NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528509861|ref|XP_005170119|]
View 

thrombospondin-3b isoform X1 [Danio rerio]

Protein Classification

LamG domain-containing protein( domain architecture ID 11034754)

LamG (Laminin G) domain-containing protein may serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules; similar to Oncorhynchus mykiss sex hormone-binding globulin beta form that may participate in the local control of ovarian functions in salmonids

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 738-935 9.53e-124

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: 373.51  E-value: 9.53e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  738 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTIHVNTATDDDYVGFIFGYQDSSSFYVVMWKQTEQTYWQNL 817
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  818 PFKALAQPGIQLKAVKSRTGPGEYLRNALWHTGDTTGEVTLLWKDPRNVGWKDRASYRWHLSHRPQVGYIRLRLYEGTAL 897
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 528509861  898 VADSGVVIDSTMRGGRLGVFCFSQENVIWSNLGYRCND 935
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 55-192 9.43e-24

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 99.35  E-value: 9.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861    55 DLYITSTFMLPPKLGGVLFGLYDKQdNKKYLEIAVVGKINKLLVRYLRSDGKAHTVNLQNPALAEGRTQSLILRIGGLrr 134
Cdd:smart00210  53 DFSLLTTFRQTPKSRGVLFAIYDAQ-NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGS-- 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 528509861   135 shiNLELYVNCRLVDSAQGLPSFvGLPSEAESVDVRTGQKS-YARIQGLVESVKLALGG 192
Cdd:smart00210 130 ---SATLYVDCNEIDSRPLDRPG-QPPIDTDGIEVRGAQAAdRKPFQGDLQQLKIVCDP 184
TSPcc super family cl13107
Coiled coil region of thrombospondin; This domain family contains coiled coil region of ...
 226-268 1.87e-22

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: 90.79  E-value: 1.87e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528509861 226 HTKALIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVC 268
Cdd:cd16079    1 HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 549-583 5.72e-12

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: 60.84  E-value: 5.72e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528509861  549 DTDGNGKGDICDTDIDGDGIPNVLDNCPKIPNPMQ 583
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 489-524 1.07e-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: 54.29  E-value: 1.07e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 528509861  489 EDTDGDGIGDQCDEDADGDGIKNVEDNCRLVPNKDQ 524
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 686-719 3.34e-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: 50.06  E-value: 3.34e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 528509861  686 DTDANGVGDVCETDFDNDKVTDLLDACPESAEVT 719
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
gliding_CglD super family cl45602
adventurous gliding motility lipoprotein CglD;
449-705 1.28e-07

adventurous gliding motility lipoprotein CglD;


The actual alignment was detected with superfamily member NF033765:

Pssm-ID: 468178 [Multi-domain]  Cd Length: 1124  Bit Score: 55.71  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  449 GNICGPDSDIDGYPDEPLPCMDNDKHCRADNCANT------------PNSGQEDTDGDGIGDqcdeDADGDGIKNVEDNC 516
Cdd:NF033765   54 GVDPDPDPDPGEVPTDPRDPDNKTKDSDCDGLTDAeefaniyagglkTNPGLRDTDGDGIRD----GVEVGRTSSVNPLC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  517 RLVPNKDQQ------NSDTDSYGdacdncpnVPNGDQlDTDGNGKGDICDT-----DIDGDGIPNVLDNC-------PKI 578
Cdd:NF033765  130 SFIADQDPTsrtspvKADTDGDG--------IPDGLE-DRNRNGRRDPGETdpnaiDSDGDGLSDGEEDTnkngivsPGE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  579 PNPMQTDRDGDGVGDACDScPEVNDPLQSDMDndlvGDVC-DTNKDIDGDGYQDTRDNCPEVPN--SSQLDSDNDGIgde 655
Cdd:NF033765  201 TDPRKRDTDGDGLSDGLEL-KTGTDPLKPDTD----GDTCsDGDEDRNRNGLVDPGETDPKVADcaASIPDADFDGI--- 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528509861  656 cdddddndgipdilppgPDNCRLV--PNPSQIDTDANGVGDVCETDFDNDKV 705
Cdd:NF033765  273 -----------------PDSVEVAtgTNPNNADTDGDGLPDGVEDRNRNGRV 307
EGF_CA smart00179
Calcium-binding EGF-like domain;
368-406 1.20e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 528509861   368 DIDECAELSGsCVPNSVCINTVGSFKCgQCKAGFVGNQT 406
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRC-ECPPGYTDGRN 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 315-350 5.54e-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: 38.39  E-value: 5.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 528509861 315 DIDEC-TVQPCFSAELCVNTAKGFSCQsCPIGFTGPT 350
Cdd:cd00054    1 DIDECaSGNPCQNGGTCVNTVGSYRCS-CPPGYTGRN 36
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
 738-935 9.53e-124

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: 373.51  E-value: 9.53e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  738 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTIHVNTATDDDYVGFIFGYQDSSSFYVVMWKQTEQTYWQNL 817
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  818 PFKALAQPGIQLKAVKSRTGPGEYLRNALWHTGDTTGEVTLLWKDPRNVGWKDRASYRWHLSHRPQVGYIRLRLYEGTAL 897
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 528509861  898 VADSGVVIDSTMRGGRLGVFCFSQENVIWSNLGYRCND 935
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 55-192 9.43e-24

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 99.35  E-value: 9.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861    55 DLYITSTFMLPPKLGGVLFGLYDKQdNKKYLEIAVVGKINKLLVRYLRSDGKAHTVNLQNPALAEGRTQSLILRIGGLrr 134
Cdd:smart00210  53 DFSLLTTFRQTPKSRGVLFAIYDAQ-NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGS-- 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 528509861   135 shiNLELYVNCRLVDSAQGLPSFvGLPSEAESVDVRTGQKS-YARIQGLVESVKLALGG 192
Cdd:smart00210 130 ---SATLYVDCNEIDSRPLDRPG-QPPIDTDGIEVRGAQAAdRKPFQGDLQQLKIVCDP 184
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
 226-268 1.87e-22

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: 90.79  E-value: 1.87e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528509861 226 HTKALIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVC 268
Cdd:cd16079    1 HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43
COMP pfam11598
Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded ...
 227-269 4.16e-14

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: 67.06  E-value: 4.16e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528509861  227 TKALIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVCG 269
Cdd:pfam11598   1 TKQLATQLTQLTQLLKELKDDMRQQVKETSFLRNTIEECQACG 43
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 549-583 5.72e-12

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: 60.84  E-value: 5.72e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528509861  549 DTDGNGKGDICDTDIDGDGIPNVLDNCPKIPNPMQ 583
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 489-524 1.07e-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: 54.29  E-value: 1.07e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 528509861  489 EDTDGDGIGDQCDEDADGDGIKNVEDNCRLVPNKDQ 524
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 686-719 3.34e-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: 50.06  E-value: 3.34e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 528509861  686 DTDANGVGDVCETDFDNDKVTDLLDACPESAEVT 719
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
gliding_CglD NF033765
adventurous gliding motility lipoprotein CglD;
449-705 1.28e-07

adventurous gliding motility lipoprotein CglD;


Pssm-ID: 468178 [Multi-domain]  Cd Length: 1124  Bit Score: 55.71  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  449 GNICGPDSDIDGYPDEPLPCMDNDKHCRADNCANT------------PNSGQEDTDGDGIGDqcdeDADGDGIKNVEDNC 516
Cdd:NF033765   54 GVDPDPDPDPGEVPTDPRDPDNKTKDSDCDGLTDAeefaniyagglkTNPGLRDTDGDGIRD----GVEVGRTSSVNPLC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  517 RLVPNKDQQ------NSDTDSYGdacdncpnVPNGDQlDTDGNGKGDICDT-----DIDGDGIPNVLDNC-------PKI 578
Cdd:NF033765  130 SFIADQDPTsrtspvKADTDGDG--------IPDGLE-DRNRNGRRDPGETdpnaiDSDGDGLSDGEEDTnkngivsPGE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  579 PNPMQTDRDGDGVGDACDScPEVNDPLQSDMDndlvGDVC-DTNKDIDGDGYQDTRDNCPEVPN--SSQLDSDNDGIgde 655
Cdd:NF033765  201 TDPRKRDTDGDGLSDGLEL-KTGTDPLKPDTD----GDTCsDGDEDRNRNGLVDPGETDPKVADcaASIPDADFDGI--- 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528509861  656 cdddddndgipdilppgPDNCRLV--PNPSQIDTDANGVGDVCETDFDNDKV 705
Cdd:NF033765  273 -----------------PDSVEVAtgTNPNNADTDGDGLPDGVEDRNRNGRV 307
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 608-644 2.03e-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: 47.74  E-value: 2.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 528509861  608 DMDNDLVGDVCDtnKDIDGDGYQDTRDNCPEVPNSSQ 644
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 455-690 2.71e-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: 54.53  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 455 DSDIDGYPDEplpcmDNDKHCRADNCANTPNSGQEDTDGDGIGDQcDEDADGDGIKNVEDNCRLVPNKDQqNSDTDSYGD 534
Cdd:NF033609 663 DSDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSD 735

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 535 ACDNCPNVPNGDQlDTDGNGKGDiCDTDIDGDGipnvlDNCPKIPNPMQTDRDGDGVGDAcDSCPEVNDPLQSDMDNDLV 614
Cdd:NF033609 736 SDSDSDSDSDSDS-DSDSDSDSD-SDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD 807

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528509861 615 GDvCDTNKDIDGDGYQDT---RDNCPEVPNSSQLDSDNDGIGDECDDDDDNDGIPDILPPGPDNCRLVPNPSQIDTDAN 690
Cdd:NF033609 808 SD-SDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNAS 885
EGF_CA smart00179
Calcium-binding EGF-like domain;
368-406 1.20e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 528509861   368 DIDECAELSGsCVPNSVCINTVGSFKCgQCKAGFVGNQT 406
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRC-ECPPGYTDGRN 37
EGF_CA pfam07645
Calcium-binding EGF domain;
368-400 2.05e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 2.05e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 528509861  368 DIDECAELSGSCVPNSVCINTVGSFKCgQCKAG 400
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFEC-RCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 368-403 2.11e-06

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: 44.94  E-value: 2.11e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 528509861 368 DIDECAElSGSCVPNSVCINTVGSFKCgQCKAGFVG 403
Cdd:cd00054    1 DIDECAS-GNPCQNGGTCVNTVGSYRC-SCPPGYTG 34
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 448-740 2.35e-06

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: 51.83  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 448 NGNICGPDSDIDGYPDEPlPCMDNDKHCRADNCANTPNSGQEDTDGDGIGDQ-CDEDADGDGIKNVEDNCRLVPNKDQqN 526
Cdd:NF033609 582 SGSDSTSDSGSDSASDSD-SASDSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSDSDSDSDSDSDSDSDS-D 659

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 527 SDTDSYGDA-----CDNCPNVPNGDQLDTDGNGKGDiCDTDIDGDGipnvlDNCPKIPNPMQTDRDGDGVGDAcDSCPEV 601
Cdd:NF033609 660 SDSDSDSDSdsdsdSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDS 732

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 602 NDPLQSDMDNDLVGDvCDTNKDIDGDGYQDTrDNCPEVPNSSQLDSDNDGIGDECDDDDDNDGIPDILPPGPDNcrlvPN 681
Cdd:NF033609 733 DSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS----DS 806

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528509861 682 PSQIDTDANGVGDvCETDFDNDKVTDlLDACPESAEVTMTDFRAFQTVILDPEGDAQID 740
Cdd:NF033609 807 DSDSDSDSDSDSD-SDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD 863
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 315-350 5.54e-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: 38.39  E-value: 5.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 528509861 315 DIDEC-TVQPCFSAELCVNTAKGFSCQsCPIGFTGPT 350
Cdd:cd00054    1 DIDECaSGNPCQNGGTCVNTVGSYRCS-CPPGYTGRN 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
315-347 2.74e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 2.74e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 528509861   315 DIDEC-TVQPCFSAELCVNTAKGFSCQsCPIGFT 347
Cdd:smart00179   1 DIDECaSGNPCQNGGTCVNTVGSYRCE-CPPGYT 33
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
 738-935 9.53e-124

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: 373.51  E-value: 9.53e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  738 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTIHVNTATDDDYVGFIFGYQDSSSFYVVMWKQTEQTYWQNL 817
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  818 PFKALAQPGIQLKAVKSRTGPGEYLRNALWHTGDTTGEVTLLWKDPRNVGWKDRASYRWHLSHRPQVGYIRLRLYEGTAL 897
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 528509861  898 VADSGVVIDSTMRGGRLGVFCFSQENVIWSNLGYRCND 935
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 55-192 9.43e-24

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 99.35  E-value: 9.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861    55 DLYITSTFMLPPKLGGVLFGLYDKQdNKKYLEIAVVGKINKLLVRYLRSDGKAHTVNLQNPALAEGRTQSLILRIGGLrr 134
Cdd:smart00210  53 DFSLLTTFRQTPKSRGVLFAIYDAQ-NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQWHKLALSVSGS-- 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 528509861   135 shiNLELYVNCRLVDSAQGLPSFvGLPSEAESVDVRTGQKS-YARIQGLVESVKLALGG 192
Cdd:smart00210 130 ---SATLYVDCNEIDSRPLDRPG-QPPIDTDGIEVRGAQAAdRKPFQGDLQQLKIVCDP 184
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
 226-268 1.87e-22

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: 90.79  E-value: 1.87e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528509861 226 HTKALIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVC 268
Cdd:cd16079    1 HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43
COMP pfam11598
Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded ...
 227-269 4.16e-14

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: 67.06  E-value: 4.16e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528509861  227 TKALIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVCG 269
Cdd:pfam11598   1 TKQLATQLTQLTQLLKELKDDMRQQVKETSFLRNTIEECQACG 43
TSPcc cd16076
Coiled coil region of thrombospondin; This domain family contains coiled coil region of ...
 229-268 9.47e-14

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: 65.92  E-value: 9.47e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 528509861 229 ALIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVC 268
Cdd:cd16076    1 QLARQLTELNQMLQELREEMRQQVKETAFLRNTIMECQAC 40
TSP-4cc cd16080
Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled ...
 227-269 5.18e-12

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: 61.02  E-value: 5.18e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 528509861 227 TKALIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVCG 269
Cdd:cd16080    2 GRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 549-583 5.72e-12

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: 60.84  E-value: 5.72e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528509861  549 DTDGNGKGDICDTDIDGDGIPNVLDNCPKIPNPMQ 583
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 489-524 1.07e-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: 54.29  E-value: 1.07e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 528509861  489 EDTDGDGIGDQCDEDADGDGIKNVEDNCRLVPNKDQ 524
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 686-719 3.34e-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: 50.06  E-value: 3.34e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 528509861  686 DTDANGVGDVCETDFDNDKVTDLLDACPESAEVT 719
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35
gliding_CglD NF033765
adventurous gliding motility lipoprotein CglD;
449-705 1.28e-07

adventurous gliding motility lipoprotein CglD;


Pssm-ID: 468178 [Multi-domain]  Cd Length: 1124  Bit Score: 55.71  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  449 GNICGPDSDIDGYPDEPLPCMDNDKHCRADNCANT------------PNSGQEDTDGDGIGDqcdeDADGDGIKNVEDNC 516
Cdd:NF033765   54 GVDPDPDPDPGEVPTDPRDPDNKTKDSDCDGLTDAeefaniyagglkTNPGLRDTDGDGIRD----GVEVGRTSSVNPLC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  517 RLVPNKDQQ------NSDTDSYGdacdncpnVPNGDQlDTDGNGKGDICDT-----DIDGDGIPNVLDNC-------PKI 578
Cdd:NF033765  130 SFIADQDPTsrtspvKADTDGDG--------IPDGLE-DRNRNGRRDPGETdpnaiDSDGDGLSDGEEDTnkngivsPGE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861  579 PNPMQTDRDGDGVGDACDScPEVNDPLQSDMDndlvGDVC-DTNKDIDGDGYQDTRDNCPEVPN--SSQLDSDNDGIgde 655
Cdd:NF033765  201 TDPRKRDTDGDGLSDGLEL-KTGTDPLKPDTD----GDTCsDGDEDRNRNGLVDPGETDPKVADcaASIPDADFDGI--- 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528509861  656 cdddddndgipdilppgPDNCRLV--PNPSQIDTDANGVGDVCETDFDNDKV 705
Cdd:NF033765  273 -----------------PDSVEVAtgTNPNNADTDGDGLPDGVEDRNRNGRV 307
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
 608-644 2.03e-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: 47.74  E-value: 2.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 528509861  608 DMDNDLVGDVCDtnKDIDGDGYQDTRDNCPEVPNSSQ 644
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 455-690 2.71e-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: 54.53  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 455 DSDIDGYPDEplpcmDNDKHCRADNCANTPNSGQEDTDGDGIGDQcDEDADGDGIKNVEDNCRLVPNKDQqNSDTDSYGD 534
Cdd:NF033609 663 DSDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSD 735

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 535 ACDNCPNVPNGDQlDTDGNGKGDiCDTDIDGDGipnvlDNCPKIPNPMQTDRDGDGVGDAcDSCPEVNDPLQSDMDNDLV 614
Cdd:NF033609 736 SDSDSDSDSDSDS-DSDSDSDSD-SDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD 807

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528509861 615 GDvCDTNKDIDGDGYQDT---RDNCPEVPNSSQLDSDNDGIGDECDDDDDNDGIPDILPPGPDNCRLVPNPSQIDTDAN 690
Cdd:NF033609 808 SD-SDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNAS 885
EGF_CA smart00179
Calcium-binding EGF-like domain;
368-406 1.20e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 528509861   368 DIDECAELSGsCVPNSVCINTVGSFKCgQCKAGFVGNQT 406
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRC-ECPPGYTDGRN 37
EGF_CA pfam07645
Calcium-binding EGF domain;
368-400 2.05e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 2.05e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 528509861  368 DIDECAELSGSCVPNSVCINTVGSFKCgQCKAG 400
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFEC-RCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 368-403 2.11e-06

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: 44.94  E-value: 2.11e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 528509861 368 DIDECAElSGSCVPNSVCINTVGSFKCgQCKAGFVG 403
Cdd:cd00054    1 DIDECAS-GNPCQNGGTCVNTVGSYRC-SCPPGYTG 34
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 448-740 2.35e-06

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: 51.83  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 448 NGNICGPDSDIDGYPDEPlPCMDNDKHCRADNCANTPNSGQEDTDGDGIGDQ-CDEDADGDGIKNVEDNCRLVPNKDQqN 526
Cdd:NF033609 582 SGSDSTSDSGSDSASDSD-SASDSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSDSDSDSDSDSDSDSDS-D 659

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 527 SDTDSYGDA-----CDNCPNVPNGDQLDTDGNGKGDiCDTDIDGDGipnvlDNCPKIPNPMQTDRDGDGVGDAcDSCPEV 601
Cdd:NF033609 660 SDSDSDSDSdsdsdSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDS-DSDSDS 732

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509861 602 NDPLQSDMDNDLVGDvCDTNKDIDGDGYQDTrDNCPEVPNSSQLDSDNDGIGDECDDDDDNDGIPDILPPGPDNcrlvPN 681
Cdd:NF033609 733 DSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS----DS 806

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528509861 682 PSQIDTDANGVGDvCETDFDNDKVTDlLDACPESAEVTMTDFRAFQTVILDPEGDAQID 740
Cdd:NF033609 807 DSDSDSDSDSDSD-SDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD 863
TSP-5cc cd16077
Coiled coil region of thrombospondin-5 (TSP-5); This family contains the N-terminal coiled ...
 230-268 3.92e-05

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: 41.74  E-value: 3.92e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 528509861 230 LIGQLIIFNQIMGELREDIREQTKEMSLIRNTILECQVC 268
Cdd:cd16077    5 MLSEMQETNQALAEVKELLKQQVKEITFLKNTVMECDAC 43
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 372-404 9.85e-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: 40.27  E-value: 9.85e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 528509861  372 CAELSGSCVPNSVCINTVGSFKCgQCKAGFVGN 404
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 315-350 5.54e-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: 38.39  E-value: 5.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 528509861 315 DIDEC-TVQPCFSAELCVNTAKGFSCQsCPIGFTGPT 350
Cdd:cd00054    1 DIDECaSGNPCQNGGTCVNTVGSYRCS-CPPGYTGRN 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
315-347 2.74e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 2.74e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 528509861   315 DIDEC-TVQPCFSAELCVNTAKGFSCQsCPIGFT 347
Cdd:smart00179   1 DIDECaSGNPCQNGGTCVNTVGSYRCE-CPPGYT 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 371-406 4.04e-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: 35.92  E-value: 4.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 528509861 371 ECAElSGSCVPNSVCINTVGSFKCgQCKAGFVGNQT 406
Cdd:cd00053    1 ECAA-SNPCSNGGTCVNTPGSYRC-VCPPGYTGDRS 34
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH