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Conserved domains on  [gi|767910311|ref|XP_011508238|]
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thrombospondin-3 isoform X9 [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 ...
 489-686 3.74e-122

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: 362.34  E-value: 3.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311  489 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFLFSYQDSGRFYVVMWKQTEQTYWQAT 568
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311  569 PFRAVAQPGLQLKAVTSVSGPGEHLRNALWHTGHTPDQVRLLWTDPRNVGWRDKTSYRWQLLHRPQVGYIRVKLYEGPQL 648
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767910311  649 VADSGVIIDTSMRGGRLGVFCFSQENIIWSNLQYRCND 686
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 296-331 2.98e-10

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: 55.45  E-value: 2.98e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767910311  296 KDTDGNGEGDACDNDVDGDGIPNGLDNCPKVPNPLQ 331
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 436-470 1.19e-07

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: 48.13  E-value: 1.19e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767910311  436 KDSDGNGVGDVCEDDFDNDAVVDPLDVCPESAEVT 470
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 61-96 9.58e-07

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: 45.71  E-value: 9.58e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767910311  61 DINECAHADPCFPGSSCINTMPGFHCEaCPRGYKGT 96
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 359-395 3.42e-06

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: 44.28  E-value: 3.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767910311  359 DADSDLVGDVCDtnEDSDGDGHQDTKDNCPQLPNSSQ 395
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 123-152 3.53e-05

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: 41.05  E-value: 3.53e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 767910311  123 NNGGCDPNSICTNTVGSFKCgPCRLGFLGN 152
Cdd:pfam12947   4 NNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 202-459 4.44e-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.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.83  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 202 TDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 281
Cdd:NF033609 632 SDSDSASDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 282 DAcDNCPNVPNNDQKDTDGNGEGDA-CDNDVDGDGiPNGLDNCPKVPNPLQTDRDEDGVGDACDSCPEMSNPTQVQGDDA 360
Cdd:NF033609 709 DS-DSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 786

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 361 DSDLVGDvCDTNEDSDGDGHQDTkdncpqlpnSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDG 440
Cdd:NF033609 787 DSDSDSD-SDSDSDSDSDSDSDS---------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 856

                        250
                 ....*....|....*....
gi 767910311 441 NGVGDVCEDDFDNDAVVDP 459
Cdd:NF033609 857 ESDSNSDSESGSNNNVVPP 875
TSPcc super family cl13107
Coiled coil region of thrombospondin; This domain family contains coiled coil region of ...
 1-14 7.27e-04

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.


The actual alignment was detected with superfamily member cd16079:

Pssm-ID: 472419  Cd Length: 43  Bit Score: 37.63  E-value: 7.27e-04
                         10
                 ....*....|....
gi 767910311   1 MSLIRNTIMECQVC 14
Cdd:cd16079   30 MSLIRNTIMECQVC 43
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
 489-686 3.74e-122

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: 362.34  E-value: 3.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311  489 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFLFSYQDSGRFYVVMWKQTEQTYWQAT 568
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311  569 PFRAVAQPGLQLKAVTSVSGPGEHLRNALWHTGHTPDQVRLLWTDPRNVGWRDKTSYRWQLLHRPQVGYIRVKLYEGPQL 648
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767910311  649 VADSGVIIDTSMRGGRLGVFCFSQENIIWSNLQYRCND 686
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 296-331 2.98e-10

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: 55.45  E-value: 2.98e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767910311  296 KDTDGNGEGDACDNDVDGDGIPNGLDNCPKVPNPLQ 331
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 436-470 1.19e-07

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: 48.13  E-value: 1.19e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767910311  436 KDSDGNGVGDVCEDDFDNDAVVDPLDVCPESAEVT 470
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 61-96 9.58e-07

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: 45.71  E-value: 9.58e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767910311  61 DINECAHADPCFPGSSCINTMPGFHCEaCPRGYKGT 96
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
61-93 1.15e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 1.15e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767910311    61 DINECAHADPCFPGSSCINTMPGFHCEaCPRGY 93
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE-CPPGY 32
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 359-395 3.42e-06

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: 44.28  E-value: 3.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767910311  359 DADSDLVGDVCDtnEDSDGDGHQDTKDNCPQLPNSSQ 395
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 123-152 3.53e-05

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: 41.05  E-value: 3.53e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 767910311  123 NNGGCDPNSICTNTVGSFKCgPCRLGFLGN 152
Cdd:pfam12947   4 NNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 202-459 4.44e-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: 46.83  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 202 TDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 281
Cdd:NF033609 632 SDSDSASDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 282 DAcDNCPNVPNNDQKDTDGNGEGDA-CDNDVDGDGiPNGLDNCPKVPNPLQTDRDEDGVGDACDSCPEMSNPTQVQGDDA 360
Cdd:NF033609 709 DS-DSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 786

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 361 DSDLVGDvCDTNEDSDGDGHQDTkdncpqlpnSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDG 440
Cdd:NF033609 787 DSDSDSD-SDSDSDSDSDSDSDS---------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 856

                        250
                 ....*....|....*....
gi 767910311 441 NGVGDVCEDDFDNDAVVDP 459
Cdd:NF033609 857 ESDSNSDSESGSNNNVVPP 875
EGF_CA smart00179
Calcium-binding EGF-like domain;
115-149 2.17e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 2.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 767910311   115 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGF 149
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 ...
 115-151 2.29e-04

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: 39.16  E-value: 2.29e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767910311 115 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGFLG 151
Cdd:cd00054    1 DIDECASGNP--CQNGGTCVNTVGSYRCS-CPPGYTG 34
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-458 4.18e-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: 43.74  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 194 AGNGNVCGTDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQ 273
Cdd:NF033609 588 SDSGSDSASDSDSASDSDSA---SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDS 664

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 274 NSDTDSFGDA-CDNCPNVPNNDQKDTDGNGEGDAcDNDVDGDGIPNGlDNCPKVPNPLQTDRDEDGVGDACDSCPEMSNP 352
Cdd:NF033609 665 DSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 353 TQVQGDDADSDLVGDV-CDTNEDSDGDGHQDT-KDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLV 430
Cdd:NF033609 743 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 822

                        250       260
                 ....*....|....*....|....*...
gi 767910311 431 PNPNQKDSDGNGVGDvCEDDFDNDAVVD 458
Cdd:NF033609 823 DSDSDSDSDSDSDSD-SDSDSDSDSDSD 849
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
 1-14 7.27e-04

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: 37.63  E-value: 7.27e-04
                         10
                 ....*....|....
gi 767910311   1 MSLIRNTIMECQVC 14
Cdd:cd16079   30 MSLIRNTIMECQVC 43
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 292-458 9.07e-03

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: 39.51  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 292 NNDQKDTDGNGEGDACDNDVdgdgIPNGLDNcPKVPNPLQTDRDEDGVGDAcDSCPEMSNPTQVQGDDADSDLVGD-VCD 370
Cdd:NF033609 524 DNEVAFNNGSGSGDGIDKPV----VPEQPDE-PGEIEPIPEDSDSDPGSDS-GSDSSNSDSGSDSGSDSTSDSGSDsASD 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 371 TNEDSDGDGHQDTkDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDGNGVGDVCED- 449
Cdd:NF033609 598 SDSASDSDSASDS-DSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDs 676


                 ....*....
gi 767910311 450 DFDNDAVVD 458
Cdd:NF033609 677 DSDSDSDSD 685
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
 489-686 3.74e-122

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: 362.34  E-value: 3.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311  489 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFLFSYQDSGRFYVVMWKQTEQTYWQAT 568
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311  569 PFRAVAQPGLQLKAVTSVSGPGEHLRNALWHTGHTPDQVRLLWTDPRNVGWRDKTSYRWQLLHRPQVGYIRVKLYEGPQL 648
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767910311  649 VADSGVIIDTSMRGGRLGVFCFSQENIIWSNLQYRCND 686
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 296-331 2.98e-10

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: 55.45  E-value: 2.98e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767910311  296 KDTDGNGEGDACDNDVDGDGIPNGLDNCPKVPNPLQ 331
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 436-470 1.19e-07

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: 48.13  E-value: 1.19e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767910311  436 KDSDGNGVGDVCEDDFDNDAVVDPLDVCPESAEVT 470
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 61-96 9.58e-07

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: 45.71  E-value: 9.58e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767910311  61 DINECAHADPCFPGSSCINTMPGFHCEaCPRGYKGT 96
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
61-93 1.15e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 1.15e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767910311    61 DINECAHADPCFPGSSCINTMPGFHCEaCPRGY 93
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE-CPPGY 32
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 359-395 3.42e-06

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: 44.28  E-value: 3.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767910311  359 DADSDLVGDVCDtnEDSDGDGHQDTKDNCPQLPNSSQ 395
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 123-152 3.53e-05

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: 41.05  E-value: 3.53e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 767910311  123 NNGGCDPNSICTNTVGSFKCgPCRLGFLGN 152
Cdd:pfam12947   4 NNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 202-459 4.44e-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: 46.83  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 202 TDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQNSDTDSFG 281
Cdd:NF033609 632 SDSDSASDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 282 DAcDNCPNVPNNDQKDTDGNGEGDA-CDNDVDGDGiPNGLDNCPKVPNPLQTDRDEDGVGDACDSCPEMSNPTQVQGDDA 360
Cdd:NF033609 709 DS-DSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 786

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 361 DSDLVGDvCDTNEDSDGDGHQDTkdncpqlpnSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDG 440
Cdd:NF033609 787 DSDSDSD-SDSDSDSDSDSDSDS---------DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 856

                        250
                 ....*....|....*....
gi 767910311 441 NGVGDVCEDDFDNDAVVDP 459
Cdd:NF033609 857 ESDSNSDSESGSNNNVVPP 875
EGF_CA smart00179
Calcium-binding EGF-like domain;
115-149 2.17e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 2.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 767910311   115 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGF 149
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 ...
 115-151 2.29e-04

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: 39.16  E-value: 2.29e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767910311 115 DIDECNDGNNggCDPNSICTNTVGSFKCGpCRLGFLG 151
Cdd:cd00054    1 DIDECASGNP--CQNGGTCVNTVGSYRCS-CPPGYTG 34
EGF_CA pfam07645
Calcium-binding EGF domain;
115-142 3.86e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 38.37  E-value: 3.86e-04
                          10        20
                  ....*....|....*....|....*...
gi 767910311  115 DIDECNDGNNGgCDPNSICTNTVGSFKC 142
Cdd:pfam07645   1 DVDECATGTHN-CPANTVCVNTIGSFEC 27
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 194-458 4.18e-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: 43.74  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 194 AGNGNVCGTDTDIDGYPDQAlpcMDNNKHCKQDNCLLTPNSGQEDADNDGVGDQCDDDADGDGIKNVEDNCRLFPNKDQQ 273
Cdd:NF033609 588 SDSGSDSASDSDSASDSDSA---SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDS 664

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 274 NSDTDSFGDA-CDNCPNVPNNDQKDTDGNGEGDAcDNDVDGDGIPNGlDNCPKVPNPLQTDRDEDGVGDACDSCPEMSNP 352
Cdd:NF033609 665 DSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 353 TQVQGDDADSDLVGDV-CDTNEDSDGDGHQDT-KDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLV 430
Cdd:NF033609 743 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 822

                        250       260
                 ....*....|....*....|....*...
gi 767910311 431 PNPNQKDSDGNGVGDvCEDDFDNDAVVD 458
Cdd:NF033609 823 DSDSDSDSDSDSDSD-SDSDSDSDSDSD 849
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
 1-14 7.27e-04

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: 37.63  E-value: 7.27e-04
                         10
                 ....*....|....
gi 767910311   1 MSLIRNTIMECQVC 14
Cdd:cd16079   30 MSLIRNTIMECQVC 43
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 64-95 5.45e-03

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: 35.15  E-value: 5.45e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767910311  64 ECAHADPCFPGSSCINTMPGFHCEaCPRGYKG 95
Cdd:cd00053    1 ECAASNPCSNGGTCVNTPGSYRCV-CPPGYTG 31
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 292-458 9.07e-03

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: 39.51  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 292 NNDQKDTDGNGEGDACDNDVdgdgIPNGLDNcPKVPNPLQTDRDEDGVGDAcDSCPEMSNPTQVQGDDADSDLVGD-VCD 370
Cdd:NF033609 524 DNEVAFNNGSGSGDGIDKPV----VPEQPDE-PGEIEPIPEDSDSDPGSDS-GSDSSNSDSGSDSGSDSTSDSGSDsASD 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910311 371 TNEDSDGDGHQDTkDNCPQLPNSSQLDSDNDGLGDECDGDDDNDGIPDYVPPGPDNCRLVPNPNQKDSDGNGVGDVCED- 449
Cdd:NF033609 598 SDSASDSDSASDS-DSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDs 676


                 ....*....
gi 767910311 450 DFDNDAVVD 458
Cdd:NF033609 677 DSDSDSDSD 685
 
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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