cd11241   155 LRTAQYNSKWLNEPNFVGSYEI-------GNHTYFFFRENAVEHQDCGKTVYSRIARVCKNDIGGRFLLEDTWTTFMKAR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 308 LICSIPGSdgADTYFDELQDIYLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYd 387
Cdd:cd11241   228 LNCSLPGE--FPFYYNEIQGTFYLPETD----LIYAVFTTNVNGIAGSAICAFNLSAINQAFNGPFKYQENNGSAWLPT- 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 388 griPYPRPGTCPSKTYD---PLIKSTRDFPDDvisfiKRHSVMYKSVYPVAGGPTFKRINVdyRLTQIVVDHVIAEDGQ- 463
Cdd:cd11241   301 ---PNPHPNFQCTTSIDrgqPANTTERDLQDA-----QKYQLMAEVVQPVTKIPLVTMDDV--RFSKLAVDVVQGRGTQl 370
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 464 YDVMFLGTDIGTVLKVVSISKekwNMEEVVLEELQIF--KHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11241   371 VHIFYVGTDYGTILKMYQPHR---SQKSCTLEEIKILpaMKGEPITSLQFLKSEKSLFVGLETGVLRIPL 437
Sema_6A cd11266
The Sema domain, a protein interacting module, of semaphorins 6A (Sema6A); In the cerebellum, ...
68-531 4.23e-87

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: 283.07  E-value: 4.23e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  68 LDFQTLLLDEERgrLLLGAKDHIFLlslVDLNKNF-------KKIYWPAAKERVELCKLAGKDANtECANFIRVLQPYNK 140
Cdd:cd11266     9 LDIQMIMIMNRT--LYIAARDHIYT---VDIDTSHteeiyfsKKLTWKSRQADVDTCRMKGKHKD-ECHNFIKVLLKRND 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 141 THIYVCGTGAFHPICGYidlgvYKEDIIFKLDTHNleSGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLG 220
Cdd:cd11266    83 DTLFVCGTNAFNPSCRN-----YKMDTLEFFGDEF--SGMARCPYDAKHANVALFADGKLYSATVTDFLAIDAVIYRSLG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 221 pthDHHYIRTDISEHYWLNGAKFIGTFfipdTYNpddDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGG-QRSLINK 299
Cdd:cd11266   156 ---DSPTLRTVKHDSKWLKEPYFVQAV----DYG---DYIYFFFREIAVEYNSMGKVVFPRVAQVCKNDMGGsQRVLEKQ 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 300 WTTFLKARLICSIPGSdgADTYFDELQ---DIYLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHK 376
Cdd:cd11266   226 WTSFLKARLNCSVPGD--SHFYFNILQavtDVIHINGRD----VVLATFSTPYNSIPGSAVCAYDMLDIASVFTGRFKEQ 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 377 ESADHRWVQY-DGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVD 455
Cdd:cd11266   300 KSPDSTWTPVpDERVPKPRPGCCAGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVD 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 456 HVIAEDGQYDVMFLGTDIGTVLK-VVSISKEKWNMEEVVLEELQIFKHSSI---------ILNMELSLKQQQLYIGSRDG 525
Cdd:cd11266   380 NAAGPYQNHTVVFLGSEKGIILKfLARTGNSGFLNDSLFLEEMNVYNSEKCsydgvedkrIMGMQLDKASSALYVAFSTC 459

                  ....*.
gi 1863909954 526 LVQLSL 531
Cdd:cd11266   460 VIKVPL 465
Sema_5C cd11265
The Sema domain, a protein interacting module, of semaphorin 5C (sema5C); In Drosophila, ...
73-529 8.41e-84

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: 273.20  E-value: 8.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  73 LLLDEERGRLLLGAKDHIFLLSLVDLNKnFKKIYWPAAKERVELCKLAGKdANTECANFIRVLQPYNKtHIYVCGTGAFH 152
Cdd:cd11265    12 MLFDVARNQVIVGARDNLYRLSLDGLEL-LERASWPAAESKVALCQNKGQ-SEEDCHNYVKVLLSYGK-QLFACGTNAFS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 153 PICGYIDLgvykEDIIFKLDThnlESGRLKCPFDPQQPFASVMTDE-YLYSGTASDFLGKDTAFTRSLGPTHDHhYIRTD 231
Cdd:cd11265    89 PRCSWREM----ENLTSVTEW---DSGVAKCPYSPHANITALLSSSgQLFVGSPTDFSGSDSAIYRTLGTSNKS-FLRTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 232 ISEHYWLNGAKFIGTFfipdtynPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLI-NKWTTFLKARLIC 310
Cdd:cd11265   161 QYNSKWLNEPQFVGSF-------ETGNFVYFLFRESAVEYMNCGKVIYSRIARVCKNDVGGGTMLLkDNWTTFLKARLNC 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 311 SIPGSdgADTYFDELQDIYLLPtrDERnpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYDgrI 390
Cdd:cd11265   234 SLPGE--YPFYFDEIQGMTYLP--DEG--ILYATFTTPENSIAGSAVCAFNLSSINAAFDGPFKHQESSGAAWERVN--V 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 391 PY-PRPGTCPSKTYDPLIKSTrdfpddvisfikRHSVMYKSVYPVAGGPTFkRINVDyRLTQIVVDhVIAE--DGQYDVM 467
Cdd:cd11265   306 NHrDHFNQCSSSSSSHLLESS------------RYQLMDEAVQPITLEPLH-HAKLE-RFSHIAVD-VIPTkiHQSVHVL 370
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863909954 468 FLGTDIGTVLKVVSISKEKwnmEEVVLEELQIFKHS-SIILNMELSLKQQQLYIGSRDGLVQL 529
Cdd:cd11265   371 YVATTGGLIKKISVLPRTQ---ETCLVEIWQPLPTPdSPIKTMQYLKVTDSLYVGTELALMRI 430
Sema_6E cd11270
The Sema domain, a protein interacting module, semaphorin 6E (sema6E); Sema6E is expressed ...
67-531 1.64e-80

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: 265.43  E-value: 1.64e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  67 GLDFQTLLldEERGRLLLGAKDHIFLLSLVDLNKNF---KKIYWPAakERVELCKLAGKdANTECANFIRVLQPYNKTHI 143
Cdd:cd11270     8 GLDFQRML--RINHMVYIAARDHVFAINLSASLERIvpqQKLTWKT--KDVEKCTVRGK-NSDECYNYIKVLVPRNDETL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 144 YVCGTGAFHPICGyidlgVYKediIFKLDTHNLE-SGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRSLGpt 222
Cdd:cd11270    83 FACGTNAFNPTCR-----NYK---MSSLEQDGEEvIGQARCPFESRQSNVGLFAGGDFYSATMTDFLASDAVIYRSLG-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 223 HDHHYIRTDISEHYWLNGAKFIGTFfipdTYNpddDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINK-WT 301
Cdd:cd11270   153 ESSPVLRTVKYDSKWLREPHFLHAI----EYG---NYVYFFLSEIAVEYTTLGKVVFSRVARVCKNDNGGSPRVLERyWT 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 302 TFLKARLICSIPGSdgADTYFDELQDIYLLPTRDERnPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADH 381
Cdd:cd11270   226 SFLKARLNCSVPGD--SFFYFDVLQSLTNVMQINHR-PAVLGVFTTQANSITGSAVCAFYMDDIEKVFNGKFKEQRNSES 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 382 RWVQY-DGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVDYRLTQIVVDHVIAE 460
Cdd:cd11270   303 AWTPVpDEAVPKPRPGSCAGDGPAAGYKSSTNFPDETLTFIKSYPLMDEAVPSVNNRPCFTRTTSRFKLTQIAVDTAAGP 382
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863909954 461 DGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIF--------KHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11270   383 YKNYTVVFLGSENGHVLKVLASMHPNSSYSTQVLEDIDVYnpnkcnvrGEDRRILGLELDKDHHALFVAFTGCVIRVPL 461
Sema_6B cd11267
The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as ...
63-501 9.06e-80

The Sema domain, a protein interacting module, of semaphorin 6B (Sema6B); Sema6B functions as repellents for axon growth; this repulsive activity is mediated by its receptor Plexin A4. Sema6B is expressed in CA3, and repels mossy fibers in a Plexin A4 dependent manner. In human, it was shown that peroxisome proliferator-activated receptors (PPARs) and 9-cis-retinoic acid receptor (RXR) regulate human semaphorin 6B (Sema6B) gene expression. Sema6B is a member of the class 6 semaphorin family of proteins, which are membrane associated semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200528 [Multi-domain]  Cd Length: 466  Bit Score: 263.62  E-value: 9.06e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  63 GSSEGLDFQTLLLDEERgrLLLGAKDHIFLLSLVDLNKN----FKKIYWPAAKERVELCKLAGKDANtECANFIRVLQPY 138
Cdd:cd11267     4 RGRDRLNIQRVLRVNRT--LYIGDRDNLYRVELDPTAGTemryHKKLTWRSNKNDINVCRMKGKHEG-ECRNFIKVLLLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 139 NKTHIYVCGTGAFHPICGYidlgvykediiFKLDThnLE------SGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKD 212
Cdd:cd11267    81 DYGTLFVCGTNAFNPVCAN-----------YSIDT--LEpvgdniSGMARCPYDPKHANVALFADGMLFTATVTDFLAID 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 213 TAFTRSLGPT-------HDHHYIRtdisEHYWLNGAKFigtffipdtynpdDDKIYFFFRESSQEGSTSDKTILSRVGRV 285
Cdd:cd11267   148 AVIYRSLGDSpalrtvkHDSKWFK----EPYFVHAVEW-------------GSHVYFFFREIAMEFNYLEKVVVSRVARV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 286 CKNDVGG-QRSLINKWTTFLKARLICSIPGSdgADTYFDELQ---DIYLLPTRdernPVVYGVFTTTSSIFKGSAVCVYS 361
Cdd:cd11267   211 CKNDMGGsQRVLEKQWTSFLKARLNCSVPGD--SHFYFNVLQavsDILNLGGR----PVVLAVFSTPTNSIPGSAVCAFD 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 362 MADIRAVFNGPYAHKESADHRWVQY-DGRIPYPRPGTC--PSKTYDplikSTRDFPDDVISFIKRHSVMYKSVYPVAGGP 438
Cdd:cd11267   285 MTQVAAVFEGRFREQKSPESIWTPVpEELVPRPRPGCCaaPGMRYN----SSSTLPDEVLNFVKTHPLMDEAVPSLGHAP 360
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863909954 439 TFKRINVDYRLTQIVVDHVIAEDGQYDVMFLGTDIGTVLKVV---SISKEKWNMEEVVLEELQIFK 501
Cdd:cd11267   361 WIVRTMTRYQLTHMVVDTEAGPHGNHTVVFLGSTRGTVLKFLiipNASSSEISNQSVFLEELETYN 426
Sema_5A cd11263
The Sema domain, a protein interacting module, of semaphorin 5A (Sema5A); Originally, mouse ...
68-531 3.88e-79

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: 261.12  E-value: 3.88e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  68 LDFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKnFKKIYWPAAKERVELCKLAGKdANTECANFIRVLQpYNKTHIYVCG 147
Cdd:cd11263     7 VDFSQLTFDPGQKELIVGARNYLFRLQLEDLSL-IQAVEWECDEATKKACYSKGK-SKEECQNYIRVLL-VGGDRLFTCG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 148 TGAFHPICGYIDLGVYKEdiifkldTHNLESGRLKCPFDPQQPFASVMTDE-YLYSGTASDFLGKDTAFTRSLG--PThd 224
Cdd:cd11263    84 TNAFTPICTNRTLNNLTE-------IHDQISGMARCPYSPQHNSTALLTSSgELYAATAMDFPGRDPAIYRSLGilPP-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 225 hhyIRTDISEHYWLNGAKFIGTFFIPDTynpdddkIYFFFRESSQEGSTSdKTILSRVGRVCKNDVGGQRSLINKWTTFL 304
Cdd:cd11263   155 ---LRTAQYNSKWLNEPNFVSSYDIGNF-------TYFFFRENAVEHDCG-KTVFSRAARVCKNDIGGRFLLEDTWTTFM 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 305 KARLICSIPGSdgADTYFDELQDIYLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWv 384
Cdd:cd11263   224 KARLNCSRPGE--IPFYYNELQSTFFLPELD----LIYGIFTTNVNSIAASAVCVFNLSAISQAFNGPFKYQENSRSAW- 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 385 qydgrIPYPRP------GTCPSKTYDPLikSTRDFpDDVISFIKRHSVmyksVYPVAGGPTFKRINVdyRLTQIVVDHVI 458
Cdd:cd11263   297 -----LPYPNPnpnfqcGTMDQGLYVNL--TERNL-QDAQKFILMHEV----VQPVTPVPYFMEDNS--RFSHVAVDVVQ 362
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863909954 459 AEDGQYDVMFLGTDIGTVLKVVSISKEkwNMEEVVLEELQIF--KHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11263   363 GKDMLFHIIYLATDYGTIKKVLAPLNQ--SSSSCLLEEIELFpkRQREPIRSLQILHSQSVLFVGLQEHVIKIPL 435
Sema pfam01403
Sema domain; The Sema domain occurs in semaphorins, which are a large family of secreted and ...
325-512 1.09e-78

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: 250.65  E-value: 1.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 325 LQDIYLLP--TRDERNPVVYGVFTTT-SSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYDGRIPYPRPGTCPSK 401
Cdd:pfam01403   1 LQDVFVLKpgAGDALDTVLYGVFTTQwSNSIGGSAVCAFSLSDINAVFEGPFKEQEKSDSKWLPYTGKVPYPRPGTCIND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 402 TYdpliksTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRinVDYRLTQIVVDHVIAEDGQYDVMFLGTDIGTVLKVVS 481
Cdd:pfam01403  81 PL------RLDLPDSVLNFVKDHPLMDEAVQPVGGRPLLVR--TGVRLTSIAVDRVQALDGNYTVLFLGTDDGRLHKVVL 152
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1863909954 482 ISKEkwnmEEVVLEELQIFKHSSIILNMELS 512
Cdd:pfam01403 153 VGSE----ESHIIEEIQVFPEPQPVLNLLLS 179
Sema_5B cd11264
The Sema domain, a protein interacting module, of semaphorin 5B (Sema5B); Sema5B is expressed ...
69-531 2.62e-77

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: 256.06  E-value: 2.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIFLLSLVDLNKnFKKIYWPAAKERVELCKLAGKdANTECANFIRVLQpYNKTHIYVCGT 148
Cdd:cd11264     8 DFSQLALDLNRNQLIVGARNYLFRLSLHNVSL-IQATEWGSDEDTRRSCQSKGK-TEEECQNYVRVLI-VYGKKVFTCGT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 149 GAFHPICGYIDLGVYKEdIIFKLDthnlesGRLKCPFDPQQPFASVMTDE-YLYSGTASDFLGKDTAFTRSLGPTHDhhy 227
Cdd:cd11264    85 NAFSPVCTSRQVGNLSK-VIERIN------GVARCPYDPRHNSTAVITSRgELYAATVIDFSGRDPAIYRSLGSVPP--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 228 IRTDISEHYWLNGAKFIGTFFIPDTynpdddkIYFFFRESSQEGSTSdKTILSRVGRVCKNDVGGQRSLINKWTTFLKAR 307
Cdd:cd11264   155 LRTAQYNSKWLNEPNFIAAYDIGLF-------TYFFFRENAVEHDCG-KTVYSRVARVCKNDIGGRFLLEDTWTTFMKAR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 308 LICSIPGSdgADTYFDELQDIYLLPTRDernpVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKESADHRWVQYD 387
Cdd:cd11264   227 LNCSRPGE--IPFYYNELQSTFYLPEQD----LIYGVFTTNVNSIAASAVCAFNLSAITQAFNGPFRYQENPRSAWLPTA 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 388 GRIPYPRPGTCPSKTydplikSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINVdyRLTQIVVDHVIAEDGQYDVM 467
Cdd:cd11264   301 NPIPNFQCGTLSDDS------PNENLTERSLQDAQRLFLMNDVVQPVTVDPLVTQDSV--RFSKLVVDIVQGKDTLYHVM 372
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863909954 468 FLGTDIGTVLKVVSISKEkwNMEEVVLEELQIFK--HSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11264   373 YIGTEYGTILKALSTTNR--SLRSCYLEEMQILPpgQREPIRSLQILHSDRSLFVGLNNGVLKIPL 436
Sema_6C cd11268
The Sema domain, a protein interacting module, of semaphorin 6C (Sema6C, also called ...
67-531 3.46e-76

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: 254.24  E-value: 3.46e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  67 GLDFQTLLLDEERgrLLLGAKDHIFLLSLVDLNKN-----FKKIYWPAakERVELCKLAGKDANtECANFIRVLQPYNKT 141
Cdd:cd11268     8 GLDFQRFLTLNRT--LLVAARDHVFSFDLQAEEEGeglvpNKYLTWRS--QDVENCAVRGKLTD-ECYNYIRVLVPWDSQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 142 HIYVCGTGAFHPIC---GYIDLGVYKEDIifkldthnleSGRLKCPFDPQQPFASVMTDEYLYSGTASDFLGKDTAFTRS 218
Cdd:cd11268    83 TLLACGTNSFSPVCrsyGITSLQQEGEEL----------SGQARCPFDATQSNVAIFAEGSLYSATAADFQASDAVVYRS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 219 LGPTHDhhyIRTDISEHYWLNGAKFIGTFfipdtynPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQ-RSLI 297
Cdd:cd11268   153 LGPQPP---LRSAKYDSKWLREPHFVQAL-------EHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSpRALD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 298 NKWTTFLKARLICSIPGSdgADTYFDELQDIyLLPTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPYAHKE 377
Cdd:cd11268   223 RHWTSFLKLRLNCSVPGD--STFYFDVLQAL-TGPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDEIERGFEGKFKEQR 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 378 SADHRWVQY-DGRIPYPRPGTCPSKTYDPLIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKrINVDYRLTQIVVDH 456
Cdd:cd11268   300 SLDGAWTPVsEDRVPSPRPGSCAGVGGAALFSSSRDLPDDVLTFIKAHPLLDPAVPPVTHQPLLT-LTSRALLTQVAVDG 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 457 VIAEDGQYDVMFLGTDIGTVLKVVSISKEKWNMEEVVLEELQIF-----------KHSSIILNMELSLKQQQLYIGSRDG 525
Cdd:cd11268   379 MAGPHSNITVMFLGSNDGTVLKVLPPGGRSGGPEPILLEEIDAYsparcsgkrtaQTARRIIGLELDTEGHRLFVAFSGC 458

                  ....*.
gi 1863909954 526 LVQLSL 531
Cdd:cd11268   459 IVYLPL 464
Sema cd09295
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
69-531 5.71e-62

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: 213.61  E-value: 5.71e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  69 DFQTLLLDEERGRLLLGAKDHIF----LLSLVDLNKNFKKIYWPAAKERVELCKLaGKDANTECANFIRVLQP-YNKTHI 143
Cdd:cd09295     1 DDDKILVSFRKDTIYVGAIARIYkvdgGGTRLLLSCISPELNFGFNEDQKAFCPL-RRGKWTECINYIKVLQQkGDLDIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 144 YVCGTGAFHPICGYidlgvYKEDIIFKLDTHNLESGRLKCPFDPQQPFASVMTDEYLYSGTASDFL-GKDTAFTRSLGPT 222
Cdd:cd09295    80 AVCGSNAAQPSCGS-----YRLDVLVELGKVRWPSGRPRCPIDNKHSNMGVNVDSKLYSATDHDFKdGDRPALSRRSSNV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 223 HdhhYIRTDISEHYWLNGAkfigTFFIPDTYNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSLINKWTT 302
Cdd:cd09295   155 H---YLRIVVDSSTGLDEI----TFVYAFVSGDDDDEVYFFFRQEPVEYLKKGMVYVPRIARVCKLDVGGCHRLKKKLTS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 303 FLKARLICSIPGSdgaDTYFDELQDIYLLpTRDERNPVVYGVFTTTSSIFKGSAVCVYSMADIRAVFNGPyahkesadhr 382
Cdd:cd09295   228 FLKADLNCSRPQS---GFAFNLLQDATGD-TKNLIQDVKFAIFSSCLNKSVESAVCAYLFTDINNVFDDP---------- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 383 wvqydgripyprpgtcpsktydplikstrdfpddvisfikrhsvmyksVYPVAGGPTFKRINVDYRLTQIVVDHVIAEDG 462
Cdd:cd09295   294 ------------------------------------------------VEAINNRPLYAHQNQRSRLTSIAVDATKQKSV 325
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863909954 463 QYDVMFLGTDIGTVLKVvsISKEKWNmEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd09295   326 GYQVVFLGLKLGSLGKA--LAFFFLY-KGHIIEEWKVFKDSSRITNLDLSRPPLYLYVGSESGVLGVPV 391
Sema_7A cd11243
The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); ...
81-531 1.13e-60

The Sema domain, a protein interacting module, of semaphorin 7A (Sema7A, also called CD108); Sema7A plays regulatory roles in both immune and nervous systems. Unlike other semaphorins, which act as repulsive guidance cues, Sema7A enhances central and peripheral axon growth and is required for proper axon tract formation during embryonic development. Sema7A also plays a critical role in the negative regulation of T cell activation and function. Sema7A is a membrane-anchored member of the semaphorin family of proteins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems and cancer. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module.


Pssm-ID: 200504 [Multi-domain]  Cd Length: 414  Bit Score: 210.47  E-value: 1.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  81 RLLLGAKDHIFLLSLVDLNKNFKKIywPAAKERVELCKLAGKDantECANFIRVLQPYNKThIYVCGTGAFHPICgyidl 160
Cdd:cd11243    15 SVYVGGQGALYLLDFTGSAVIVKKI--PDEKTEKDCKKRATLD---DCENYITLIKKLDYR-LLVCGTNAGSPKC----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 161 gvykediiFKLDTHNLES---GRLKCPFDPQQPFASVMTDEYLYSgTASDFLGKDTAFTRslgpthdhhyIRTDiSEHY- 236
Cdd:cd11243    84 --------WFLVNQTLVTlsaDRGVAPFLPDENSLVLIEGNNVYS-TISGKKGNIPRFRR----------YGGK-KELYt 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 237 ---WLNGAKFIGTFFIPDTyNPDDDKIYFFFRESSQEGSTSDKTILSRVGRVCKNDVGGQRSL-INKWTTFLKARLICSI 312
Cdd:cd11243   144 sdtVMQKPQFVKATLLPED-EQYQDKIYYFFREDNEDKGPEAEPNISRVARLCKEDQGGTSSLsTSKWSTFLKARLVCGD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 313 PGSDGadtYFDELQDIYLLPTRDERNPVVYGVFTTTssiFKGSAVCVYSMADIRAVFngpyahkeSADHRWvQYDGRIPY 392
Cdd:cd11243   223 PATPM---NFNRLQDVFLLPKEEWREAVVYGVFSNT---WGSSAVCSYSLGDIDKVF--------RTSSLK-GYSGSLPN 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 393 PRPGTCpsktydplIKSTRDFPDDVISFIKRHSVMYKSVYPVAGGPTFKRINvDYRLTQIVVDHVIAEDG-QYDVMFLGT 471
Cdd:cd11243   288 PRPGTC--------VPPEQTHPSETFSFADEHPELDDRIEPDEPRKLPVFQN-KDHYQKVVVDEVRASDGvSYDVLYLAT 358
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 472 DIGTVLKVVSIskekwNMEEVVLEELQIFKHSSIILNMELSLKQQQLYIGSRDGLVQLSL 531
Cdd:cd11243   359 DKGKIHKVVES-----KGQTHNIMEIQPFKEQEPIQSMILDAERSHLYVGTKAEVTRLPL 413
Ig_Sema3 cd05871
Immunoglobulin (Ig)-like domain of class III semaphorin Sema3; The members here are composed ...
595-686 1.12e-48

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


Pssm-ID: 409455  Cd Length: 92  Bit Score: 166.37  E-value: 1.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 595 TADEKVIFGIEFNSTFLECIPKSQQATIKWYIQRSGDEHREELKPDERIIKTEYGLLIRSLQKKDSGMYYCKAQEHTFIH 674
Cdd:cd05871     1 NAEEKVVYGVEGNSTFLECLPKSPQATVKWLFQRGGDQRKEEVKSEERLIVTDRGLLLRSLQRSDAGVYTCQAVEHGFSQ 80
                          90
                  ....*....|..
gi 1863909954 675 TIVKLTLNVIEN 686
Cdd:cd05871    81 TLVKIRLHVIEP 92
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
608-685 1.40e-14

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


Pssm-ID: 409368  Cd Length: 88  Bit Score: 69.80  E-value: 1.40e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863909954 608 STFLECIPKSQQATIKWYIQRSgdeHREELKPDERIIKTEYGLLIRSLQKKDSGMYYCKAQEHTFIHTIVKLTLNVIE 685
Cdd:cd04979    13 TVILSCSVKSNNAPVTWIHNGK---KVPRYRSPRLVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSVTLHVLE 87
Sema_plexin_like cd11236
The Sema domain, a protein interacting module, of Plexins and MET-like receptor tyrosine ...
70-520 1.34e-09

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: 60.81  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  70 FQTLLLDEERGRLLLGAKDHIFLLSLVDLNKNFKKIywpAAKERVELCKLAGKDANTECA----NFIRVLQPYNK-THIY 144
Cdd:cd11236     2 FNHLAVDNSTGRVYVGAVNRLYQLDSSLLLEAEVST---GPVLDSPLCLPPGCCSCDHPRsptdNYNKILLIDYSsGRLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 145 VCGTgAFHPICGyidlgVYKEDIIFKLD---THNLESGrlkcpfDPQQPFASVMT------DEYLYSGTASDFLGKDTAF 215
Cdd:cd11236    79 TCGS-LYQGVCQ-----LRNLSNISVVVersSTPVAAN------DPNASTVGFVGpgpynnENVLYVGATYTNNGYRDYR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 216 ----TRSLGPTHDHH----------YIRTDISEHYWLngaKFIGTFfipdtynPDDDKIYFFFResSQEGSTSDKTILSR 281
Cdd:cd11236   147 pavsSRSLPPDDDFNagsltggsaiSIDDEYRDRYSI---KYVYGF-------SSGGFSYFVTV--QRKSVDDESPYISR 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 282 VGRVCKNDvggqrsliNKWTTFLKARLICSipGSDGADtyFDELQDIYL------------LPTRDErnpVVYGVFTTTS 349
Cdd:cd11236   215 LVRVCQSD--------SNYYSYTEVPLQCT--GGDGTN--YNLLQAAYVgkagsdlarslgISTDDD---VLFGVFSKSK 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 350 SIFKG----SAVCVYSMADIRAVFNgpyahkesadhrwvqydgripyprpGTCPsktydplikstrdfpddvISFikrhs 425
Cdd:cd11236   280 GPSAEpsskSALCVFSMKDIEAAFN-------------------------DNCP------------------LGG----- 311
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 426 vmyksVYPVAGGPTFkrinVDYRLTQIVVDHViaedGQYDVMFLGTDIGTVLKVVSISKEkwnmEEVVLEELQIFKHSSI 505
Cdd:cd11236   312 -----GVPITTSAVL----SDSLLTSVAVTTT----RNHTVAFLGTSDGQLKKVVLESSS----SATQYETLLVDSGSPI 374
                         490
                  ....*....|....*
gi 1863909954 506 ILNMELSLKQQQLYI 520
Cdd:cd11236   375 LPDMVFDPDGEHLYV 389
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
533-570 2.33e-08

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 50.62  E-value: 2.33e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1863909954  533 RCDTYgKACADCCLARDPYCAWD--GNACSRYAPTSKRRA 570
Cdd:smart00423   1 RCSKY-TSCSECLLARDPYCAWCssQGRCTSGERCDSRRQ 39
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
464-561 9.99e-07

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


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 52.24  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 464 YDVMFLGTDIGTVLKVVSISKEKWNmeeVVLEELQIFKHSSIIL-NMELSLKQQQLYIGSRDGLVQLSLHRCDTYgKACA 542
Cdd:cd11272   406 YSVVFVGTKSGKLKKIRADGPPHGG---VQYEMVSVFKDGSPILrDMAFSIDHKYLYVMSERQVSRVPVESCEQY-TTCG 481
                          90       100
                  ....*....|....*....|.
gi 1863909954 543 DCCLARDPYCAWDG--NACSR 561
Cdd:cd11272   482 ECLSSGDPHCGWCAlhNMCSR 502
Sema_plexin_B2 cd11276
The Sema domain, a protein interacting module, of Plexin B2; Plexin B2 serves as the receptor ...
73-530 1.82e-06

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: 51.32  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954  73 LLLDEERGRLLLGAKDHIFLLSlVDLN----------KNFKKIYWPAAKERvelCKLAGKDANTecaNFIRVLQPYNKTh 142
Cdd:cd11276    11 LVVDPQTGRVYLGAVNALYQLD-ADLQlesrvetgpkKDNKKCTPPIEENQ---CTEAKMTDNY---NKLLLLDSANKT- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 143 IYVCGTgAFHPICGYIDLGVYKEdIIFKLDThnleSGrlkcpfdpQQPFASvMTDEYL-------YSGTASD---FLGK- 211
Cdd:cd11276    83 LVVCGS-LFKGICSLRNLSNISE-VIYYSDT----SG--------EKSFVA-SNDEGVstvglisSLKPGNDrvfFVGKg 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 212 ----DTAF---TRSLgPTHDHHYIRTDISEHYWLNGA-------KFIGTFfipdtynPDDDKIYFFFresSQEGSTSDKT 277
Cdd:cd11276   148 ngsnDNGKiisTRLL-QNYDDREVFENYIDAATVKSAyvsrytqQFRYAF-------EDNNYVYFLF---NQQLGHPDKN 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 278 IlSRVGRVCKNDvggqrsliNKWTTFLKARLICSipgsDGADTYfDELQDIYL----------LPTRDERNPVVYGVFTT 347
Cdd:cd11276   217 R-TLIARLCEND--------HHYYSYTEMDLNCR----DGANAY-NKCQAAYVstpgkelaqnYGNSILSDKVLFAVFSR 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 348 TSSIFKGSAVCVYSMADIRAVF--NGPYAHKESADHRWVQYDgriPYPRPGTCPSKTYDPliKSTRDFPDDViSFIKrhs 425
Cdd:cd11276   283 DEKDSGESALCMFPLKSINAKMeaNREACYTGTIDDRDVFYK---PFHSQKDIICGSHQQ--KNSKSFPCGS-EHLP--- 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 426 vmyksvYPVAG-------GPTFKRINVDyrLTQIVVdhviAEDGQYDVMFLGTDIGTVLKV-VSISKEKWNmeevvleEL 497
Cdd:cd11276   354 ------YPLGSrdelaltAPVLQRGGLN--LTAVTV----AVENGHTVAFLGTSDGRILKVhLSPDPEEYN-------SI 414
                         490       500       510
                  ....*....|....*....|....*....|...
gi 1863909954 498 QIFKHSSIILNMELSLKQQQLYIGSRDGLVQLS 530
Cdd:cd11276   415 LIEKNKPVNKDLVLDKTLEHLYIMTEDKVFRLP 447
Sema_plexin_B cd11245
The Sema domain, a protein interacting module, of Plexin B; Plexins, which contain semaphorin ...
243-479 2.31e-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: 50.70  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 243 FIGTFfipdtynPDDDKIYFFFresSQEGSTSDKTILSRVGRVCKNDvggqrsliNKWTTFLKARLICsipgSDGADTYF 322
Cdd:cd11245   186 FVYAF-------ADNGYIYFLF---SRRPGTADSTKRTYISRLCEND--------HHYYSYVELPLNC----TVNQENTY 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 323 DELQDIYLLPTRDERN-PVVYGVFTTTSSIFKG----SAVCVYSMADIRAVFN------------GPYAHKESAdhrwvq 385
Cdd:cd11245   244 NLVQAAYLAKPGKVLNgKVLFGVFSADEASTAApdgrSALCMYPLSSVDARFErtrescytgeglEDDKPETAY------ 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863909954 386 ydgrIPYPRPGTC---PSKTYDPLIKSTRDFPDDVisfikrhsvmyKSVYPVAGGPTFKRINvdyRLTQIVvdhVIAEDG 462
Cdd:cd11245   318 ----IEYNVKSICktlPDKNVKAYPCGAEHTPSPL-----------ASRYPLAAKPILTRND---MLTAVA---VAVENG 376
                         250
                  ....*....|....*..
gi 1863909954 463 qYDVMFLGTDIGTVLKV 479
Cdd:cd11245   377 -HTIAFLGDSGGQLHKV 392
IgV_TCR_beta cd05899
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here ...
608-665 1.44e-04

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here are composed of the immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409480  Cd Length: 110  Bit Score: 41.88  E-value: 1.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1863909954 608 STFLECIPKSQQATIKWYIQRSGDE------HREELKPDE-----------RIIKTEYGLLIRSLQKKDSGMYYC 665
Cdd:cd05899    15 SVTLRCSQKSGHDNMYWYRQDPGKGlqllfySYGGGLNEEgdlpgdrfsasRPSLTRSSLTIKSAEPEDSAVYLC 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
611-668 2.18e-04

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 40.01  E-value: 2.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1863909954 611 LEC-IPKSQQATIKWYiqRSGDEHREELKPDERIIKTEYGLLIRSLQKKDSGMYYCKAQ 668
Cdd:cd00096     3 LTCsASGNPPPTITWY--KNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
533-561 9.98e-04

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 37.69  E-value: 9.98e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1863909954 533 RCDTYGkACADCCLARDPYCAWD--GNACSR 561
Cdd:pfam01437   1 RCSQYT-SCSSCLAARDPYCGWCssEGRCVR 30
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
611-680 1.31e-03

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 38.26  E-value: 1.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863909954  611 LECIPKSQ-QATIKWYIQRsgdehREELKPDERIIKTEYG----LLIRSLQKKDSGMYYCKAQ-EHTFIHTIVKLT 680
Cdd:smart00410  14 LSCEASGSpPPEVTWYKQG-----GKLLAESGRFSVSRSGststLTISNVTPEDSGTYTCAATnSSGSASSGTTLT 84
IgV_CD79b_beta cd16096
Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B; The members here are ...
622-666 2.19e-03

Immunoglobulin variable domain (IgV) Cluster of Differentiation (CD) 79B; The members here are composed of the immunoglobulin variable domain (IgV) of the Cluster of Differentiation (CD) 79B (also known as CD79b molecule, immunoglobulin-associated beta (Ig-beta), and B29). The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-beta protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409515  Cd Length: 96  Bit Score: 38.01  E-value: 2.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1863909954 622 IKWYIQRsGDEHREELKPDE-RIIKTE----YGLLIRSLQKKDSGMYYCK 666
Cdd:cd16096    28 MTWFRKK-GNQRPQELFPEDgRISQTQngsvYTLTIQNIQYEDNGIYFCQ 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
611-667 3.15e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.16  E-value: 3.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1863909954 611 LEC-IPKSQQATIKWYiqRSGDEHREELKPDERIIKTEYGLLIRSLQKKDSGMYYCKA 667
Cdd:pfam13927  21 LTCeATGSPPPTITWY--KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
611-669 8.99e-03

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 36.54  E-value: 8.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863909954 611 LECIPKSQQAT--IKWYIQRSG-----------DEHREELKPDERII-----KTEYGLLIRSLQKKDSGMYYCKAQE 669
Cdd:cd00099    18 LSCEVSSSFSStyIYWYRQKPGqgpefliylssSKGKTKGGVPGRFSgsrdgTSSFSLTISNLQPEDSGTYYCAVSE 94
 
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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