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Conserved domains on  [gi|6005902|ref|NP_009043|]
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thrombospondin-3 isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
 741-938 1.81e-121

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.


:

Pssm-ID: 461725  Cd Length: 198  Bit Score: 367.35  E-value: 1.81e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902    741 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFLFSYQDSGRFYVVMWKQTEQTYWQAT 820
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902    821 PFRAVAQPGLQLKAVTSVSGPGEHLRNALWHTGHTPDQVRLLWTDPRNVGWRDKTSYRWQLLHRPQVGYIRVKLYEGPQL 900
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6005902    901 VADSGVIIDTSMRGGRLGVFCFSQENIIWSNLQYRCND 938
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 23-193 4.90e-43

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 154.82  E-value: 4.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902      23 QDLQVIDLLTVGES-RQMV---------------AVAEKIRTAL--LTAGDIYLLSTFRLPPKQGGVLFGLYSRQdNTRW 84
Cdd:smart00210   3 DLLQVFDLPSLSFAiRQVVgpepgspayrlgdpaLVPQPTRDLFpsGLPEDFSLLTTFRQTPKSRGVLFAIYDAQ-NVRQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902      85 LEASVVGKINKVLVRYQREDGKVHAVNLQQAGLADGRTHTVLLRLRGPSrpspaLHLYVDCKLGDQHAgLPALAPiPPAE 164
Cdd:smart00210  82 FGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSS-----ATLYVDCNEIDSRP-LDRPGQ-PPID 154

                          170       180       190
                   ....*....|....*....|....*....|
gi 6005902     165 VDGLEIRTGQKA-YLRMQGFVESMKIILGG 193
Cdd:smart00210 155 TDGIEVRGAQAAdRKPFQGDLQQLKIVCDP 184
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
 227-269 3.40e-24

Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled coil region of TSP-3, which is highly expressed in osteosarcomas and associated with metastasis. TSP-3, along with TSP-5 and type IX collagen, is also expressed in the growth plate and all operate in concert and participate in growth plate organization that directly modulates linear growth. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-3 knockout mice have been shown to display accelerated endochondral ossification and increased trabecular bone in the femoral head.


:

Pssm-ID: 293925  Cd Length: 43  Bit Score: 95.80  E-value: 3.40e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6005902  227 QTKALVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVC 269
Cdd:cd16079   1 HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 551-586 1.06e-11

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


:

Pssm-ID: 367074  Cd Length: 36  Bit Score: 60.07  E-value: 1.06e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6005902    551 KDTDGNGEGDACDNDVDGDGIPNGLDNCPKVPNPLQ 586
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 688-722 7.01e-09

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


:

Pssm-ID: 367074  Cd Length: 36  Bit Score: 51.98  E-value: 7.01e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6005902    688 KDSDGNGVGDVCEDDFDNDAVVDPLDVCPESAEVT 722
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 610-647 7.42e-08

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


:

Pssm-ID: 367074  Cd Length: 36  Bit Score: 49.29  E-value: 7.42e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6005902    610 TDADSDLVGDVCDtnEDSDGDGHQDTKDNCPQLPNSSQ 647
Cdd:pfam02412   1 TDSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 316-351 9.03e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.79  E-value: 9.03e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6005902  316 DINECAHADPCFPGSSCINTMPGFHCEaCPRGYKGT 351
Cdd:cd00054   1 DIDECASGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 457-711 1.09e-07

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 56.07  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   457 TDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 536
Cdd:NF033609 632 SDSDSASDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   537 DAcDNCPNVPNNDQKDTDGNGEGDAcDNDVDGDGipnglDNCPKVPNPLQTDRDEDGVGDAcDSCPEMSNPTQTDADSDL 616
Cdd:NF033609 709 DS-DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDS 780

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   617 VGDvCDTNEDSDGDGHQDT-KDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDGNGV 695
Cdd:NF033609 781 DSD-SDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD 859

                        250
                 ....*....|....*.
gi 6005902   696 GDVCEDDFDNDAVVDP 711
Cdd:NF033609 860 SNSDSESGSNNNVVPP 875
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 378-407 3.91e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 44.13  E-value: 3.91e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 6005902    378 NNGGCDPNSICTNTVGSFKCgPCRLGFLGN 407
Cdd:pfam12947   4 NNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
 741-938 1.81e-121

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.


Pssm-ID: 461725  Cd Length: 198  Bit Score: 367.35  E-value: 1.81e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902    741 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFLFSYQDSGRFYVVMWKQTEQTYWQAT 820
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902    821 PFRAVAQPGLQLKAVTSVSGPGEHLRNALWHTGHTPDQVRLLWTDPRNVGWRDKTSYRWQLLHRPQVGYIRVKLYEGPQL 900
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6005902    901 VADSGVIIDTSMRGGRLGVFCFSQENIIWSNLQYRCND 938
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 23-193 4.90e-43

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 154.82  E-value: 4.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902      23 QDLQVIDLLTVGES-RQMV---------------AVAEKIRTAL--LTAGDIYLLSTFRLPPKQGGVLFGLYSRQdNTRW 84
Cdd:smart00210   3 DLLQVFDLPSLSFAiRQVVgpepgspayrlgdpaLVPQPTRDLFpsGLPEDFSLLTTFRQTPKSRGVLFAIYDAQ-NVRQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902      85 LEASVVGKINKVLVRYQREDGKVHAVNLQQAGLADGRTHTVLLRLRGPSrpspaLHLYVDCKLGDQHAgLPALAPiPPAE 164
Cdd:smart00210  82 FGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSS-----ATLYVDCNEIDSRP-LDRPGQ-PPID 154

                          170       180       190
                   ....*....|....*....|....*....|
gi 6005902     165 VDGLEIRTGQKA-YLRMQGFVESMKIILGG 193
Cdd:smart00210 155 TDGIEVRGAQAAdRKPFQGDLQQLKIVCDP 184
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
 227-269 3.40e-24

Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled coil region of TSP-3, which is highly expressed in osteosarcomas and associated with metastasis. TSP-3, along with TSP-5 and type IX collagen, is also expressed in the growth plate and all operate in concert and participate in growth plate organization that directly modulates linear growth. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-3 knockout mice have been shown to display accelerated endochondral ossification and increased trabecular bone in the femoral head.


Pssm-ID: 293925  Cd Length: 43  Bit Score: 95.80  E-value: 3.40e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6005902  227 QTKALVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVC 269
Cdd:cd16079   1 HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43
COMP pfam11598
Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded ...
 228-270 2.31e-16

Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded coiled-coil domain of cartilage oligomeric matrix protein (COMP). This region has a binding site between two internal rings formed by Leu37 and Thr40


Pssm-ID: 463304  Cd Length: 43  Bit Score: 73.61  E-value: 2.31e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6005902    228 TKALVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVCG 270
Cdd:pfam11598   1 TKQLATQLTQLTQLLKELKDDMRQQVKETSFLRNTIEECQACG 43
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 551-586 1.06e-11

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 367074  Cd Length: 36  Bit Score: 60.07  E-value: 1.06e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6005902    551 KDTDGNGEGDACDNDVDGDGIPNGLDNCPKVPNPLQ 586
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 688-722 7.01e-09

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 367074  Cd Length: 36  Bit Score: 51.98  E-value: 7.01e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6005902    688 KDSDGNGVGDVCEDDFDNDAVVDPLDVCPESAEVT 722
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 610-647 7.42e-08

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 367074  Cd Length: 36  Bit Score: 49.29  E-value: 7.42e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6005902    610 TDADSDLVGDVCDtnEDSDGDGHQDTKDNCPQLPNSSQ 647
Cdd:pfam02412   1 TDSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 316-351 9.03e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.79  E-value: 9.03e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6005902  316 DINECAHADPCFPGSSCINTMPGFHCEaCPRGYKGT 351
Cdd:cd00054   1 DIDECASGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
316-348 1.07e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.78  E-value: 1.07e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 6005902     316 DINECAHADPCFPGSSCINTMPGFHCEaCPRGY 348
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE-CPPGY 32
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 457-711 1.09e-07

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 56.07  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   457 TDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 536
Cdd:NF033609 632 SDSDSASDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   537 DAcDNCPNVPNNDQKDTDGNGEGDAcDNDVDGDGipnglDNCPKVPNPLQTDRDEDGVGDAcDSCPEMSNPTQTDADSDL 616
Cdd:NF033609 709 DS-DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDS 780

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   617 VGDvCDTNEDSDGDGHQDT-KDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDGNGV 695
Cdd:NF033609 781 DSD-SDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD 859

                        250
                 ....*....|....*.
gi 6005902   696 GDVCEDDFDNDAVVDP 711
Cdd:NF033609 860 SNSDSESGSNNNVVPP 875
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 378-407 3.91e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 44.13  E-value: 3.91e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 6005902    378 NNGGCDPNSICTNTVGSFKCgPCRLGFLGN 407
Cdd:pfam12947   4 NNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 449-710 1.55e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 49.14  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   449 AGNGNVCGTDTDIDGYPDQAL---PCMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNK 525
Cdd:NF033609 588 SDSGSDSASDSDSASDSDSASdsdSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 667

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   526 DQQNSDTDSFGDAcDNCPNVPNNDQKDTDGNGEGDA-CDNDVDGDGIPNGlDNCPKVPNPLQTDRDEDGVGDA-CDSCPE 603
Cdd:NF033609 668 SDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSdSDSDSD 745

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   604 MSNPTQTDADSDLVGDvCDTNEDSDGDGHQDTkDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVP 683
Cdd:NF033609 746 SDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 823

                        250       260
                 ....*....|....*....|....*..
gi 6005902   684 NPNQKDSDGNGVGDvCEDDFDNDAVVD 710
Cdd:NF033609 824 SDSDSDSDSDSDSD-SDSDSDSDSDSD 849
EGF_CA smart00179
Calcium-binding EGF-like domain;
370-404 2.29e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 2.29e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 6005902     370 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGF 404
Cdd:smart00179   1 DIDECASGNP--CQNGGTCVNTVGSYRCE-CPPGY 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 370-406 2.42e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 2.42e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6005902  370 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGFLG 406
Cdd:cd00054   1 DIDECASGNP--CQNGGTCVNTVGSYRCS-CPPGYTG 34
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 457-690 3.59e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   457 TDTDIDGYPDQalpcmDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 536
Cdd:NF033609 662 SDSDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 736

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   537 DAcDNCPNVPNNDQKDTDGNGEGDAcDNDVDGDGipnglDNCPKVPNPLQTDRDEDGVGDAcDSCPEMSNPTQTDADSDL 616
Cdd:NF033609 737 DS-DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDS 808

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   617 VGDvCDTNEDSDGDGHQDTkDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPD-----------YVPP-GPDNCRLVPN 684
Cdd:NF033609 809 DSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSnsdsesgsnnnVVPPnSPKNGTNASN 886


                 ....*..
gi 6005902   685 PNQ-KDS 690
Cdd:NF033609 887 KNEaKDS 893
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 526-652 9.86e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 9.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   526 DQQNSDTDSFGDAcDNCPNVPNNDQKDTDGNGEGD-ACDNDVDGDGiPNGLDNCPKVPNPLQTDRDEDGVGD-ACDSCPE 603
Cdd:NF033609 572 DSSNSDSGSDSGS-DSTSDSGSDSASDSDSASDSDsASDSDSASDS-DSASDSDSASDSDSASDSDSASDSDsDSDSDSD 649

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 6005902   604 MSNPTQTDADSDLVGDvCDTNEDSDGDGHQDTkDNCPQLPNSSQLDSDN 652
Cdd:NF033609 650 SDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDS 696
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
 741-938 1.81e-121

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.


Pssm-ID: 461725  Cd Length: 198  Bit Score: 367.35  E-value: 1.81e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902    741 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFLFSYQDSGRFYVVMWKQTEQTYWQAT 820
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902    821 PFRAVAQPGLQLKAVTSVSGPGEHLRNALWHTGHTPDQVRLLWTDPRNVGWRDKTSYRWQLLHRPQVGYIRVKLYEGPQL 900
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6005902    901 VADSGVIIDTSMRGGRLGVFCFSQENIIWSNLQYRCND 938
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 23-193 4.90e-43

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 154.82  E-value: 4.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902      23 QDLQVIDLLTVGES-RQMV---------------AVAEKIRTAL--LTAGDIYLLSTFRLPPKQGGVLFGLYSRQdNTRW 84
Cdd:smart00210   3 DLLQVFDLPSLSFAiRQVVgpepgspayrlgdpaLVPQPTRDLFpsGLPEDFSLLTTFRQTPKSRGVLFAIYDAQ-NVRQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902      85 LEASVVGKINKVLVRYQREDGKVHAVNLQQAGLADGRTHTVLLRLRGPSrpspaLHLYVDCKLGDQHAgLPALAPiPPAE 164
Cdd:smart00210  82 FGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGSS-----ATLYVDCNEIDSRP-LDRPGQ-PPID 154

                          170       180       190
                   ....*....|....*....|....*....|
gi 6005902     165 VDGLEIRTGQKA-YLRMQGFVESMKIILGG 193
Cdd:smart00210 155 TDGIEVRGAQAAdRKPFQGDLQQLKIVCDP 184
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
 227-269 3.40e-24

Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled coil region of TSP-3, which is highly expressed in osteosarcomas and associated with metastasis. TSP-3, along with TSP-5 and type IX collagen, is also expressed in the growth plate and all operate in concert and participate in growth plate organization that directly modulates linear growth. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-3 knockout mice have been shown to display accelerated endochondral ossification and increased trabecular bone in the femoral head.


Pssm-ID: 293925  Cd Length: 43  Bit Score: 95.80  E-value: 3.40e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6005902  227 QTKALVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVC 269
Cdd:cd16079   1 HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43
COMP pfam11598
Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded ...
 228-270 2.31e-16

Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded coiled-coil domain of cartilage oligomeric matrix protein (COMP). This region has a binding site between two internal rings formed by Leu37 and Thr40


Pssm-ID: 463304  Cd Length: 43  Bit Score: 73.61  E-value: 2.31e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6005902    228 TKALVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVCG 270
Cdd:pfam11598   1 TKQLATQLTQLTQLLKELKDDMRQQVKETSFLRNTIEECQACG 43
TSPcc cd16076
Coiled coil region of thrombospondin; This domain family contains coiled coil region of ...
 230-269 3.28e-15

Coiled coil region of thrombospondin; This domain family contains coiled coil region of subgroup B of thrombospondins, comprising TSP-3, TSP-4, and TSP-5, that assemble as pentamers. This region is located adjacent to the N-terminal domain (NTD) of thrombospondin (TSP), that mediates co-translational oligomerization via formation of a left-handed super-helix which binds hydrophilic signaling molecules such as vitamin D3 and vitamin A. Pentameric TSPs are stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end. TSP-5 is also known as cartilage oligomeric matrix protein (COMP). TSPs comprise a conserved family of extracellular, oligomeric, multidomain, calcium-binding glycoproteins. In mammals, they have several complex tissue-specific roles, including activities in wound healing and angiogenesis, connective tissue organization, vessel wall biology, and synaptogenesis, all mechanistically derived from interactions with cell surfaces, cytokines, growth factors, or components of the extracellular matrix (ECM) that together regulate many aspects of cell phenotype. In invertebrates, TSPs may have ancient functions such as bridging activities in cell-cell and cell-ECM interactions. Most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil.


Pssm-ID: 293923  Cd Length: 40  Bit Score: 70.16  E-value: 3.28e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 6005902  230 ALVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVC 269
Cdd:cd16076   1 QLARQLTELNQMLQELREEMRQQVKETAFLRNTIMECQAC 40
TSP-4cc cd16080
Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled ...
 228-270 5.40e-13

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.


Pssm-ID: 293926  Cd Length: 44  Bit Score: 64.10  E-value: 5.40e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6005902  228 TKALVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVCG 270
Cdd:cd16080   2 GRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 551-586 1.06e-11

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 367074  Cd Length: 36  Bit Score: 60.07  E-value: 1.06e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6005902    551 KDTDGNGEGDACDNDVDGDGIPNGLDNCPKVPNPLQ 586
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 688-722 7.01e-09

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 367074  Cd Length: 36  Bit Score: 51.98  E-value: 7.01e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6005902    688 KDSDGNGVGDVCEDDFDNDAVVDPLDVCPESAEVT 722
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 610-647 7.42e-08

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 367074  Cd Length: 36  Bit Score: 49.29  E-value: 7.42e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6005902    610 TDADSDLVGDVCDtnEDSDGDGHQDTKDNCPQLPNSSQ 647
Cdd:pfam02412   1 TDSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 316-351 9.03e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.79  E-value: 9.03e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6005902  316 DINECAHADPCFPGSSCINTMPGFHCEaCPRGYKGT 351
Cdd:cd00054   1 DIDECASGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
316-348 1.07e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 48.78  E-value: 1.07e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 6005902     316 DINECAHADPCFPGSSCINTMPGFHCEaCPRGY 348
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE-CPPGY 32
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 457-711 1.09e-07

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 56.07  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   457 TDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 536
Cdd:NF033609 632 SDSDSASDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   537 DAcDNCPNVPNNDQKDTDGNGEGDAcDNDVDGDGipnglDNCPKVPNPLQTDRDEDGVGDAcDSCPEMSNPTQTDADSDL 616
Cdd:NF033609 709 DS-DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDS 780

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   617 VGDvCDTNEDSDGDGHQDT-KDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDGNGV 695
Cdd:NF033609 781 DSD-SDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD 859

                        250
                 ....*....|....*.
gi 6005902   696 GDVCEDDFDNDAVVDP 711
Cdd:NF033609 860 SNSDSESGSNNNVVPP 875
TSP-5cc cd16077
Coiled coil region of thrombospondin-5 (TSP-5); This family contains the N-terminal coiled ...
 231-269 1.68e-06

Coiled coil region of thrombospondin-5 (TSP-5); This family contains the N-terminal coiled coil region of TSP-5, also known as cartilage oligomeric matrix protein (COMP). It forms a pentameric left-handed coiled coil (COMPcc) with a channel that is a unique carrier for lipophilic compounds. It is known to bind hydrophilic signaling molecules such as vitamin D3 and vitamin A, making it a possible targeted drug delivery system. TSP-5/COMP is expressed in all types of cartilage as well as in the vitreous of the eye, tendons, vascular smooth muscle cells, and heart. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-5 is essential for modulating the phenotypic transition of vascular smooth muscle cells and vascular remodeling. Mutations in TSP-5 result in two different inherited chondrodysplasias and osteoarthritic phenotypes: pseudoachondroplasia and multiple epithelial dysplasia. Deficiency of TSP-5 causes dilated cardiomyopathy (DCM), a common cause of congestive heart failure. Early increase in serum TSP-5 is associated with joint damage progression in patients with rheumatoid arthritis, thus representing a novel indicator of an activated destructive process in the joint.


Pssm-ID: 293924  Cd Length: 43  Bit Score: 45.59  E-value: 1.68e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 6005902  231 LVTQLTLFNQILVELRDDIRDQVKEMSLIRNTIMECQVC 269
Cdd:cd16077   5 MLSEMQETNQALAEVKELLKQQVKEITFLKNTVMECDAC 43
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 378-407 3.91e-06

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 44.13  E-value: 3.91e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 6005902    378 NNGGCDPNSICTNTVGSFKCgPCRLGFLGN 407
Cdd:pfam12947   4 NNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 449-710 1.55e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 49.14  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   449 AGNGNVCGTDTDIDGYPDQAL---PCMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNK 525
Cdd:NF033609 588 SDSGSDSASDSDSASDSDSASdsdSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 667

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   526 DQQNSDTDSFGDAcDNCPNVPNNDQKDTDGNGEGDA-CDNDVDGDGIPNGlDNCPKVPNPLQTDRDEDGVGDA-CDSCPE 603
Cdd:NF033609 668 SDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSdSDSDSD 745

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   604 MSNPTQTDADSDLVGDvCDTNEDSDGDGHQDTkDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVP 683
Cdd:NF033609 746 SDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 823

                        250       260
                 ....*....|....*....|....*..
gi 6005902   684 NPNQKDSDGNGVGDvCEDDFDNDAVVD 710
Cdd:NF033609 824 SDSDSDSDSDSDSD-SDSDSDSDSDSD 849
EGF_CA smart00179
Calcium-binding EGF-like domain;
370-404 2.29e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 2.29e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 6005902     370 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGF 404
Cdd:smart00179   1 DIDECASGNP--CQNGGTCVNTVGSYRCE-CPPGY 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 370-406 2.42e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 42.24  E-value: 2.42e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6005902  370 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGFLG 406
Cdd:cd00054   1 DIDECASGNP--CQNGGTCVNTVGSYRCS-CPPGYTG 34
EGF_CA pfam07645
Calcium-binding EGF domain;
370-397 5.04e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.07  E-value: 5.04e-05
                          10        20
                  ....*....|....*....|....*...
gi 6005902    370 DIDECNDGNNGgCDPNSICTNTVGSFKC 397
Cdd:pfam07645   1 DVDECATGTHN-CPANTVCVNTIGSFEC 27
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 457-690 3.59e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   457 TDTDIDGYPDQalpcmDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 536
Cdd:NF033609 662 SDSDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 736

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   537 DAcDNCPNVPNNDQKDTDGNGEGDAcDNDVDGDGipnglDNCPKVPNPLQTDRDEDGVGDAcDSCPEMSNPTQTDADSDL 616
Cdd:NF033609 737 DS-DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDS 808

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   617 VGDvCDTNEDSDGDGHQDTkDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPD-----------YVPP-GPDNCRLVPN 684
Cdd:NF033609 809 DSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSnsdsesgsnnnVVPPnSPKNGTNASN 886


                 ....*..
gi 6005902   685 PNQ-KDS 690
Cdd:NF033609 887 KNEaKDS 893
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 319-350 8.47e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.84  E-value: 8.47e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 6005902  319 ECAHADPCFPGSSCINTMPGFHCEaCPRGYKG 350
Cdd:cd00053   1 ECAASNPCSNGGTCVNTPGSYRCV-CPPGYTG 31
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 526-652 9.86e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 9.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6005902   526 DQQNSDTDSFGDAcDNCPNVPNNDQKDTDGNGEGD-ACDNDVDGDGiPNGLDNCPKVPNPLQTDRDEDGVGD-ACDSCPE 603
Cdd:NF033609 572 DSSNSDSGSDSGS-DSTSDSGSDSASDSDSASDSDsASDSDSASDS-DSASDSDSASDSDSASDSDSASDSDsDSDSDSD 649

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 6005902   604 MSNPTQTDADSDLVGDvCDTNEDSDGDGHQDTkDNCPQLPNSSQLDSDN 652
Cdd:NF033609 650 SDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDS 696
 
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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