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Conserved domains on  [gi|1958767160|ref|XP_038962693|]
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collagen alpha-1(XX) chain isoform X7 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 222-386 4.67e-84

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


:

Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 271.08  E-value: 4.67e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNTF 301
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLDITVH 381
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAV-GVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1958767160  382 NVLDF 386
Cdd:cd01482    160 NVADF 164
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 887-1081 3.81e-29

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: 115.15  E-value: 3.81e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   887 GYDLMMAFGLVAKEYASIRGVAMEPSAfgvaPTFTLFKDAQLMRRVSDVHPATLPPEHTIVFLVRLlpeTPREAFALWQM 966
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGS----PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   967 MAEDFQPILGVLLDAGRKSLTYFNHDSRAALQEITFDlqdAKKIFFGSFHKVHIAVGHSKIRLYVDCRKVAERPIGDAGS 1046
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFR---NLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958767160  1047 PP--TAGFITLGRLAKARGPrsssATFQLQMLQIMCS 1081
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1172-1282 2.46e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 76.87  E-value: 2.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1172 QGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAGLPGPPGPRGFQGLAGASGTSGEQGPPGAVG 1251
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958767160 1252 PTGLPGSKGERGE--KVGRATVPchhlPAGEPG 1282
Cdd:NF038329   214 PDGEAGPAGEDGPagPAGDGQQG----PDGDPG 242
fn3 pfam00041
Fibronectin type III domain;
423-501 2.91e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 2.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  423 PTPTRLTLTHVTSSSIHLSWTPALY---PPLKYLIVWQPSRGG-APKEVVVEGPVSSMELGNLTSNTEYSVSVLPVYESG 498
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1958767160  499 VGK 501
Cdd:pfam00041   81 EGP 83
fn3 pfam00041
Fibronectin type III domain;
797-865 5.32e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 5.32e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958767160  797 TPNSLQVSWAPP---SGHVLHYRLNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGESM 865
Cdd:pfam00041   12 TSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
fn3 pfam00041
Fibronectin type III domain;
692-768 3.21e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  692 PSPSQLSVTELPGDTVKLSWLA-TALSGVLV-YQIKWMPLGEGKA-HEISVPGTLGTAILPGLMKHVEYEITILAYYRDG 768
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPpPDGNGPITgYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
569-874 2.80e-08

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 58.09  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  569 DDLEPGQDYEVSVQSL----RGPEASEARNIHARTPvPGPPRHLSFSDVRYNSTCVSWEAQRPVRLV--KVsYVSSDGSH 642
Cdd:COG3401    197 GDIEPGTTYYYRVAATdtggESAPSNEVSVTTPTTP-PSAPTGLTATADTPGSVTLSWDPVTESDATgyRV-YRSNSGDG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  643 SGQIQVPGNVTSATLGPLSSSTVYTIRVTCFYLRGGSSVLTG--HVTTQKAP--SPSQLSVTELPGDTVKLSWLATALSG 718
Cdd:COG3401    275 PFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNvvSVTTDLTPpaAPSGLTATAVGSSSITLSWTASSDAD 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  719 VLVYQIKWMPLGEGKAHEISVPGTLGTAILPGLMKHVEYEITILAYYRDGTRSDPVSLRYTPSAANRSPPSSLALSSETP 798
Cdd:COG3401    355 VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVP 434

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767160  799 NSLQVSWAPPSGHVLHYrlNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGESMAVSATYRTA 874
Cdd:COG3401    435 LTDVAGATAAASAASNP--GVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNS 508
fn3 pfam00041
Fibronectin type III domain;
522-586 1.83e-07

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 1.83e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767160  522 AVTPRTLHLTWQPSAGA----TQYLVQYllAASTGEEQKREVHVGRPE--VVLDDLEPGQDYEVSVQSLRG 586
Cdd:pfam00041   10 DVTSTSLTVSWTPPPDGngpiTGYEVEY--RPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNG 78
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 222-386 4.67e-84

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 271.08  E-value: 4.67e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNTF 301
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLDITVH 381
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAV-GVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1958767160  382 NVLDF 386
Cdd:cd01482    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
223-392 1.17e-58

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 199.42  E-value: 1.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  223 DIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNT-F 301
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQD-DVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLDITV 380
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAV-GVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|..
gi 1958767160  381 HNVLDFPQLTTL 392
Cdd:pfam00092  160 FTVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 223-392 9.80e-47

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 165.32  E-value: 9.80e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   223 DIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYK-GGNTF 301
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQD---DVRTAARVLKDQDIDVFTVAGVKNVDEAELKLLASQPLDI 378
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|....
gi 1958767160   379 TVHNVLDFPQLTTL 392
Cdd:smart00327  161 YVFLPELLDLLIDL 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 887-1081 3.81e-29

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 115.15  E-value: 3.81e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   887 GYDLMMAFGLVAKEYASIRGVAMEPSAfgvaPTFTLFKDAQLMRRVSDVHPATLPPEHTIVFLVRLlpeTPREAFALWQM 966
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGS----PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   967 MAEDFQPILGVLLDAGRKSLTYFNHDSRAALQEITFDlqdAKKIFFGSFHKVHIAVGHSKIRLYVDCRKVAERPIGDAGS 1046
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFR---NLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958767160  1047 PP--TAGFITLGRLAKARGPrsssATFQLQMLQIMCS 1081
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 130-374 5.54e-20

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 91.15  E-value: 5.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  130 RLAGATLEPPSFPLRDPDSEKTSEPSIAFTSSRDLPILGVASKDQRKLKQGLGVQDSAQPTPDLERQSHTAVSVGKRGKL 209
Cdd:COG1240      1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  210 DDPQFQCTPPTPADIIFLVDGSWS-IGHNNFQQVKDFLASIITHFaigPDKVQVGLTQYSGDPQTEWDLNSfhTKEQVLA 288
Cdd:COG1240     81 LAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  289 AVHHLHYKGGnTftglALTHVLGQNLKPAAGVRPEAAKVLILVTDGK---SQDDVRTAARVLKDQDIDVFTVA-GVKNVD 364
Cdd:COG1240    156 ALDELPPGGG-T----PLGDALALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGvGTEAVD 230

                          250
                   ....*....|
gi 1958767160  365 EAELKLLASQ 374
Cdd:COG1240    231 EGLLREIAEA 240
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1172-1282 2.46e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 76.87  E-value: 2.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1172 QGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAGLPGPPGPRGFQGLAGASGTSGEQGPPGAVG 1251
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958767160 1252 PTGLPGSKGERGE--KVGRATVPchhlPAGEPG 1282
Cdd:NF038329   214 PDGEAGPAGEDGPagPAGDGQQG----PDGDPG 242
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1169-1283 1.87e-13

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.17  E-value: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1169 RAVQGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAGLpgppgprgfQGLAGASGTSGEQGPPG 1248
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP---------QGPAGKDGEAGAKGPAG 189

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958767160 1249 AVGPTGLPGSKGERGE--KVGRATVPCHHLPAGEPGL 1283
Cdd:NF038329   190 EKGPQGPRGETGPAGEqgPAGPAGPDGEAGPAGEDGP 226
fn3 pfam00041
Fibronectin type III domain;
423-501 2.91e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 2.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  423 PTPTRLTLTHVTSSSIHLSWTPALY---PPLKYLIVWQPSRGG-APKEVVVEGPVSSMELGNLTSNTEYSVSVLPVYESG 498
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1958767160  499 VGK 501
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 425-504 2.23e-11

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 61.36  E-value: 2.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  425 PTRLTLTHVTSSSIHLSWTPALY---PPLKYLIVWQPSRGGAPKEVVVE-GPVSSMELGNLTSNTEYSVSVLPVYESGVG 500
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                   ....
gi 1958767160  501 KSLQ 504
Cdd:cd00063     84 PPSE 87
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1122-1282 4.64e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.47  E-value: 4.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1122 QGPPGLPGRNGTPGQQGHPGPKGEPGPPGQTGPEGPGGQQGSPGTQG----RAVQGPMGPPGAKGEKGDHGLPGLQGLSG 1197
Cdd:NF038329   128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGpagkDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1198 QQGIPGKTGLQGPKGMRGLEGPAGLPGppgprgfQGLAGASGTSGEQGPPGAVGPTGLPGSKGERGE--KVGRATVPCHH 1275
Cdd:NF038329   208 PAGPAGPDGEAGPAGEDGPAGPAGDGQ-------QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEagPDGPDGKDGER 280


                   ....*..
gi 1958767160 1276 LPAGEPG 1282
Cdd:NF038329   281 GPVGPAG 287
fn3 pfam00041
Fibronectin type III domain;
797-865 5.32e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 5.32e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958767160  797 TPNSLQVSWAPP---SGHVLHYRLNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGESM 865
Cdd:pfam00041   12 TSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 423-500 2.52e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.01  E-value: 2.52e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   423 PTPTRLTLTHVTSSSIHLSWTPALYP-PLKYLIVWQPSRGGAP---KEVVVEGPVSSMELGNLTSNTEYSVSVLPVYESG 498
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1958767160   499 VG 500
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
692-768 3.21e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  692 PSPSQLSVTELPGDTVKLSWLA-TALSGVLV-YQIKWMPLGEGKA-HEISVPGTLGTAILPGLMKHVEYEITILAYYRDG 768
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPpPDGNGPITgYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 797-864 3.72e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 3.72e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767160  797 TPNSLQVSWAPPS---GHVLHYRLNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGES 864
Cdd:cd00063     13 TSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 797-864 2.06e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.62  E-value: 2.06e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958767160   797 TPNSLQVSWAPPS-----GHVLHYRLNYTlaSGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGES 864
Cdd:smart00060   13 TSTSVTLSWEPPPddgitGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
569-874 2.80e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 58.09  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  569 DDLEPGQDYEVSVQSL----RGPEASEARNIHARTPvPGPPRHLSFSDVRYNSTCVSWEAQRPVRLV--KVsYVSSDGSH 642
Cdd:COG3401    197 GDIEPGTTYYYRVAATdtggESAPSNEVSVTTPTTP-PSAPTGLTATADTPGSVTLSWDPVTESDATgyRV-YRSNSGDG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  643 SGQIQVPGNVTSATLGPLSSSTVYTIRVTCFYLRGGSSVLTG--HVTTQKAP--SPSQLSVTELPGDTVKLSWLATALSG 718
Cdd:COG3401    275 PFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNvvSVTTDLTPpaAPSGLTATAVGSSSITLSWTASSDAD 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  719 VLVYQIKWMPLGEGKAHEISVPGTLGTAILPGLMKHVEYEITILAYYRDGTRSDPVSLRYTPSAANRSPPSSLALSSETP 798
Cdd:COG3401    355 VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVP 434

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767160  799 NSLQVSWAPPSGHVLHYrlNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGESMAVSATYRTA 874
Cdd:COG3401    435 LTDVAGATAAASAASNP--GVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNS 508
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1172-1215 3.93e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.96  E-value: 3.93e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958767160 1172 QGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRG 1215
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 694-775 1.62e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.57  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  694 PSQLSVTELPGDTVKLSWLATALSG--VLVYQIKWMPLGEGKAHEISV-PGTLGTAILPGLMKHVEYEITILAYYRDGtR 770
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG-E 82


                   ....*
gi 1958767160  771 SDPVS 775
Cdd:cd00063     83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
522-586 1.83e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 1.83e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767160  522 AVTPRTLHLTWQPSAGA----TQYLVQYllAASTGEEQKREVHVGRPE--VVLDDLEPGQDYEVSVQSLRG 586
Cdd:pfam00041   10 DVTSTSLTVSWTPPPDGngpiTGYEVEY--RPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNG 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 522-582 3.94e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 3.94e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958767160   522 AVTPRTLHLTWQP--SAGATQYLVQYLLAASTGEEQKREVHV--GRPEVVLDDLEPGQDYEVSVQ 582
Cdd:smart00060   11 DVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVR 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 522-591 4.56e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 4.56e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958767160  522 AVTPRTLHLTWQPSAGA----TQYLVQYLLAASTGEEQKREVHVGRPEVVLDDLEPGQDYEVSVQSLRGPEASE 591
Cdd:cd00063     11 DVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84
fn3 pfam00041
Fibronectin type III domain;
603-671 4.63e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.95  E-value: 4.63e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958767160  603 GPPRHLSFSDVRYNSTCVSWEA----QRPVRLVKVSYVSSDGSHSGQ-IQVPGNVTSATLGPLSSSTVYTIRVT 671
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQ 74
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 602-688 6.60e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.65  E-value: 6.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  602 PGPPRHLSFSDVRYNSTCVSWEA----QRPVRLVKVSYVSSDGSHSGQIQV-PGNVTSATLGPLSSSTVYTIRVTCFYLR 676
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1958767160  677 G-GSSVLTGHVTT 688
Cdd:cd00063     81 GeSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 602-679 1.64e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.22  E-value: 1.64e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   602 PGPPRHLSFSDVRYNSTCVSWEAqrPVRLVKVSYV-------SSDGSHSGQIQVPGNVTSATLGPLSSSTVYTIRVTCFY 674
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEP--PPDDGITGYIvgyrveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1958767160   675 LRGGS 679
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 692-768 1.69e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.22  E-value: 1.69e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   692 PSPSQLSVTELPGDTVKLSWLATALSGVLVYQIKWMPLGEGKA---HEISVPGTLGTAILPGLMKHVEYEITILAYYRDG 768
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1170-1263 3.76e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1170 AVQGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAGLPGPPGPRGFQGLAGASGTSGEQGPPGA 1249
Cdd:COG5164     16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95

                           90
                   ....*....|....
gi 1958767160 1250 VGPTGLPGSKGERG 1263
Cdd:COG5164     96 TGGTTPAGDGGATG 109
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
408-498 7.51e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 40.76  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  408 GPVKPAAGTRILDPLPTPTRLTLTHVTSSSIHLSWTPALYPPLK-YLIVWQPSRGGAPKEVVVEGPVSSMELGNLTSNTE 486
Cdd:COG3401    313 APSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTgYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTT 392

                           90
                   ....*....|..
gi 1958767160  487 YSVSVLPVYESG 498
Cdd:COG3401    393 YYYKVTAVDAAG 404
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 222-386 4.67e-84

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 271.08  E-value: 4.67e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNTF 301
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLDITVH 381
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAV-GVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1958767160  382 NVLDF 386
Cdd:cd01482    160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 222-386 8.18e-69

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 228.27  E-value: 8.18e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNTF 301
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLDITVH 381
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAV-GVKNADEEELKQIASDPKELYVF 159


                   ....*
gi 1958767160  382 NVLDF 386
Cdd:cd01472    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
223-392 1.17e-58

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 199.42  E-value: 1.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  223 DIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNT-F 301
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQD-DVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLDITV 380
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAV-GVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|..
gi 1958767160  381 HNVLDFPQLTTL 392
Cdd:pfam00092  160 FTVSDFEALEDL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 222-377 8.35e-54

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 185.19  E-value: 8.35e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGN-T 300
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958767160  301 FTGLALTHVLgQNLKPAAGVRPEAAKVLILVTDGKSQD--DVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLD 377
Cdd:cd01450     81 NTGKALQYAL-EQLFSESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVV-GVGPADEEELREIASCPSE 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 223-392 9.80e-47

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 165.32  E-value: 9.80e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   223 DIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYK-GGNTF 301
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   302 TGLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQD---DVRTAARVLKDQDIDVFTVAGVKNVDEAELKLLASQPLDI 378
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|....
gi 1958767160   379 TVHNVLDFPQLTTL 392
Cdd:smart00327  161 YVFLPELLDLLIDL 174
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 221-402 1.34e-43

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 158.32  E-value: 1.34e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  221 PADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNT 300
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  301 FTGLALTHVLGQNLKPAAGVRPEAA---KVLILVTDGKSQDDVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLD 377
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAV-GVGRADEEELREIASEPLA 160

                          170       180
                   ....*....|....*....|....*
gi 1958767160  378 ITVHNVLDFPQLTTLAPLLSRLICQ 402
Cdd:cd01475    161 DHVFYVEDFSTIEELTKKFQGKICV 185
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 223-392 1.03e-39

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 145.19  E-value: 1.03e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  223 DIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNTFT 302
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  303 GLALTHVLGQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARV--LKDQDIDVFTVA--GVKNVDEA--ELKLLASQPL 376
Cdd:cd01469     82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGvgGHFQRENSreELKTIASKPP 161

                          170
                   ....*....|....*.
gi 1958767160  377 DITVHNVLDFPQLTTL 392
Cdd:cd01469    162 EEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 222-386 3.23e-38

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 140.54  E-value: 3.23e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNTF 301
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  302 -TGLALTHVLGQNLKPAAGVRPEAA--KVLILVTDGKSQDDVRTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQPLdi 378
Cdd:cd01481     81 nTGSALDYVVKNLFTKSAGSRIEEGvpQFLVLITGGKSQDDVERPAVALKRAGIVPFAI-GARNADLAELQQIAFDPS-- 157


                   ....*...
gi 1958767160  379 TVHNVLDF 386
Cdd:cd01481    158 FVFQVSDF 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 222-380 3.09e-29

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 114.97  E-value: 3.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYK-GGNT 300
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  301 FTGLALTHVLgQNLKPAAgvRPEAAKVLILVTDGKSQDD---VRTAARVLKDQDIDVFTVAGVKNVDEAELKLLASQPLD 377
Cdd:cd00198     81 NIGAALRLAL-ELLKSAK--RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDDANEDELKEIADKTTG 157


                   ...
gi 1958767160  378 ITV 380
Cdd:cd00198    158 GAV 160
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 887-1081 3.81e-29

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 115.15  E-value: 3.81e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   887 GYDLMMAFGLVAKEYASIRGVAMEPSAfgvaPTFTLFKDAQLMRRVSDVHPATLPPEHTIVFLVRLlpeTPREAFALWQM 966
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGS----PAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   967 MAEDFQPILGVLLDAGRKSLTYFNHDSRAALQEITFDlqdAKKIFFGSFHKVHIAVGHSKIRLYVDCRKVAERPIGDAGS 1046
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFR---NLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1958767160  1047 PP--TAGFITLGRLAKARGPrsssATFQLQMLQIMCS 1081
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 222-372 1.41e-28

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 112.88  E-value: 1.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNnFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQT--EWDLNSFHTKEQVLAAVHHLHYKGGN 299
Cdd:cd01476      1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767160  300 TFTGLALTHVLgQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARVLKDQ-DIDVFTVA--GVKNVDEAELKLLA 372
Cdd:cd01476     80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGtgDPGTVDTEELHSIT 154
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 223-377 9.49e-25

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 102.85  E-value: 9.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  223 DIIFLVDGSWSIG-HNNFQQVKDFLASIITHFAIGPDKVQVGLTQYSGDPQTEWDLNSFHT--KEQVLAAVHHL---HYK 296
Cdd:cd01471      2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALlslYYP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  297 GGNTFTGLALTHVLgQNLKPAAGVRPEAAKVLILVTDGKSQDDVRT--AARVLKDQDIdVFTVAGV-KNVDEAELKLLAS 373
Cdd:cd01471     82 NGSTNTTSALLVVE-KHLFDTRGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGV-IIAVLGVgQGVNHEENRSLVG 159


                   ....
gi 1958767160  374 QPLD 377
Cdd:cd01471    160 CDPD 163
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 130-374 5.54e-20

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 91.15  E-value: 5.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  130 RLAGATLEPPSFPLRDPDSEKTSEPSIAFTSSRDLPILGVASKDQRKLKQGLGVQDSAQPTPDLERQSHTAVSVGKRGKL 209
Cdd:COG1240      1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  210 DDPQFQCTPPTPADIIFLVDGSWS-IGHNNFQQVKDFLASIITHFaigPDKVQVGLTQYSGDPQTEWDLNSfhTKEQVLA 288
Cdd:COG1240     81 LAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  289 AVHHLHYKGGnTftglALTHVLGQNLKPAAGVRPEAAKVLILVTDGK---SQDDVRTAARVLKDQDIDVFTVA-GVKNVD 364
Cdd:COG1240    156 ALDELPPGGG-T----PLGDALALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGvGTEAVD 230

                          250
                   ....*....|
gi 1958767160  365 EAELKLLASQ 374
Cdd:COG1240    231 EGLLREIAEA 240
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 221-358 1.30e-17

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 82.05  E-value: 1.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  221 PADIIFLVDGSWSIGHNNFQQVKDFLASIITHF------AIGPDKVQVGLTQYSGDPQTEWDLNSFHTKEQVLA-AVHHL 293
Cdd:cd01480      2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKeAVDNL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958767160  294 HYKGGNTFTGLALTHVLGQNLKpaaGVRPEAAKVLILVTDGKSQ-DDVRTAARVLKDQD---IDVFTVA 358
Cdd:cd01480     82 EYIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgSPDGGIEKAVNEADhlgIKIFFVA 147
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1172-1282 2.46e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 76.87  E-value: 2.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1172 QGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAGLPGPPGPRGFQGLAGASGTSGEQGPPGAVG 1251
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958767160 1252 PTGLPGSKGERGE--KVGRATVPchhlPAGEPG 1282
Cdd:NF038329   214 PDGEAGPAGEDGPagPAGDGQQG----PDGDPG 242
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1169-1283 1.87e-13

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.17  E-value: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1169 RAVQGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAGLpgppgprgfQGLAGASGTSGEQGPPG 1248
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP---------QGPAGKDGEAGAKGPAG 189

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958767160 1249 AVGPTGLPGSKGERGE--KVGRATVPCHHLPAGEPGL 1283
Cdd:NF038329   190 EKGPQGPRGETGPAGEqgPAGPAGPDGEAGPAGEDGP 226
fn3 pfam00041
Fibronectin type III domain;
423-501 2.91e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 2.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  423 PTPTRLTLTHVTSSSIHLSWTPALY---PPLKYLIVWQPSRGG-APKEVVVEGPVSSMELGNLTSNTEYSVSVLPVYESG 498
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1958767160  499 VGK 501
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 425-504 2.23e-11

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 61.36  E-value: 2.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  425 PTRLTLTHVTSSSIHLSWTPALY---PPLKYLIVWQPSRGGAPKEVVVE-GPVSSMELGNLTSNTEYSVSVLPVYESGVG 500
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                   ....
gi 1958767160  501 KSLQ 504
Cdd:cd00063     84 PPSE 87
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1122-1282 4.64e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.47  E-value: 4.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1122 QGPPGLPGRNGTPGQQGHPGPKGEPGPPGQTGPEGPGGQQGSPGTQG----RAVQGPMGPPGAKGEKGDHGLPGLQGLSG 1197
Cdd:NF038329   128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGpagkDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1198 QQGIPGKTGLQGPKGMRGLEGPAGLPGppgprgfQGLAGASGTSGEQGPPGAVGPTGLPGSKGERGE--KVGRATVPCHH 1275
Cdd:NF038329   208 PAGPAGPDGEAGPAGEDGPAGPAGDGQ-------QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEagPDGPDGKDGER 280


                   ....*..
gi 1958767160 1276 LPAGEPG 1282
Cdd:NF038329   281 GPVGPAG 287
fn3 pfam00041
Fibronectin type III domain;
797-865 5.32e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 5.32e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958767160  797 TPNSLQVSWAPP---SGHVLHYRLNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGESM 865
Cdd:pfam00041   12 TSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 423-500 2.52e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.01  E-value: 2.52e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   423 PTPTRLTLTHVTSSSIHLSWTPALYP-PLKYLIVWQPSRGGAP---KEVVVEGPVSSMELGNLTSNTEYSVSVLPVYESG 498
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1958767160   499 VG 500
Cdd:smart00060   82 EG 83
VWA_2 pfam13519
von Willebrand factor type A domain;
224-331 1.13e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.92  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  224 IIFLVDGSWSI-----GHNNFQQVKDFLASIITHFAIgpdkVQVGLTQYSGDPQTEWDLNSfhTKEQVLAAVHHLHYKGG 298
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958767160  299 NTFTGLALTHVLgQNLKpaaGVRPEAAKVLILV 331
Cdd:pfam13519   75 GTNLAAALQLAR-AALK---HRRKNQPRRIVLI 103
fn3 pfam00041
Fibronectin type III domain;
692-768 3.21e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  692 PSPSQLSVTELPGDTVKLSWLA-TALSGVLV-YQIKWMPLGEGKA-HEISVPGTLGTAILPGLMKHVEYEITILAYYRDG 768
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPpPDGNGPITgYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 797-864 3.72e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 3.72e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767160  797 TPNSLQVSWAPPS---GHVLHYRLNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGES 864
Cdd:cd00063     13 TSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
648-890 5.79e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 60.40  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  648 VPGNVTSATLGPLSSSTVYTIRVTCFYLRGGSS---VLTGHVTTQKAPSPSQLSVTELPGDTVKLSWLATALSGVLVYQI 724
Cdd:COG3401    187 VTSTTLVDGGGDIEPGTTYYYRVAATDTGGESApsnEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  725 KWMPLGEGKAHEI-SVPGTlgTAILPGLMKHVEYEITILAYYRDGTRSDP-----VSLRYTPSAANRSPPSSLAlsseTP 798
Cdd:COG3401    267 YRSNSGDGPFTKVaTVTTT--SYTDTGLTNGTTYYYRVTAVDAAGNESAPsnvvsVTTDLTPPAAPSGLTATAV----GS 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  799 NSLQVSWAPPSG-HVLHYRLNYTLASGSGPEKSISVPGTRSHVVlRDLMSAAKYRVLVSAVYGAGESMAVSATYR---TA 874
Cdd:COG3401    341 SSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTD-TGLTPGTTYYYKVTAVDAAGNESAPSEEVSattAS 419

                          250
                   ....*....|....*.
gi 1958767160  875 ACPALHPDSSLSGYDL 890
Cdd:COG3401    420 AASGESLTASVDAVPL 435
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 797-864 2.06e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.62  E-value: 2.06e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958767160   797 TPNSLQVSWAPPS-----GHVLHYRLNYTlaSGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGES 864
Cdd:smart00060   13 TSTSVTLSWEPPPddgitGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
569-874 2.80e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 58.09  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  569 DDLEPGQDYEVSVQSL----RGPEASEARNIHARTPvPGPPRHLSFSDVRYNSTCVSWEAQRPVRLV--KVsYVSSDGSH 642
Cdd:COG3401    197 GDIEPGTTYYYRVAATdtggESAPSNEVSVTTPTTP-PSAPTGLTATADTPGSVTLSWDPVTESDATgyRV-YRSNSGDG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  643 SGQIQVPGNVTSATLGPLSSSTVYTIRVTCFYLRGGSSVLTG--HVTTQKAP--SPSQLSVTELPGDTVKLSWLATALSG 718
Cdd:COG3401    275 PFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNvvSVTTDLTPpaAPSGLTATAVGSSSITLSWTASSDAD 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  719 VLVYQIKWMPLGEGKAHEISVPGTLGTAILPGLMKHVEYEITILAYYRDGTRSDPVSLRYTPSAANRSPPSSLALSSETP 798
Cdd:COG3401    355 VTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVP 434

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958767160  799 NSLQVSWAPPSGHVLHYrlNYTLASGSGPEKSISVPGTRSHVVLRDLMSAAKYRVLVSAVYGAGESMAVSATYRTA 874
Cdd:COG3401    435 LTDVAGATAAASAASNP--GVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNS 508
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1172-1215 3.93e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.96  E-value: 3.93e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958767160 1172 QGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRG 1215
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 223-372 1.15e-07

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 53.48  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  223 DIIFLVDGSWSIGHNNFQ-QVKDFLASIITHFAIGPDKVQVGLTQYSG---DPQTEWDLNSFHtKEQVLAAVHHL--HYK 296
Cdd:cd01473      2 DLTLILDESASIGYSNWRkDVIPFTEKIINNLNISKDKVHVGILLFAEknrDVVPFSDEERYD-KNELLKKINDLknSYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  297 -GGNTFTGLALTHVLgQNLKPAAGVRPEAAKVLILVTDG----KSQDDVRTAARVLKDQDIDVFtVAGVKNVDEAELKLL 371
Cdd:cd01473     81 sGGETYIVEALKYGL-KNYTKHGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLL-VVGVGAASENKLKLL 158


                   .
gi 1958767160  372 A 372
Cdd:cd01473    159 A 159
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 694-775 1.62e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.57  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  694 PSQLSVTELPGDTVKLSWLATALSG--VLVYQIKWMPLGEGKAHEISV-PGTLGTAILPGLMKHVEYEITILAYYRDGtR 770
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG-E 82


                   ....*
gi 1958767160  771 SDPVS 775
Cdd:cd00063     83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
522-586 1.83e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 1.83e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958767160  522 AVTPRTLHLTWQPSAGA----TQYLVQYllAASTGEEQKREVHVGRPE--VVLDDLEPGQDYEVSVQSLRG 586
Cdd:pfam00041   10 DVTSTSLTVSWTPPPDGngpiTGYEVEY--RPKNSGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNG 78
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1173-1252 2.55e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1173 GPMGPPGAKGEKGDHGLPGlqglsgQQGIPGKTGLQGPkgmrglegpaglpgppgpRGFQGLAGASGTSGEQGPPGAVGP 1252
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPG------PPGPPGPPGPPGE------------------PGPPGPPGPPGPPGPPGAPGAPGP 56
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 522-582 3.94e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 3.94e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958767160   522 AVTPRTLHLTWQP--SAGATQYLVQYLLAASTGEEQKREVHV--GRPEVVLDDLEPGQDYEVSVQ 582
Cdd:smart00060   11 DVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVR 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 522-591 4.56e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 4.56e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958767160  522 AVTPRTLHLTWQPSAGA----TQYLVQYLLAASTGEEQKREVHVGRPEVVLDDLEPGQDYEVSVQSLRGPEASE 591
Cdd:cd00063     11 DVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84
fn3 pfam00041
Fibronectin type III domain;
603-671 4.63e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.95  E-value: 4.63e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958767160  603 GPPRHLSFSDVRYNSTCVSWEA----QRPVRLVKVSYVSSDGSHSGQ-IQVPGNVTSATLGPLSSSTVYTIRVT 671
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQ 74
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 602-688 6.60e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 48.65  E-value: 6.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  602 PGPPRHLSFSDVRYNSTCVSWEA----QRPVRLVKVSYVSSDGSHSGQIQV-PGNVTSATLGPLSSSTVYTIRVTCFYLR 676
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1958767160  677 G-GSSVLTGHVTT 688
Cdd:cd00063     81 GeSPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 602-679 1.64e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.22  E-value: 1.64e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   602 PGPPRHLSFSDVRYNSTCVSWEAqrPVRLVKVSYV-------SSDGSHSGQIQVPGNVTSATLGPLSSSTVYTIRVTCFY 674
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEP--PPDDGITGYIvgyrveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1958767160   675 LRGGS 679
Cdd:smart00060   79 GAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 692-768 1.69e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.22  E-value: 1.69e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160   692 PSPSQLSVTELPGDTVKLSWLATALSGVLVYQIKWMPLGEGKA---HEISVPGTLGTAILPGLMKHVEYEITILAYYRDG 768
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1200-1264 6.89e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 6.89e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958767160 1200 GIPGKTGLQGPKGMRGlegpagLPgppgprgfqGLAGASGTSGEQGPPGAVGPTGLPGSKGERGE 1264
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG------PP---------GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
522-706 3.23e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 44.99  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  522 AVTPRTLHLTWQPSA--GATQYLVQYllaASTGEEQKREVH-VGRPEVVLDDLEPGQDYEVSVQSL--RGPE--ASEARN 594
Cdd:COG3401    243 ADTPGSVTLSWDPVTesDATGYRVYR---SNSGDGPFTKVAtVTTTSYTDTGLTNGTTYYYRVTAVdaAGNEsaPSNVVS 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  595 IHARTPVPGPPRHLSFSDVRYNSTCVSWEAQRPVRLV--KVSYVSSDGSHSGQIQVPGNVTSATLGPLSSSTVYTIRVTC 672
Cdd:COG3401    320 VTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTgyNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTA 399

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958767160  673 FYLRGGSSVLTGHVTTQKAPSPSQLSVTELPGDT 706
Cdd:COG3401    400 VDAAGNESAPSEEVSATTASAASGESLTASVDAV 433
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1206-1282 3.31e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 3.31e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958767160 1206 GLQGPKGMRGlegpagLPgppgprgfqGLAGASGTSGEQGPPGAVGPTGLPGSKGERGekvgratvpchhlPAGEPG 1282
Cdd:pfam01391    1 GPPGPPGPPG------PP---------GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG-------------PPGPPG 49
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 222-375 1.80e-03

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 40.96  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  222 ADIIFLVDGSWSIGHNNFqQVKDFLASIITHFaIGPDkVQVGLTQYSGDPQTEWDLNSFHTKEQVLAAVHHLHYKGGNTF 301
Cdd:cd01474      5 FDLYFVLDKSGSVAANWI-EIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958767160  302 TGLALTHVLGQNLKPAAGVRpEAAKVLILVTDGKSQDDV----RTAARVLKDQDIDVFTVaGVKNVDEAELKLLASQP 375
Cdd:cd01474     82 IHEGLENANEQIFNRNGGGR-ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCV-GVTDFLKSQLINIADSK 157
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1170-1263 3.76e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160 1170 AVQGPMGPPGAKGEKGDHGLPGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAGLPGPPGPRGFQGLAGASGTSGEQGPPGA 1249
Cdd:COG5164     16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95

                           90
                   ....*....|....
gi 1958767160 1250 VGPTGLPGSKGERG 1263
Cdd:COG5164     96 TGGTTPAGDGGATG 109
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
408-498 7.51e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 40.76  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958767160  408 GPVKPAAGTRILDPLPTPTRLTLTHVTSSSIHLSWTPALYPPLK-YLIVWQPSRGGAPKEVVVEGPVSSMELGNLTSNTE 486
Cdd:COG3401    313 APSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTgYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTT 392

                           90
                   ....*....|..
gi 1958767160  487 YSVSVLPVYESG 498
Cdd:COG3401    393 YYYKVTAVDAAG 404
 
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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