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Conserved domains on  [gi|1207157718|ref|XP_021324387|]
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collagen alpha-1(XII) chain isoform X5 [Danio rerio]

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 ...
 33-196 1.66e-86

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: 279.56  E-value: 1.66e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM 112
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQDEIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPDEIHMYN 192
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1207157718  193 VNDF 196
Cdd:cd01482    161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1705-1869 1.83e-74

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: 245.27  E-value: 1.83e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNT 1784
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1785 KTGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQDDVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSERHVF 1864
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1207157718 1865 VVDDF 1869
Cdd:cd01482    160 NVADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1903-2097 1.11e-42

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 155.21  E-value: 1.11e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1903 GFRMLEAFNLTEKMYASTKGVSMEPGsfnsYTAYRLHKNAFLSQPSSYIHPDGLPSTYTIILMFRLLPDSPneaFDIWQV 1982
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1983 SDKNYKPETGVTIDPSAQSVSFYNKDTTGEIQRATFKNdqvKRIFHGSFHKLHILVSSKSVKLNVDCHEVAEKEIKPAGN 2062
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1207157718  2063 T--STDGFQVLGKMsksiGSKGESATFQLQMFDIVCS 2097
Cdd:smart00210  151 PpiDTDGIEVRGAQ----AADRKPFQGDLQQLKIVCD 183
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2151-2377 9.37e-23

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: 104.22  E-value: 9.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2151 GERGEPGQVGPVGTRGEMGMpgpmgppgpqgpsgRSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIGPVGPAGIRGPP 2230
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGP--------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2231 GKEGPVGPMGPQGAMGPPGAPGMPGPAGKPGKNGDTGVPGLTGVKGD--KGERGDiasqsmmRSIARQVCEQLVNGQMGr 2308
Cdd:NF038329   183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGP-------DGDPGPTGEDGPQGPDG- 254

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207157718 2309 fndmfnqipsnyhsnspgpsgppgppgpqgprgepgRLGRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:NF038329   255 ------------------------------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1499-1576 1.71e-16

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: 76.77  E-value: 1.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1499 APQNLRVSDEWYTRFRVSWDPAP---SPVMGYKLVYQPTTKDESLEV--FVGDVTSYTLHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ...
gi 1207157718 1574 SKP 1576
Cdd:cd00063     83 SPP 85
fn3 pfam00041
Fibronectin type III domain;
592-670 5.76e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 5.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  592 GPPQNLQVFNATTTTLTVKWDHAP---GPVQSYKVTHQPV-AGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRTG 667
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1207157718  668 ESK 670
Cdd:pfam00041   81 EGP 83
fn3 pfam00041
Fibronectin type III domain;
1317-1395 8.17e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 8.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1317 PPRNIKVYNPTPNSLNVRWEPA---SGQVQQYRVAYAPLTGIRPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYADGE 1393
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1394 GP 1395
Cdd:pfam00041   82 GP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 955-1041 1.31e-12

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: 65.60  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  955 GSVRNLQVTDPTISTLNVRWEPAE---GNVREYIVIYVPAGSQD-QEVDQVPGTTTSTVLKNLEPDTTYTVTLVPVYHEM 1030
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1207157718 1031 EGK-SLSENGKT 1041
Cdd:cd00063     82 ESPpSESVTVTT 93
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
465-762 2.77e-12

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: 72.34  E-value: 2.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  465 TEYDVAVTPVYDEGSG---NPMLGTAITDVVPAPKNLRFSEVGQTSFRATWE-HGAPDVGMYRIgwsKKGDRENVKSEIL 540
Cdd:COG3401    203 TTYYYRVAATDTGGESapsNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDpVTESDATGYRV---YRSNSGDGPFTKV 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  541 ARE-ETSHLLTELDPDTEYDVTVTAIYPDESESEDlmgSQrTLSKLITPVPTGPPQNLQVFNATTTTLTVKWDHAPGP-V 618
Cdd:COG3401    280 ATVtTTSYTDTGLTNGTTYYYRVTAVDAAGNESAP---SN-VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdV 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  619 QSYKVTHQPVAGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRTGESKDISGQGRTKPLGGVRNLQVLNPTMTTLN 698
Cdd:COG3401    356 TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPL 435

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207157718  699 VRWEPAEGKVKEYKVVYVPAAGGAESMVGLEQVSGATTNTVLRGLQSDTLYTVTLIPVYAEGEG 762
Cdd:COG3401    436 TDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGG 499
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1409-1485 5.32e-12

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: 64.05  E-value: 5.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1409 PRNMRVFETTTSTISIGWDHAE---GPVQQYKISYASLTGDPITEFTVVPGNRNNAMLQNLHPDTPYNITVTAVYPEGPG 1485
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
fn3 pfam00041
Fibronectin type III domain;
867-944 2.84e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 2.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  867 VRNLRLIDPTFTTLTATWEAA---DGNVQGYKVIYVPTGGGTELMEQ-VSESTTTLVLQKLMPDTMYTVTVLPVYAEGDG 942
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 1207157718  943 PR 944
Cdd:pfam00041   83 PP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 402-480 4.13e-11

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: 61.09  E-value: 4.13e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   402 PLPPaGKLKITEVTHSSMRLTWDA-APGNVRKYIITYKREDGEL----KELEVNGDITTMVLTNLRSQTEYDVAVTPVYD 476
Cdd:smart00060    1 PSPP-SNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEgsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1207157718   477 EGSG 480
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
1136-1215 6.21e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 6.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1136 GSVKNLQVTDPTVNSLRVRWDAA---DGDVRQYNVIYVPVAGGAAGQTQ-VSGMSTNTILRNLQPNTEYKVTVVPVYADA 1211
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718 1212 EGKR 1215
Cdd:pfam00041   81 EGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 775-852 1.30e-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: 57.12  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  775 GGVKNLRVTDPTMTSLNVKWDPAD---GAVRQYKIFFVPAAGGT-EAMETVPGPQNTIVLRNLQPDTVYTVSVVPVYPAT 850
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ..
gi 1207157718  851 EG 852
Cdd:cd00063     82 ES 83
fn3 pfam00041
Fibronectin type III domain;
226-301 4.29e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 4.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  226 DLETSEVTHYSFRATWMPPDE---PVERFRIEYVPAAGGKTEV-LFVDGEENTLVLVNLNPMTEYIVRVYGVIGEESSEP 301
Cdd:pfam00041    5 NLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
1047-1113 6.81e-08

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 6.81e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207157718 1047 VRNLQVTDPTSSTLNVRWEHA---DGNPRNYKVFYIPQ-PGDAEMMELVSGGTTSTVLRNLNANTMYKVTL 1113
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73
fn3 pfam00041
Fibronectin type III domain;
1228-1289 9.07e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 9.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207157718 1228 VKNLQVTDPTTSSLKVRWEPAE---GNVRQYRIFYVPASGGAEDMEQ-VSGGTTNTILRNLLSDTV 1289
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTE 68
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 312-393 1.40e-03

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.


The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  312 PAVTSMSVYDEALTSMRVRWELVKGASGYLLNYN--AINASVPSGMMEMRVGADVNDVQLLQLLPNTAYSISLFALHGEA 389
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEveYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718  390 ASQP 393
Cdd:pfam00041   81 EGPP 84
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1588-1665 8.68e-03

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.


The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain]  Cd Length: 85  Bit Score: 37.39  E-value: 8.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1588 VTNLESYDVGYNRFCIKWTP----HRAATSYRIKLNPVDpSAKGQQEITITASQSQYCFEGLSQDSLYTATVFVQTPNLE 1663
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1664 GP 1665
Cdd:pfam00041   82 GP 83
 
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 ...
 33-196 1.66e-86

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: 279.56  E-value: 1.66e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM 112
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQDEIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPDEIHMYN 192
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1207157718  193 VNDF 196
Cdd:cd01482    161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1705-1869 1.83e-74

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: 245.27  E-value: 1.83e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNT 1784
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1785 KTGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQDDVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSERHVF 1864
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1207157718 1865 VVDDF 1869
Cdd:cd01482    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
34-205 5.74e-63

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 212.91  E-value: 5.74e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   34 DIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM- 112
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQD-EIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPDEIHMY 191
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 1207157718  192 NVNDFSFLLDIVDD 205
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1706-1878 1.04e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.05  E-value: 1.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1706 DVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNTK 1785
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1786 -TGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQD-DVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSERHV 1863
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 1207157718 1864 FVVDDFDAFSTIQDN 1878
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-203 4.16e-48

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: 170.33  E-value: 4.16e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718    34 DIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYK-GGNTM 112
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQD---EIVVNSQRLRDSGIELYAIGVKNA-DENELRSIATDPDEI 188
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 1207157718   189 HMYNVNDFSFLLDIV 203
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1706-1876 4.50e-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: 167.25  E-value: 4.50e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1706 DVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQ-GGNT 1784
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1785 KTGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQD---DVHKNAAKLQHAGYSVFVVGV-ADVDFVELQNIASKPSE 1860
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*.
gi 1207157718  1861 RHVFVVDDFDAFSTIQ 1876
Cdd:smart00327  160 VYVFLPELLDLLIDLL 175
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1903-2097 1.11e-42

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 155.21  E-value: 1.11e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1903 GFRMLEAFNLTEKMYASTKGVSMEPGsfnsYTAYRLHKNAFLSQPSSYIHPDGLPSTYTIILMFRLLPDSPneaFDIWQV 1982
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1983 SDKNYKPETGVTIDPSAQSVSFYNKDTTGEIQRATFKNdqvKRIFHGSFHKLHILVSSKSVKLNVDCHEVAEKEIKPAGN 2062
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1207157718  2063 T--STDGFQVLGKMsksiGSKGESATFQLQMFDIVCS 2097
Cdd:smart00210  151 PpiDTDGIEVRGAQ----AADRKPFQGDLQQLKIVCD 183
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2151-2377 9.37e-23

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: 104.22  E-value: 9.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2151 GERGEPGQVGPVGTRGEMGMpgpmgppgpqgpsgRSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIGPVGPAGIRGPP 2230
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGP--------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2231 GKEGPVGPMGPQGAMGPPGAPGMPGPAGKPGKNGDTGVPGLTGVKGD--KGERGDiasqsmmRSIARQVCEQLVNGQMGr 2308
Cdd:NF038329   183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGP-------DGDPGPTGEDGPQGPDG- 254

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207157718 2309 fndmfnqipsnyhsnspgpsgppgppgpqgprgepgRLGRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:NF038329   255 ------------------------------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2147-2377 3.00e-22

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: 102.68  E-value: 3.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2147 KGPRGERGEPGQVGPVGTRGEMGMPGPMGPPGPQGPSG-RSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIGPVGPAG 2225
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2226 IRGPPGKEGPVGPMGPQgAMGPPGAPGMPGPAGKPGKNGDTGVPGLTGVKGDKGERGDiASQSMMRSIARQVCEQLVNGQ 2305
Cdd:NF038329   214 PDGEAGPAGEDGPAGPA-GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP-DGPDGKDGERGPVGPAGKDGQ 291

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207157718 2306 MGRfndmfNQIPSnyhsnspgpsgppgppgpqgprgepgRLGRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:NF038329   292 NGK-----DGLPG--------------------------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2139-2282 8.25e-17

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: 85.73  E-value: 8.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2139 GPVGAPGSKGPRGERGEPGQVGPVGTRGEMGMPGPMGPPGPQGPSGRSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAI 2218
Cdd:NF038329   180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207157718 2219 GPVGPAGIRGPPGKEGPVGPMGPQGAMGPPGAPGMPGPAGKPGKNGDTGVPGLTGVKGDKGERG 2282
Cdd:NF038329   260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1499-1576 1.71e-16

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: 76.77  E-value: 1.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1499 APQNLRVSDEWYTRFRVSWDPAP---SPVMGYKLVYQPTTKDESLEV--FVGDVTSYTLHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ...
gi 1207157718 1574 SKP 1576
Cdd:cd00063     83 SPP 85
fn3 pfam00041
Fibronectin type III domain;
1499-1576 1.93e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1499 APQNLRVSDEWYTRFRVSWDPAP---SPVMGYKLVYQPTTK-DESLEVFV-GDVTSYTLHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSgEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1207157718 1574 SKP 1576
Cdd:pfam00041   82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
592-670 5.76e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 5.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  592 GPPQNLQVFNATTTTLTVKWDHAP---GPVQSYKVTHQPV-AGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRTG 667
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1207157718  668 ESK 670
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 592-670 1.98e-13

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: 67.91  E-value: 1.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  592 GPPQNLQVFNATTTTLTVKWDHAP---GPVQSYKVTHQPVAGGKPLSVQVG-GKKNSVILQKLTPNTPYTITVAAVYRTG 667
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1207157718  668 ESK 670
Cdd:cd00063     82 ESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1499-1574 5.22e-13

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: 66.48  E-value: 5.22e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1499 APQNLRVSDEWYTRFRVSWDPAP-----SPVMGYKLVYQPTTKDESLEVFVGDVTSYTLHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1207157718  1574 S 1574
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
1317-1395 8.17e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 8.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1317 PPRNIKVYNPTPNSLNVRWEPA---SGQVQQYRVAYAPLTGIRPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYADGE 1393
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1394 GP 1395
Cdd:pfam00041   82 GP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 955-1041 1.31e-12

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: 65.60  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  955 GSVRNLQVTDPTISTLNVRWEPAE---GNVREYIVIYVPAGSQD-QEVDQVPGTTTSTVLKNLEPDTTYTVTLVPVYHEM 1030
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1207157718 1031 EGK-SLSENGKT 1041
Cdd:cd00063     82 ESPpSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
465-762 2.77e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 72.34  E-value: 2.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  465 TEYDVAVTPVYDEGSG---NPMLGTAITDVVPAPKNLRFSEVGQTSFRATWE-HGAPDVGMYRIgwsKKGDRENVKSEIL 540
Cdd:COG3401    203 TTYYYRVAATDTGGESapsNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDpVTESDATGYRV---YRSNSGDGPFTKV 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  541 ARE-ETSHLLTELDPDTEYDVTVTAIYPDESESEDlmgSQrTLSKLITPVPTGPPQNLQVFNATTTTLTVKWDHAPGP-V 618
Cdd:COG3401    280 ATVtTTSYTDTGLTNGTTYYYRVTAVDAAGNESAP---SN-VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdV 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  619 QSYKVTHQPVAGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRTGESKDISGQGRTKPLGGVRNLQVLNPTMTTLN 698
Cdd:COG3401    356 TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPL 435

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207157718  699 VRWEPAEGKVKEYKVVYVPAAGGAESMVGLEQVSGATTNTVLRGLQSDTLYTVTLIPVYAEGEG 762
Cdd:COG3401    436 TDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGG 499
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1409-1485 5.32e-12

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: 64.05  E-value: 5.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1409 PRNMRVFETTTSTISIGWDHAE---GPVQQYKISYASLTGDPITEFTVVPGNRNNAMLQNLHPDTPYNITVTAVYPEGPG 1485
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
fn3 pfam00041
Fibronectin type III domain;
955-1033 8.65e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 8.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  955 GSVRNLQVTDPTISTLNVRWEPAE---GNVREYIVIYVPAGSQDQEVDQ-VPGTTTSTVLKNLEPDTTYTVTLVPVYHEM 1030
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1207157718 1031 EGK 1033
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1317-1395 1.30e-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: 62.90  E-value: 1.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1317 PPRNIKVYNPTPNSLNVRWEPAS---GQVQQYRVAYAPLTGIRPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYADGE 1393
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ..
gi 1207157718 1394 GP 1395
Cdd:cd00063     83 SP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 592-669 2.10e-11

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: 61.86  E-value: 2.10e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   592 GPPQNLQVFNATTTTLTVKWDHAP-----GPVQSYKVTHQPVaGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRT 666
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 1207157718   667 GES 669
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
1409-1486 2.16e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1409 PRNMRVFETTTSTISIGWDHAE---GPVQQYKISYASL-TGDPITEFTVvPGNRNNAMLQNLHPDTPYNITVTAVYPEGP 1484
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITV-PGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1485 GG 1486
Cdd:pfam00041   82 GP 83
fn3 pfam00041
Fibronectin type III domain;
867-944 2.84e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 2.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  867 VRNLRLIDPTFTTLTATWEAA---DGNVQGYKVIYVPTGGGTELMEQ-VSESTTTLVLQKLMPDTMYTVTVLPVYAEGDG 942
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 1207157718  943 PR 944
Cdd:pfam00041   83 PP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 402-480 4.13e-11

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: 61.09  E-value: 4.13e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   402 PLPPaGKLKITEVTHSSMRLTWDA-APGNVRKYIITYKREDGEL----KELEVNGDITTMVLTNLRSQTEYDVAVTPVYD 476
Cdd:smart00060    1 PSPP-SNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEgsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1207157718   477 EGSG 480
Cdd:smart00060   80 AGEG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2204-2281 4.36e-11

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: 60.20  E-value: 4.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207157718 2204 GLPGQKGPPGPTgaiGPVGPAGIRGPPGKEGPVGPMGPqgamgppgapgmpgpagkPGKNGDTGVPGLTGVKGDKGER 2281
Cdd:pfam01391    1 GPPGPPGPPGPP---GPPGPPGPPGPPGPPGPPGEPGP------------------PGPPGPPGPPGPPGAPGAPGPP 57
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 402-482 7.84e-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: 60.59  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  402 PLPPaGKLKITEVTHSSMRLTWDAAP---GNVRKYIITYKRED-GELKELEVN-GDITTMVLTNLRSQTEYDVAVTPVYD 476
Cdd:cd00063      1 PSPP-TNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGsGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   ....*.
gi 1207157718  477 EGSGNP 482
Cdd:cd00063     80 GGESPP 85
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-206 1.65e-10

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: 64.19  E-value: 1.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718    4 RHLAAVALFTLAALTSVRAQGNECKTSAKADIVLLVDGSWSIG---RLNF--KTIRAFIGRMvgvfdigPDKVQIGLAQY 78
Cdd:COG1240     64 AALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaenRLEAakGALLDFLDDY-------RPRDRVGLVAF 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   79 SGDPktewHLNAHPTR--ASLLDAVANLPYKGGnTMTGMALNY---ILQNNfrpnvgmRPDSRKIGVLVTDGK---SQDE 150
Cdd:COG1240    137 GGEA----EVLLPLTRdrEALKRALDELPPGGG-TPLGDALALaleLLKRA-------DPARRKVIVLLTDGRdnaGRID 204

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207157718  151 IVVNSQRLRDSGIELYAIGV--KNADENELRSIAtdpdEI---HMYNVNDFSFLLDIVDDL 206
Cdd:COG1240    205 PLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA----EAtggRYFRADDLSELAAIYREI 261
fn3 pfam00041
Fibronectin type III domain;
493-566 3.60e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 3.60e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718  493 PAPKNLRFSEVGQTSFRATWEHGAPDVG---MYRIGWSKKGDRENVKSEILAREETSHLLTELDPDTEYDVTVTAIY 566
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
fn3 pfam00041
Fibronectin type III domain;
1136-1215 6.21e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 6.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1136 GSVKNLQVTDPTVNSLRVRWDAA---DGDVRQYNVIYVPVAGGAAGQTQ-VSGMSTNTILRNLQPNTEYKVTVVPVYADA 1211
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718 1212 EGKR 1215
Cdd:pfam00041   81 EGPP 84
fn3 pfam00041
Fibronectin type III domain;
404-482 6.85e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 6.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  404 PPAGKLKITEVTHSSMRLTWDAAP---GNVRKYIITYKREDGELKELEVN--GDITTMVLTNLRSQTEYDVAVTPVYDEG 478
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718  479 SGNP 482
Cdd:pfam00041   81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 955-1032 9.19e-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: 57.24  E-value: 9.19e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   955 GSVRNLQVTDPTISTLNVRWE-PAEGNVREYIVIYVPAGSQD---QEVDQVPGTTTSTVLKNLEPDTTYTVTLVPVYHEM 1030
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgseWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718  1031 EG 1032
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1317-1394 1.12e-09

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: 56.85  E-value: 1.12e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1317 PPRNIKVYNPTPNSLNVRWEPAS-----GQVQQYRVAYAPLTGirPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYAD 1391
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGS--EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 1207157718  1392 GEG 1394
Cdd:smart00060   81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 775-852 1.30e-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: 57.12  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  775 GGVKNLRVTDPTMTSLNVKWDPAD---GAVRQYKIFFVPAAGGT-EAMETVPGPQNTIVLRNLQPDTVYTVSVVPVYPAT 850
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ..
gi 1207157718  851 EG 852
Cdd:cd00063     82 ES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 865-943 2.45e-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: 56.35  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  865 GGVRNLRLIDPTFTTLTATWEAAD---GNVQGYKVIYVPTGGGT-ELMEQVSESTTTLVLQKLMPDTMYTVTVLPVYAEG 940
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1207157718  941 DGP 943
Cdd:cd00063     82 ESP 84
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1705-1855 2.62e-09

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: 60.34  E-value: 2.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDES-FSKVIQFVFSVVGAFdvigPTGMQISFVQYSDDANTEFRLNTykDKGTALSALKLIRYqGGN 1783
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY----RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPP-GGG 165

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718 1784 TKTGVALKHVYEKVITVENGMRrnvpKVVVAVTDGR---SQDDVHKNAAKLQHAGYSVFVVGVAD--VDFVELQNIA 1855
Cdd:COG1240    166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIA 238
fn3 pfam00041
Fibronectin type III domain;
226-301 4.29e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 4.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  226 DLETSEVTHYSFRATWMPPDE---PVERFRIEYVPAAGGKTEV-LFVDGEENTLVLVNLNPMTEYIVRVYGVIGEESSEP 301
Cdd:pfam00041    5 NLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 493-566 4.40e-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: 55.58  E-value: 4.40e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718  493 PAPKNLRFSEVGQTSFRATWEHGAPDVGM---YRIGWSKKGDRENVKSEILAREETSHLLTELDPDTEYDVTVTAIY 566
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
fn3 pfam00041
Fibronectin type III domain;
777-854 5.42e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 5.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  777 VKNLRVTDPTMTSLNVKWDPA---DGAVRQYKIFFVPAAGGTEAME-TVPGPQNTIVLRNLQPDTVYTVSVVPVYPATEG 852
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 1207157718  853 RR 854
Cdd:pfam00041   83 PP 84
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2147-2242 6.20e-09

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: 61.07  E-value: 6.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2147 KGPRGERGEPGQVGPVGTRGEMGMPGPMGPPGPQGPSG-------RSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIG 2219
Cdd:NF038329   247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGpagkdgqNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326

                           90       100
                   ....*....|....*....|...
gi 1207157718 2220 PVGPAGIRGPPGKEGPVGPMGPQ 2242
Cdd:NF038329   327 LPGKDGKDGQPGKPAPKTPEVPQ 349
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 493-566 8.04e-09

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: 54.54  E-value: 8.04e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718   493 PAPKNLRFSEVGQTSFRATWEHGAPDVGM-YRIGWSKKGDRENVKSEILAR--EETSHLLTELDPDTEYDVTVTAIY 566
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 226-308 8.20e-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: 54.81  E-value: 8.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  226 DLETSEVTHYSFRATWMPPDE---PVERFRIEYVPAAGGK-TEVLFVDGEENTLVLVNLNPMTEYIVRVYGVIGEESSEP 301
Cdd:cd00063      6 NLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85


                   ....*..
gi 1207157718  302 LKGTETT 308
Cdd:cd00063     86 SESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1136-1214 1.55e-08

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: 54.04  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1136 GSVKNLQVTDPTVNSLRVRWDAADGD---VRQYNVIYVPVAGGAAGQTQVSGMSTNT-ILRNLQPNTEYKVTVVPVYADA 1211
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1207157718 1212 EGK 1214
Cdd:cd00063     82 ESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1409-1485 2.83e-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: 53.00  E-value: 2.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1409 PRNMRVFETTTSTISIGWDHAEGPVQQ-YKISYASLTGDPITEFTVV--PGNRNNAMLQNLHPDTPYNITVTAVYPEGPG 1485
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 775-852 4.40e-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: 4.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   775 GGVKNLRVTDPTMTSLNVKWD-PADGAVRQYKIFFVPA---AGGTEAMETVPGPQNTIVLRNLQPDTVYTVSVVPVYPAT 850
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718   851 EG 852
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
1047-1113 6.81e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 6.81e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207157718 1047 VRNLQVTDPTSSTLNVRWEHA---DGNPRNYKVFYIPQ-PGDAEMMELVSGGTTSTVLRNLNANTMYKVTL 1113
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1136-1213 7.17e-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: 51.85  E-value: 7.17e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1136 GSVKNLQVTDPTVNSLRVRWDAADGDVRQ-YNVIYVPVAGGAAGQTQ---VSGMSTNTILRNLQPNTEYKVTVVPVYADA 1211
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718  1212 EG 1213
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 865-942 1.85e-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: 50.69  E-value: 1.85e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   865 GGVRNLRLIDPTFTTLTATWEA-ADGNVQGYKVIYVPTGGGTELMEQ---VSESTTTLVLQKLMPDTMYTVTVLPVYAEG 940
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718   941 DG 942
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1045-1113 3.81e-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: 49.92  E-value: 3.81e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207157718  1045 GGVRNLQVTDPTSSTLNVRWEH-ADGNPRNYKVFYIPQPGDAEMMEL---VSGGTTSTVLRNLNANTMYKVTL 1113
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRV 74
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1045-1113 1.58e-06

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: 48.26  E-value: 1.58e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207157718 1045 GGVRNLQVTDPTSSTLNVRWEHAD---GNPRNYKVFYIP-QPGDAEMMELVSGGTTSTVLRNLNANTMYKVTL 1113
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREkGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRV 74
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
2188-2377 4.43e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 4.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2188 PGEAGRQGPKGDPGDAGLPGQKG---PPGPTGAIGPVGPAGIRGPPGKEGPVGPMGPQGAMGPPGAPGMPGPAGKPGKNG 2264
Cdd:COG5164     12 SDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTR 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2265 DTGVPGLTGVKGDKGERGDIASQSMMRSIARQVCEQLVNGQMGRFNDMFNQIPSNYHSNSPGPSGPPGPPGPQGPRGEPG 2344
Cdd:COG5164     92 PAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPG 171

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207157718 2345 RLGRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:COG5164    172 GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQG 204
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 226-293 7.60e-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: 46.07  E-value: 7.60e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207157718   226 DLETSEVTHYSFRATWMPPDEP-VERFRIEYVPA---AGGKTEVLFVDGEENTLVLVNLNPMTEYIVRVYGV 293
Cdd:smart00060    6 NLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
1228-1289 9.07e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 9.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207157718 1228 VKNLQVTDPTTSSLKVRWEPAE---GNVRQYRIFYVPASGGAEDMEQ-VSGGTTNTILRNLLSDTV 1289
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTE 68
fn3 pfam00041
Fibronectin type III domain;
312-393 1.40e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  312 PAVTSMSVYDEALTSMRVRWELVKGASGYLLNYN--AINASVPSGMMEMRVGADVNDVQLLQLLPNTAYSISLFALHGEA 389
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEveYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718  390 ASQP 393
Cdd:pfam00041   81 EGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1226-1289 2.60e-03

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: 39.40  E-value: 2.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207157718 1226 GGVKNLQVTDPTTSSLKVRWEPAE---GNVRQYRIFYVPA-SGGAEDMEQVSGGTTNTILRNLLSDTV 1289
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTE 69
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1226-1289 5.01e-03

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: 38.36  E-value: 5.01e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207157718  1226 GGVKNLQVTDPTTSSLKVRWE-PAEGNVRQYRIFYVPASGGAEDMEQ---VSGGTTNTILRNLLSDTV 1289
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTE 69
fn3 pfam00041
Fibronectin type III domain;
1588-1665 8.68e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 37.39  E-value: 8.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1588 VTNLESYDVGYNRFCIKWTP----HRAATSYRIKLNPVDpSAKGQQEITITASQSQYCFEGLSQDSLYTATVFVQTPNLE 1663
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1664 GP 1665
Cdd:pfam00041   82 GP 83
 
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 ...
 33-196 1.66e-86

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: 279.56  E-value: 1.66e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM 112
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQDEIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPDEIHMYN 192
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1207157718  193 VNDF 196
Cdd:cd01482    161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1705-1869 1.83e-74

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: 245.27  E-value: 1.83e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNT 1784
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1785 KTGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQDDVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSERHVF 1864
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1207157718 1865 VVDDF 1869
Cdd:cd01482    160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 33-196 3.24e-74

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: 244.44  E-value: 3.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM 112
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQDEIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPDEIHMYN 192
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                   ....
gi 1207157718  193 VNDF 196
Cdd:cd01472    161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
34-205 5.74e-63

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 212.91  E-value: 5.74e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   34 DIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM- 112
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQD-EIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPDEIHMY 191
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 1207157718  192 NVNDFSFLLDIVDD 205
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1705-1869 1.06e-62

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: 211.70  E-value: 1.06e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNT 1784
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLD-IGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1785 KTGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQDDVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSERHVF 1864
Cdd:cd01472     80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159


                   ....*
gi 1207157718 1865 VVDDF 1869
Cdd:cd01472    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
1706-1878 1.04e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.05  E-value: 1.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1706 DVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNTK 1785
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1786 -TGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQD-DVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSERHV 1863
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 1207157718 1864 FVVDDFDAFSTIQDN 1878
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 33-189 3.64e-52

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: 181.34  E-value: 3.64e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGN-T 111
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  112 MTGMALNYILQNNFRPNvGMRPDSRKIGVLVTDGKSQDEIVVN--SQRLRDSGIELYAIGVKNADENELRSIATDPDEIH 189
Cdd:cd01450     81 NTGKALQYALEQLFSES-NARENVPKVIIVLTDGRSDDGGDPKeaAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1705-1864 6.78e-51

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: 177.48  E-value: 6.78e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGN- 1783
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1784 TKTGVALKHVYEKVITvENGMRRNVPKVVVAVTDGRSQD--DVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSER 1861
Cdd:cd01450     80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                   ...
gi 1207157718 1862 HVF 1864
Cdd:cd01450    159 HVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-203 4.16e-48

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: 170.33  E-value: 4.16e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718    34 DIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYK-GGNTM 112
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   113 TGMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQD---EIVVNSQRLRDSGIELYAIGVKNA-DENELRSIATDPDEI 188
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 1207157718   189 HMYNVNDFSFLLDIV 203
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 33-211 7.08e-48

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: 171.41  E-value: 7.08e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM 112
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 TGMALNYILQNNFRPNVGMRPDSR---KIGVLVTDGKSQDEIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPDEIH 189
Cdd:cd01475     83 TGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                          170       180
                   ....*....|....*....|..
gi 1207157718  190 MYNVNDFSFLLDIVDDLTENLC 211
Cdd:cd01475    163 VFYVEDFSTIEELTKKFQGKIC 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1706-1876 4.50e-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: 167.25  E-value: 4.50e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1706 DVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQ-GGNT 1784
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1785 KTGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQD---DVHKNAAKLQHAGYSVFVVGV-ADVDFVELQNIASKPSE 1860
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*.
gi 1207157718  1861 RHVFVVDDFDAFSTIQ 1876
Cdd:smart00327  160 VYVFLPELLDLLIDLL 175
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1705-1886 2.87e-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: 2.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDViGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNT 1784
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDV-GPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1785 KTGVALKHVYEKVITVENGMR---RNVPKVVVAVTDGRSQDDVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSER 1861
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....*
gi 1207157718 1862 HVFVVDDFDAFSTIQDNLVTFICET 1886
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICVV 186
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 33-196 4.07e-43

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: 155.56  E-value: 4.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTM 112
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  113 -TGMALNYILQNNFRPNVGMR-----PdsrKIGVLVTDGKSQDEIVVNSQRLRDSGIELYAIGVKNADENELRSIATDPD 186
Cdd:cd01481     81 nTGSALDYVVKNLFTKSAGSRieegvP---QFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS 157

                          170
                   ....*....|
gi 1207157718  187 EIhmYNVNDF 196
Cdd:cd01481    158 FV--FQVSDF 165
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1903-2097 1.11e-42

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 155.21  E-value: 1.11e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1903 GFRMLEAFNLTEKMYASTKGVSMEPGsfnsYTAYRLHKNAFLSQPSSYIHPDGLPSTYTIILMFRLLPDSPneaFDIWQV 1982
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSR---GVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1983 SDKNYKPETGVTIDPSAQSVSFYNKDTTGEIQRATFKNdqvKRIFHGSFHKLHILVSSKSVKLNVDCHEVAEKEIKPAGN 2062
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1207157718  2063 T--STDGFQVLGKMsksiGSKGESATFQLQMFDIVCS 2097
Cdd:smart00210  151 PpiDTDGIEVRGAQ----AADRKPFQGDLQQLKIVCD 183
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 34-202 2.04e-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: 145.58  E-value: 2.04e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   34 DIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYKGGNTMT 113
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  114 GMALNYILQNNFRPNVGMRPDSRKIGVLVTDGKSQD----EIVVNSQrlRDSGIELYAIGV-----KNADENELRSIATD 184
Cdd:cd01469     82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQA--EREGIIRYAIGVgghfqRENSREELKTIASK 159

                          170
                   ....*....|....*...
gi 1207157718  185 PDEIHMYNVNDFSFLLDI 202
Cdd:cd01469    160 PPEEHFFNVTDFAALKDI 177
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1706-1875 7.91e-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: 143.65  E-value: 7.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1706 DVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGNTK 1785
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLD-IGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1786 TGVALKHVYEKVITVENGMRRNVPKVVVAVTDGRSQDD--VHKNAAKLQHAGYSVFVVGVADV----DFV-ELQNIASKP 1858
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGGHfqreNSReELKTIASKP 160

                          170
                   ....*....|....*..
gi 1207157718 1859 SERHVFVVDDFDAFSTI 1875
Cdd:cd01469    161 PEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1705-1869 5.26e-36

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: 135.14  E-value: 5.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDViGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQGGN- 1783
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDV-GPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSq 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1784 TKTGVALKHVYEKVITVENG--MRRNVPKVVVAVTDGRSQDDVHKNAAKLQHAGYSVFVVGVADVDFVELQNIASKPSer 1861
Cdd:cd01481     80 LNTGSALDYVVKNLFTKSAGsrIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS-- 157


                   ....*...
gi 1207157718 1862 HVFVVDDF 1869
Cdd:cd01481    158 FVFQVSDF 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 33-191 4.69e-28

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: 112.27  E-value: 4.69e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHPTRASLLDAVANLPYK-GGNT 111
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  112 MTGMALNYILQNNFRPNvgmRPDSRKIGVLVTDGKSQD---EIVVNSQRLRDSGIELYAIGVKN-ADENELRSIATDPDE 187
Cdd:cd00198     81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                   ....
gi 1207157718  188 IHMY 191
Cdd:cd00198    158 GAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1705-1864 1.75e-27

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: 110.73  E-value: 1.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRYQ-GGN 1783
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLS-ASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1784 TKTGVALKHVYEkviTVENGMRRNVPKVVVAVTDGRSQDD---VHKNAAKLQHAGYSVFVVGV-ADVDFVELQNIASKPS 1859
Cdd:cd00198     80 TNIGAALRLALE---LLKSAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTT 156


                   ....*
gi 1207157718 1860 ERHVF 1864
Cdd:cd00198    157 GGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 33-190 9.47e-25

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: 102.86  E-value: 9.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLnFKTIRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKT--EWHLNAHPTRASLLDAVANLPYKGGN 110
Cdd:cd01476      1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  111 TMTGMALNYILQnNFRPNVGMRPDSRKIGVLVTDGKSQDEIVVNSQRLRDS-GIELYAIGVK---NADENELRSIATDPD 186
Cdd:cd01476     80 TATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGNED 158


                   ....
gi 1207157718  187 EIHM 190
Cdd:cd01476    159 HIFT 162
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2151-2377 9.37e-23

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: 104.22  E-value: 9.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2151 GERGEPGQVGPVGTRGEMGMpgpmgppgpqgpsgRSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIGPVGPAGIRGPP 2230
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGP--------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2231 GKEGPVGPMGPQGAMGPPGAPGMPGPAGKPGKNGDTGVPGLTGVKGD--KGERGDiasqsmmRSIARQVCEQLVNGQMGr 2308
Cdd:NF038329   183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGP-------DGDPGPTGEDGPQGPDG- 254

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207157718 2309 fndmfnqipsnyhsnspgpsgppgppgpqgprgepgRLGRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:NF038329   255 ------------------------------------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1705-1864 1.01e-22

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: 97.08  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDEsFSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDD--ANTEFRLNTYKDKGTALSALKLIRYQGG 1782
Cdd:cd01476      1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLE-IGPTATRVALITYSGRgrQRVRFNLPKHNDGEELLEKVDNLRFIGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1783 NTKTGVALKhVYEKVITVENGMRRNVPKVVVAVTDGRSQDDVHKNAAKLQ-HAGYSVFVVGVAD---VDFVELQNIASkp 1858
Cdd:cd01476     79 TTATGAAIE-VALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDpgtVDTEELHSITG-- 155


                   ....*.
gi 1207157718 1859 SERHVF 1864
Cdd:cd01476    156 NEDHIF 161
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2147-2377 3.00e-22

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: 102.68  E-value: 3.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2147 KGPRGERGEPGQVGPVGTRGEMGMPGPMGPPGPQGPSG-RSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIGPVGPAG 2225
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2226 IRGPPGKEGPVGPMGPQgAMGPPGAPGMPGPAGKPGKNGDTGVPGLTGVKGDKGERGDiASQSMMRSIARQVCEQLVNGQ 2305
Cdd:NF038329   214 PDGEAGPAGEDGPAGPA-GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP-DGPDGKDGERGPVGPAGKDGQ 291

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207157718 2306 MGRfndmfNQIPSnyhsnspgpsgppgppgpqgprgepgRLGRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:NF038329   292 NGK-----DGLPG--------------------------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 33-194 1.57e-18

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: 85.90  E-value: 1.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRLNFKTIRAFIGRMVGVF------DIGPDKVQIGLAQYSGDPKTEWHLNAHPT-RASLLDAVANLP 105
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNLE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  106 YKGGNTMTGMALNYILQNNFRpnvGMRPDSRKIGVLVTDGKSQ------DEIVVNS-QRLrdsGIELYAIGVKNADENEL 178
Cdd:cd01480     83 YIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgspdggIEKAVNEaDHL---GIKIFFVAVGSQNEEPL 156

                          170
                   ....*....|....*.
gi 1207157718  179 RSIATDPDEIHmYNVN 194
Cdd:cd01480    157 SRIACDGKSAL-YREN 171
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1700-1884 1.80e-18

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: 85.64  E-value: 1.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1700 CKGAkADVVFLIDGSWSIGDeSFSKVIQFVFSVVGAFDvigPTGMQISFVQYSDDANTEFRLNTYKDK-GTALSALKLIr 1778
Cdd:cd01474      1 CAGH-FDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN---SPGLRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKV- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1779 YQGGNTKTGVALKHVYEKvITVENGMRRNVPKVVVAVTDGRSQDDVHKN----AAKLQHAGYSVFVVGVADVDFVELQNI 1854
Cdd:cd01474     75 TPSGQTYIHEGLENANEQ-IFNRNGGGRETVSVIIALTDGQLLLNGHKYpeheAKLSRKLGAIVYCVGVTDFLKSQLINI 153

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1207157718 1855 ASkpSERHVFVVDD-FDAFSTIQDNLVTFIC 1884
Cdd:cd01474    154 AD--SKEYVFPVTSgFQALSGIIESVVKKAC 182
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 34-187 1.11e-17

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: 83.20  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   34 DIVLLVDGSWSIGRLNFKT-IRAFIGRMVGVFDIGPDKVQIGLAQYSGDPKTEWHLNAHP-----TRASLLDAVANLPYK 107
Cdd:cd01471      2 DLYLLVDGSGSIGYSNWVThVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstnkdLALNAIRALLSLYYP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  108 GGNTMTGMALNYILQ--NNFRPNvgmRPDSRKIGVLVTDGKSQD--EIVVNSQRLRDSGIELYAIGVK---NADENelRS 180
Cdd:cd01471     82 NGSTNTTSALLVVEKhlFDTRGN---RENAPQLVIIMTDGIPDSkfRTLKEARKLRERGVIIAVLGVGqgvNHEEN--RS 156


                   ....*...
gi 1207157718  181 IA-TDPDE 187
Cdd:cd01471    157 LVgCDPDD 164
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1706-1843 4.69e-17

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: 81.28  E-value: 4.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1706 DVVFLIDGSWSIGDES-FSKVIQFVFSVVGAFDvIGPTGMQISFVQYSDDANTEFRLNTY--KDKGTAL---SALKLIRY 1779
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLN-ISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALnaiRALLSLYY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207157718 1780 QGGNTKTGVALKHVyEKVITVENGMRRNVPKVVVAVTDGRSQDDVH--KNAAKLQHAGYSVFVVGV 1843
Cdd:cd01471     81 PNGSTNTTSALLVV-EKHLFDTRGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2139-2282 8.25e-17

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: 85.73  E-value: 8.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2139 GPVGAPGSKGPRGERGEPGQVGPVGTRGEMGMPGPMGPPGPQGPSGRSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAI 2218
Cdd:NF038329   180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207157718 2219 GPVGPAGIRGPPGKEGPVGPMGPQGAMGPPGAPGMPGPAGKPGKNGDTGVPGLTGVKGDKGERG 2282
Cdd:NF038329   260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1499-1576 1.71e-16

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: 76.77  E-value: 1.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1499 APQNLRVSDEWYTRFRVSWDPAP---SPVMGYKLVYQPTTKDESLEV--FVGDVTSYTLHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ...
gi 1207157718 1574 SKP 1576
Cdd:cd00063     83 SPP 85
fn3 pfam00041
Fibronectin type III domain;
1499-1576 1.93e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1499 APQNLRVSDEWYTRFRVSWDPAP---SPVMGYKLVYQPTTK-DESLEVFV-GDVTSYTLHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSgEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1207157718 1574 SKP 1576
Cdd:pfam00041   82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
592-670 5.76e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.37  E-value: 5.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  592 GPPQNLQVFNATTTTLTVKWDHAP---GPVQSYKVTHQPV-AGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRTG 667
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1207157718  668 ESK 670
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 592-670 1.98e-13

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: 67.91  E-value: 1.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  592 GPPQNLQVFNATTTTLTVKWDHAP---GPVQSYKVTHQPVAGGKPLSVQVG-GKKNSVILQKLTPNTPYTITVAAVYRTG 667
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1207157718  668 ESK 670
Cdd:cd00063     82 ESP 84
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1705-1863 2.56e-13

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: 70.49  E-value: 2.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQFVFSVVGAF-----DVIGPTGMQISFVQYSDDANTEF-RLNTYKDKGTALSALKLIR 1778
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1779 YQGGNTKTGVALKHVYEKVItveNGMRRNVPKVVVAVTDGRSQ---DDVHKNAAKL-QHAGYSVFVVGVADVDFVELQNI 1854
Cdd:cd01480     83 YIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgspDGGIEKAVNEaDHLGIKIFFVAVGSQNEEPLSRI 159


                   ....*....
gi 1207157718 1855 ASKPSERHV 1863
Cdd:cd01480    160 ACDGKSALY 168
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1499-1574 5.22e-13

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: 66.48  E-value: 5.22e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1499 APQNLRVSDEWYTRFRVSWDPAP-----SPVMGYKLVYQPTTKDESLEVFVGDVTSYTLHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1207157718  1574 S 1574
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
1317-1395 8.17e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 8.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1317 PPRNIKVYNPTPNSLNVRWEPA---SGQVQQYRVAYAPLTGIRPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYADGE 1393
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1394 GP 1395
Cdd:pfam00041   82 GP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 955-1041 1.31e-12

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: 65.60  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  955 GSVRNLQVTDPTISTLNVRWEPAE---GNVREYIVIYVPAGSQD-QEVDQVPGTTTSTVLKNLEPDTTYTVTLVPVYHEM 1030
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1207157718 1031 EGK-SLSENGKT 1041
Cdd:cd00063     82 ESPpSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
465-762 2.77e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 72.34  E-value: 2.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  465 TEYDVAVTPVYDEGSG---NPMLGTAITDVVPAPKNLRFSEVGQTSFRATWE-HGAPDVGMYRIgwsKKGDRENVKSEIL 540
Cdd:COG3401    203 TTYYYRVAATDTGGESapsNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDpVTESDATGYRV---YRSNSGDGPFTKV 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  541 ARE-ETSHLLTELDPDTEYDVTVTAIYPDESESEDlmgSQrTLSKLITPVPTGPPQNLQVFNATTTTLTVKWDHAPGP-V 618
Cdd:COG3401    280 ATVtTTSYTDTGLTNGTTYYYRVTAVDAAGNESAP---SN-VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdV 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  619 QSYKVTHQPVAGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRTGESKDISGQGRTKPLGGVRNLQVLNPTMTTLN 698
Cdd:COG3401    356 TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPL 435

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207157718  699 VRWEPAEGKVKEYKVVYVPAAGGAESMVGLEQVSGATTNTVLRGLQSDTLYTVTLIPVYAEGEG 762
Cdd:COG3401    436 TDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGG 499
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1409-1485 5.32e-12

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: 64.05  E-value: 5.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1409 PRNMRVFETTTSTISIGWDHAE---GPVQQYKISYASLTGDPITEFTVVPGNRNNAMLQNLHPDTPYNITVTAVYPEGPG 1485
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
fn3 pfam00041
Fibronectin type III domain;
955-1033 8.65e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 8.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  955 GSVRNLQVTDPTISTLNVRWEPAE---GNVREYIVIYVPAGSQDQEVDQ-VPGTTTSTVLKNLEPDTTYTVTLVPVYHEM 1030
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1207157718 1031 EGK 1033
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1317-1395 1.30e-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: 62.90  E-value: 1.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1317 PPRNIKVYNPTPNSLNVRWEPAS---GQVQQYRVAYAPLTGIRPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYADGE 1393
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ..
gi 1207157718 1394 GP 1395
Cdd:cd00063     83 SP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 592-669 2.10e-11

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: 61.86  E-value: 2.10e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   592 GPPQNLQVFNATTTTLTVKWDHAP-----GPVQSYKVTHQPVaGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRT 666
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 1207157718   667 GES 669
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
1409-1486 2.16e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1409 PRNMRVFETTTSTISIGWDHAE---GPVQQYKISYASL-TGDPITEFTVvPGNRNNAMLQNLHPDTPYNITVTAVYPEGP 1484
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITV-PGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1485 GG 1486
Cdd:pfam00041   82 GP 83
fn3 pfam00041
Fibronectin type III domain;
867-944 2.84e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 2.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  867 VRNLRLIDPTFTTLTATWEAA---DGNVQGYKVIYVPTGGGTELMEQ-VSESTTTLVLQKLMPDTMYTVTVLPVYAEGDG 942
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 1207157718  943 PR 944
Cdd:pfam00041   83 PP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 402-480 4.13e-11

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: 61.09  E-value: 4.13e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   402 PLPPaGKLKITEVTHSSMRLTWDA-APGNVRKYIITYKREDGEL----KELEVNGDITTMVLTNLRSQTEYDVAVTPVYD 476
Cdd:smart00060    1 PSPP-SNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEgsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1207157718   477 EGSG 480
Cdd:smart00060   80 AGEG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2204-2281 4.36e-11

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: 60.20  E-value: 4.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207157718 2204 GLPGQKGPPGPTgaiGPVGPAGIRGPPGKEGPVGPMGPqgamgppgapgmpgpagkPGKNGDTGVPGLTGVKGDKGER 2281
Cdd:pfam01391    1 GPPGPPGPPGPP---GPPGPPGPPGPPGPPGPPGEPGP------------------PGPPGPPGPPGPPGAPGAPGPP 57
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 402-482 7.84e-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: 60.59  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  402 PLPPaGKLKITEVTHSSMRLTWDAAP---GNVRKYIITYKRED-GELKELEVN-GDITTMVLTNLRSQTEYDVAVTPVYD 476
Cdd:cd00063      1 PSPP-TNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGsGDWKEVEVTpGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   ....*.
gi 1207157718  477 EGSGNP 482
Cdd:cd00063     80 GGESPP 85
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-206 1.65e-10

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: 64.19  E-value: 1.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718    4 RHLAAVALFTLAALTSVRAQGNECKTSAKADIVLLVDGSWSIG---RLNF--KTIRAFIGRMvgvfdigPDKVQIGLAQY 78
Cdd:COG1240     64 AALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaenRLEAakGALLDFLDDY-------RPRDRVGLVAF 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   79 SGDPktewHLNAHPTR--ASLLDAVANLPYKGGnTMTGMALNY---ILQNNfrpnvgmRPDSRKIGVLVTDGK---SQDE 150
Cdd:COG1240    137 GGEA----EVLLPLTRdrEALKRALDELPPGGG-TPLGDALALaleLLKRA-------DPARRKVIVLLTDGRdnaGRID 204

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207157718  151 IVVNSQRLRDSGIELYAIGV--KNADENELRSIAtdpdEI---HMYNVNDFSFLLDIVDDL 206
Cdd:COG1240    205 PLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA----EAtggRYFRADDLSELAAIYREI 261
VWA_2 pfam13519
von Willebrand factor type A domain;
1707-1815 1.91e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 60.00  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1707 VVFLIDGSWSIGDES-----FSKVIQFVFSVVGAFDvigptGMQISFVQYSDDANTEFRLNtyKDKGTALSALKLIRYQG 1781
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLP-----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1207157718 1782 GNTKTGVALKHVYEkvitVENGMRRNVPKVVVAV 1815
Cdd:pfam13519   74 GGTNLAAALQLARA----ALKHRRKNQPRRIVLI 103
fn3 pfam00041
Fibronectin type III domain;
493-566 3.60e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 3.60e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718  493 PAPKNLRFSEVGQTSFRATWEHGAPDVG---MYRIGWSKKGDRENVKSEILAREETSHLLTELDPDTEYDVTVTAIY 566
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
fn3 pfam00041
Fibronectin type III domain;
1136-1215 6.21e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 6.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1136 GSVKNLQVTDPTVNSLRVRWDAA---DGDVRQYNVIYVPVAGGAAGQTQ-VSGMSTNTILRNLQPNTEYKVTVVPVYADA 1211
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718 1212 EGKR 1215
Cdd:pfam00041   81 EGPP 84
fn3 pfam00041
Fibronectin type III domain;
404-482 6.85e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 6.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  404 PPAGKLKITEVTHSSMRLTWDAAP---GNVRKYIITYKREDGELKELEVN--GDITTMVLTNLRSQTEYDVAVTPVYDEG 478
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718  479 SGNP 482
Cdd:pfam00041   81 EGPP 84
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2198-2270 7.22e-10

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: 56.73  E-value: 7.22e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207157718 2198 GDPGDAGLPGQKGPPGPTGAIGPVGPAGIRGPPGKEGPVGPMGPQgamgppgapgmpgpagkpGKNGDTGVPG 2270
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPP------------------GPPGAPGAPG 55
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 955-1032 9.19e-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: 57.24  E-value: 9.19e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   955 GSVRNLQVTDPTISTLNVRWE-PAEGNVREYIVIYVPAGSQD---QEVDQVPGTTTSTVLKNLEPDTTYTVTLVPVYHEM 1030
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgseWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718  1031 EG 1032
Cdd:smart00060   82 EG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2188-2251 9.50e-10

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: 56.35  E-value: 9.50e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207157718 2188 PGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIGPVGPAGIRGPPGKEGPvgpmgpqgamgppgaP 2251
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA---------------P 51
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1317-1394 1.12e-09

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: 56.85  E-value: 1.12e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1317 PPRNIKVYNPTPNSLNVRWEPAS-----GQVQQYRVAYAPLTGirPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYAD 1391
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGS--EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 1207157718  1392 GEG 1394
Cdd:smart00060   81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 775-852 1.30e-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: 57.12  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  775 GGVKNLRVTDPTMTSLNVKWDPAD---GAVRQYKIFFVPAAGGT-EAMETVPGPQNTIVLRNLQPDTVYTVSVVPVYPAT 850
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ..
gi 1207157718  851 EG 852
Cdd:cd00063     82 ES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 865-943 2.45e-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: 56.35  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  865 GGVRNLRLIDPTFTTLTATWEAAD---GNVQGYKVIYVPTGGGT-ELMEQVSESTTTLVLQKLMPDTMYTVTVLPVYAEG 940
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1207157718  941 DGP 943
Cdd:cd00063     82 ESP 84
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1705-1855 2.62e-09

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: 60.34  E-value: 2.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDES-FSKVIQFVFSVVGAFdvigPTGMQISFVQYSDDANTEFRLNTykDKGTALSALKLIRYqGGN 1783
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY----RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPP-GGG 165

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718 1784 TKTGVALKHVYEKVITVENGMRrnvpKVVVAVTDGR---SQDDVHKNAAKLQHAGYSVFVVGVAD--VDFVELQNIA 1855
Cdd:COG1240    166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIA 238
fn3 pfam00041
Fibronectin type III domain;
226-301 4.29e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 4.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  226 DLETSEVTHYSFRATWMPPDE---PVERFRIEYVPAAGGKTEV-LFVDGEENTLVLVNLNPMTEYIVRVYGVIGEESSEP 301
Cdd:pfam00041    5 NLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 493-566 4.40e-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: 55.58  E-value: 4.40e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718  493 PAPKNLRFSEVGQTSFRATWEHGAPDVGM---YRIGWSKKGDRENVKSEILAREETSHLLTELDPDTEYDVTVTAIY 566
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
fn3 pfam00041
Fibronectin type III domain;
777-854 5.42e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 5.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  777 VKNLRVTDPTMTSLNVKWDPA---DGAVRQYKIFFVPAAGGTEAME-TVPGPQNTIVLRNLQPDTVYTVSVVPVYPATEG 852
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 1207157718  853 RR 854
Cdd:pfam00041   83 PP 84
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2147-2242 6.20e-09

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: 61.07  E-value: 6.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2147 KGPRGERGEPGQVGPVGTRGEMGMPGPMGPPGPQGPSG-------RSIPGEAGRQGPKGDPGDAGLPGQKGPPGPTGAIG 2219
Cdd:NF038329   247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGpagkdgqNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326

                           90       100
                   ....*....|....*....|...
gi 1207157718 2220 PVGPAGIRGPPGKEGPVGPMGPQ 2242
Cdd:NF038329   327 LPGKDGKDGQPGKPAPKTPEVPQ 349
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 493-566 8.04e-09

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: 54.54  E-value: 8.04e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207157718   493 PAPKNLRFSEVGQTSFRATWEHGAPDVGM-YRIGWSKKGDRENVKSEILAR--EETSHLLTELDPDTEYDVTVTAIY 566
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 226-308 8.20e-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: 54.81  E-value: 8.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  226 DLETSEVTHYSFRATWMPPDE---PVERFRIEYVPAAGGK-TEVLFVDGEENTLVLVNLNPMTEYIVRVYGVIGEESSEP 301
Cdd:cd00063      6 NLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPP 85


                   ....*..
gi 1207157718  302 LKGTETT 308
Cdd:cd00063     86 SESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1136-1214 1.55e-08

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: 54.04  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1136 GSVKNLQVTDPTVNSLRVRWDAADGD---VRQYNVIYVPVAGGAAGQTQVSGMSTNT-ILRNLQPNTEYKVTVVPVYADA 1211
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1207157718 1212 EGK 1214
Cdd:cd00063     82 ESP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 682-762 1.94e-08

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: 53.65  E-value: 1.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  682 GGVRNLQVLNPTMTTLNVRWEPAE---GKVKEYKVVYVPAagGAESMVGLEQVSGATTNTVLRGLQSDTLYTVTLIPVYA 758
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREK--GSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 1207157718  759 EGEG 762
Cdd:cd00063     80 GGES 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1409-1485 2.83e-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: 53.00  E-value: 2.83e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1409 PRNMRVFETTTSTISIGWDHAEGPVQQ-YKISYASLTGDPITEFTVV--PGNRNNAMLQNLHPDTPYNITVTAVYPEGPG 1485
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 775-852 4.40e-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: 4.40e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   775 GGVKNLRVTDPTMTSLNVKWD-PADGAVRQYKIFFVPA---AGGTEAMETVPGPQNTIVLRNLQPDTVYTVSVVPVYPAT 850
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718   851 EG 852
Cdd:smart00060   82 EG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2147-2214 4.41e-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: 51.73  E-value: 4.41e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207157718 2147 KGPRGERGEPGQVGPvgtrgemgmpgpmgppgpqgpsgrsiPGEAGRQGPKGDPGDAGLPGQKGPPGP 2214
Cdd:pfam01391   15 PGPPGPPGPPGPPGP--------------------------PGEPGPPGPPGPPGPPGPPGAPGAPGP 56
fn3 pfam00041
Fibronectin type III domain;
1047-1113 6.81e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 6.81e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207157718 1047 VRNLQVTDPTSSTLNVRWEHA---DGNPRNYKVFYIPQ-PGDAEMMELVSGGTTSTVLRNLNANTMYKVTL 1113
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1136-1213 7.17e-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: 51.85  E-value: 7.17e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  1136 GSVKNLQVTDPTVNSLRVRWDAADGDVRQ-YNVIYVPVAGGAAGQTQ---VSGMSTNTILRNLQPNTEYKVTVVPVYADA 1211
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718  1212 EG 1213
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
684-764 1.19e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.26  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  684 VRNLQVLNPTMTTLNVRWEPAE---GKVKEYKVVYVPAAGGAESMVglEQVSGATTNTVLRGLQSDTLYTVTLIPVYAEG 760
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNE--ITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718  761 EGQR 764
Cdd:pfam00041   81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 865-942 1.85e-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: 50.69  E-value: 1.85e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   865 GGVRNLRLIDPTFTTLTATWEA-ADGNVQGYKVIYVPTGGGTELMEQ---VSESTTTLVLQKLMPDTMYTVTVLPVYAEG 940
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718   941 DG 942
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 682-762 2.10e-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: 50.69  E-value: 2.10e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   682 GGVRNLQVLNPTMTTLNVRWE-PAEGKVKEYKVVYVPAAGGAESMVGLEQVSGATTNTVLRGLQSDTLYTVTLIPVYAEG 760
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1207157718   761 EG 762
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1045-1113 3.81e-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: 49.92  E-value: 3.81e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207157718  1045 GGVRNLQVTDPTSSTLNVRWEH-ADGNPRNYKVFYIPQPGDAEMMEL---VSGGTTSTVLRNLNANTMYKVTL 1113
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRV 74
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1321-1573 6.04e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 55.01  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1321 IKVYNPTPNSLNVRWEPASG---QVQQYRVAYAPLTGIRPLESVLVPGNLNNAFLDQLVPDTPYSVNVMAVYADGEGPGI 1397
Cdd:COG3401     55 LLVAAGLSSGGGLGTGGRAGttsGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGG 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1398 DGNGKTLPRAGPrnmrVFETTTSTISIGWDHAEGPVQQYKISYASLTGDPITEFTVVPGNRNNAMLQNLHPDTPYNITVT 1477
Cdd:COG3401    135 AATAGTYALGAG----LYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVA 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1478 AVYPEG---PGGSLNGNGKTLGLLAPQNLRVSDEWYTRFRVSWDPAPSP-VMGYKlVYQPTTKDESLEVfVGDV--TSYT 1551
Cdd:COG3401    211 ATDTGGesaPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESdATGYR-VYRSNSGDGPFTK-VATVttTSYT 288

                          250       260
                   ....*....|....*....|..
gi 1207157718 1552 LHNLLPGTTYDVQVYAQYDGGV 1573
Cdd:COG3401    289 DTGLTNGTTYYYRVTAVDAAGN 310
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1705-1857 8.34e-07

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 53.18  E-value: 8.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1705 ADVVFLIDGSWSIGDESFSKVIQfvfSVVGAFDVIGPtGMQISFVQYSDDANTEFRLNTYKDKGTALSALKLIRyQGGNT 1784
Cdd:COG2304     92 LNLVFVIDVSGSMSGDKLELAKE---AAKLLVDQLRP-GDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQ-AGGGT 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1785 KTGVALKHVYEkviTVENGMRRNVPKVVVAVTDGR------SQDDVHKNAAKLQHAGYSVFVVGV-ADVDFVELQNIASK 1857
Cdd:COG2304    167 ALGAGLELAYE---LARKHFIPGRVNRVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVgSDYNEDLLERLADA 243
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1045-1113 1.58e-06

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: 48.26  E-value: 1.58e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207157718 1045 GGVRNLQVTDPTSSTLNVRWEHAD---GNPRNYKVFYIP-QPGDAEMMELVSGGTTSTVLRNLNANTMYKVTL 1113
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREkGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRV 74
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
713-1203 1.80e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.47  E-value: 1.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  713 VVYVPAAGGAESMVGLEQVSGATTNTVLRglQSDTLYTVTLIPVYAEGEGQRMSENGKTRALGGVKNLRVTDPTMTSLNV 792
Cdd:COG3401     84 VAAAPPTATGLTTLTGSGSVGGATNTGLT--SSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  793 KWDPADGAVRqykIFFVPAAGGTEAMETVPGPQNTIVLRNLQPDTVYTVSVVPVYPATEGRRQSE---NGKTLPLGGVRN 869
Cdd:COG3401    162 SVAGAGVVVS---PDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvTTPTTPPSAPTG 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  870 LRLIDPTFTTLTATWEAADG-NVQGYKVIYVPTGGGTelMEQVSEST-TTLVLQKLMPDTMYTVTVLPVYAEGDGPRLSE 947
Cdd:COG3401    239 LTATADTPGSVTLSWDPVTEsDATGYRVYRSNSGDGP--FTKVATVTtTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSN 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  948 ----KGKTKPLGSVRNLQVTDPTISTLNVRWEPAEGNVREYIVIY--VPAGSQDQEVDQVPGTTTSTVlKNLEPDTTYTV 1021
Cdd:COG3401    317 vvsvTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYrsTSGGGTYTKIAETVTTTSYTD-TGLTPGTTYYY 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1022 TLVPVYHEMEGKSLSENGKTKPLGGVRNLQVTDPTSSTLNVRWEHADGNPRNYKVFYIPQPGDAEMMELVSGGTTSTVLR 1101
Cdd:COG3401    396 KVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSS 475

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1102 NLNANTMYKVTLLP--MYENDVEGKRQSENGKTKPLGSVKNLQVTDPTVNSLRVRWDAADGDV--------RQYNVIYVP 1171
Cdd:COG3401    476 TVTATTTDTTTANLsvTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVgastgdvlITDLVSLTT 555

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1207157718 1172 VAGGAAGQTQVSGMSTNTILRNLQPNTEYKVT 1203
Cdd:COG3401    556 SASSSVSGAGLGSGNLYLITTLGGSLLTTTST 587
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
2188-2377 4.43e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 4.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2188 PGEAGRQGPKGDPGDAGLPGQKG---PPGPTGAIGPVGPAGIRGPPGKEGPVGPMGPQGAMGPPGAPGMPGPAGKPGKNG 2264
Cdd:COG5164     12 SDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTR 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2265 DTGVPGLTGVKGDKGERGDIASQSMMRSIARQVCEQLVNGQMGRFNDMFNQIPSNYHSNSPGPSGPPGPPGPQGPRGEPG 2344
Cdd:COG5164     92 PAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPG 171

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207157718 2345 RLGRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:COG5164    172 GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQG 204
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
553-1046 6.29e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.54  E-value: 6.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  553 DPDTEYDVTVTAIYPDESESEDLMGSQRTLSKLITPVPTGPPQNLQVFNATTTTLTVKWDHAPGPVQSYKVTHQPVAGGK 632
Cdd:COG3401    106 ATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSL 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  633 PLSVQVGGKKNSVIlqklTPNTPYTITVAAVYRTGE---SKDISGQGRTKPLGGVRNLQVLNPTMTTLNVRWEPAEGK-V 708
Cdd:COG3401    186 TVTSTTLVDGGGDI----EPGTTYYYRVAATDTGGEsapSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESdA 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  709 KEYKVVYVPAAGGAESMVGleqvSGATTNTVLRGLQSDTLYTVTLIPVYAEGEGQRMSE----NGKTRALGGVKNLRVTD 784
Cdd:COG3401    262 TGYRVYRSNSGDGPFTKVA----TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNvvsvTTDLTPPAAPSGLTATA 337

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  785 PTMTSLNVKWDPADGA-VRQYKIFFVPAAGGTEAMETVPGPQNTIVLRNLQPDTVYTVSVVPVYPATEGRRQSENGKTLP 863
Cdd:COG3401    338 VGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATT 417

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  864 LGGVRNLRLIDPTFTTLTATWEAADGN--VQGYKVIYVPTGGGTELMEQVSESTTTLVLQKLMPDTMYTVTVLPVYAEGD 941
Cdd:COG3401    418 ASAASGESLTASVDAVPLTDVAGATAAasAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  942 GPRLSekgktkplgSVRNLQVTDPTISTLNVRWEPAEGNVREYIVIYVPAGSQDQEVDQVPGTTTSTVLKNLEPDTTYTV 1021
Cdd:COG3401    498 GGSGA---------SSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGS 568

                          490       500
                   ....*....|....*....|....*
gi 1207157718 1022 TLVPVYHEMEGKSLSENGKTKPLGG 1046
Cdd:COG3401    569 GNLYLITTLGGSLLTTTSTNTNDVA 593
VWA_2 pfam13519
von Willebrand factor type A domain;
35-122 7.17e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.90  E-value: 7.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   35 IVLLVDGSWSI-----GRLNFKTIRAFIGRMVGVFDIgpdkVQIGLAQYSGDPKTEWHLNAHptRASLLDAVANLPYKGG 109
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTKD--RAKILRALRRLEPKGG 74

                           90
                   ....*....|...
gi 1207157718  110 NTMTGMALNYILQ 122
Cdd:pfam13519   75 GTNLAAALQLARA 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 226-293 7.60e-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: 46.07  E-value: 7.60e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207157718   226 DLETSEVTHYSFRATWMPPDEP-VERFRIEYVPA---AGGKTEVLFVDGEENTLVLVNLNPMTEYIVRVYGV 293
Cdd:smart00060    6 NLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1706-1870 8.01e-06

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 48.82  E-value: 8.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1706 DVVFLIDGSWSIGDESFSK----VIQFVfSVVGAFDVigptGMQISFVQYSDDAN-----TEFRLNtykDKGTALSALKL 1776
Cdd:cd01470      2 NIYIALDASDSIGEEDFDEaknaIKTLI-EKISSYEV----SPRYEIISYASDPKeivsiRDFNSN---DADDVIKRLED 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1777 IRYQGGNTKTGV----ALKHVYEK--VITVENGMR----RNvpkVVVAVTDGRS-------------QDDVHKN-AAKLQ 1832
Cdd:cd01470     74 FNYDDHGDKTGTntaaALKKVYERmaLEKVRNKEAfnetRH---VIILFTDGKSnmggsplptvdkiKNLVYKNnKSDNP 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207157718 1833 HAGY-SVFVVGV-ADVDFVELQNIAS-KPSERHVFVVDDFD 1870
Cdd:cd01470    151 REDYlDVYVFGVgDDVNKEELNDLASkKDNERHFFKLKDYE 191
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1012-1575 1.79e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.00  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1012 NLEPDTTYTVTLVPVYHEMEGKSLSENGKTKPLGGVRNLQVTDPTSSTLNVRWEHADGNPRNYKVFYIPQPGDAEMMELV 1091
Cdd:COG3401      3 SSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1092 ---------SGGTTSTVLRNLNANTMYKVTLLPMYENDVEGKRQSENGKTKPLGSVKNLQVTDPTVNSLRVRWDAADGDV 1162
Cdd:COG3401     83 avaaapptaTGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1163 RQYNVIYVPVAGGAAGQTQVSGMSTNTILR-----NLQPNTEYKVTVVPVYADAEG---KRQSANGKTKPLGGVKNLQVT 1234
Cdd:COG3401    163 VAGAGVVVSPDTSATAAVATTSLTVTSTTLvdgggDIEPGTTYYYRVAATDTGGESapsNEVSVTTPTTPPSAPTGLTAT 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1235 DPTTSSLKVRWEPA-EGNVRQYRIFYvpASGGAEDMEQVSGGTTNTIL-RNLLSDTVYTVTVVPVYPEGEGLRQSE---- 1308
Cdd:COG3401    243 ADTPGSVTLSWDPVtESDATGYRVYR--SNSGDGPFTKVATVTTTSYTdTGLTNGTTYYYRVTAVDAAGNESAPSNvvsv 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1309 KGKTLPRLPPRNIKVYNPTPNSLNVRWEPASG-QVQQYRVAYAPlTGIRPLESVLVPGNlNNAFLD-QLVPDTPYSVNVM 1386
Cdd:COG3401    321 TTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRST-SGGGTYTKIAETVT-TTSYTDtGLTPGTTYYYKVT 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1387 AVYADG---EGPGIDGNGKTLPRAGPRNMRV--FETTTSTISIGWDHAEGPVQQYKISYASLTGDPITEFTVVPGNRNNA 1461
Cdd:COG3401    399 AVDAAGnesAPSEEVSATTASAASGESLTASvdAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1462 MLQNLHPDTPYNITVTAVYPEGPGGSLNGNGKTLGLLAPQNLRVSDEWYTRFRVSWDPAPSPVMG---YKLVYQPTTKDE 1538
Cdd:COG3401    479 ATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGdvlITDLVSLTTSAS 558

                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1207157718 1539 SLEVFVGDVTSYTLHNLLPGTTYDVQVYAQYDGGVSK 1575
Cdd:COG3401    559 SSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGV 595
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1706-1857 4.05e-05

VWA F09G8.8 type: 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. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 46.65  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1706 DVVFLIDGSWSIGDESFSKVIQFVFSVVGAFDVIG-----PTGMQISFVQYSDDANTEFRLNTYKdkgTALSALKLIRYQ 1780
Cdd:cd01477     21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGtdyddPRSTRVGLVTYNSNATVVADLNDLQ---SFDDLYSQIQGS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1781 --------GGNTKTGVALKhvyEKVI-TVENGMRRNVPKVVVAVT---DGRSQDDVHKNAAKLQHAGYSVFVV---GVAD 1845
Cdd:cd01477     98 ltdvsstnASYLDTGLQAA---EQMLaAGKRTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAIITVaftQDES 174

                          170
                   ....*....|...
gi 1207157718 1846 VDFVE-LQNIASK 1857
Cdd:cd01477    175 SNLLDkLGKIASP 187
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 33-214 4.22e-05

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: 46.73  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718   33 ADIVLLVDGSWSIGRlNFKTIRAFIGRMVGVFdIGPDkVQIGLAQYSGDPKTEWHLNAHPT--RASLLDAVANLPykGGN 110
Cdd:cd01474      5 FDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSaiIKGLEVLKKVTP--SGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  111 TMTGMALNYILQNNFRPNVGMRPDSrKIGVLVTDGKSQDEIVVNSQR----LRDSGIELYAIGVKNADENELRSIATDPD 186
Cdd:cd01474     80 TYIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYPEHeaklSRKLGAIVYCVGVTDFLKSQLINIADSKE 158

                          170       180
                   ....*....|....*....|....*....
gi 1207157718  187 eiHMYNVND-FSFLLDIVDDLTENLCNSV 214
Cdd:cd01474    159 --YVFPVTSgFQALSGIIESVVKKACIEI 185
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2347-2377 8.40e-05

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: 42.48  E-value: 8.40e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1207157718 2347 GRNGLPGSPGLPGRQGERGTPGEKGERGSPG 2377
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG 37
fn3 pfam00041
Fibronectin type III domain;
1228-1289 9.07e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.17  E-value: 9.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207157718 1228 VKNLQVTDPTTSSLKVRWEPAE---GNVRQYRIFYVPASGGAEDMEQ-VSGGTTNTILRNLLSDTV 1289
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTE 68
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2350-2403 9.26e-05

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: 42.10  E-value: 9.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207157718 2350 GLPGSPGLPGRQGERGTPGEKGERGSPGV-GERgqrgpsgppgppgesrtGPTGS 2403
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPpGEP-----------------GPPGP 38
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2219-2282 8.80e-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: 39.40  E-value: 8.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207157718 2219 GPVGPAGIRGPPGKEGPVGPMGPQgamgppgapGMPGPagkPGKNGDTGVPGLTGVKGDKGERG 2282
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPP---------GPPGP---PGEPGPPGPPGPPGPPGPPGAPG 52
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
286-667 9.29e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 44.61  E-value: 9.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  286 YIVRVYGVIGEES-SEPLKGTETTLPLPAVTSMSVYDEALTSMRVRWELVK--GASGYLLNYnainASVPSGMMEMRVGA 362
Cdd:COG3401    207 YRVAATDTGGESApSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTesDATGYRVYR----SNSGDGPFTKVATV 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  363 DVNDVQLLQLLPNTAYSISLFAL--HGE--AASQPL-IDRGVTLPLPPAGkLKITEVTHSSMRLTWDAAPG-NVRKYIIT 436
Cdd:COG3401    283 TTTSYTDTGLTNGTTYYYRVTAVdaAGNesAPSNVVsVTTDLTPPAAPSG-LTATAVGSSSITLSWTASSDaDVTGYNVY 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  437 YK-REDGELKELEVNGDITTMVLTNLRSQTEYDVAVTPVYDEGsgnpmLGTAITDVVPAPKNLRFSEVGQTSFRATWEHG 515
Cdd:COG3401    362 RStSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAG-----NESAPSEEVSATTASAASGESLTASVDAVPLT 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  516 APDVGMYRIGWSKKGDRENVKSEILAREETSHLLTELDPDTEYDVTVTAIYPDESESEDLMGSQRTLSKLIT---PVPTG 592
Cdd:COG3401    437 DVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSvsvIGASA 516

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207157718  593 PPQNLQVFNATTTTLTVKWDHAPGPVQSYKVTHQPVAGGKPLSVQVGGKKNSVILQKLTPNTPYTITVAAVYRTG 667
Cdd:COG3401    517 AAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTND 591
fn3 pfam00041
Fibronectin type III domain;
312-393 1.40e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  312 PAVTSMSVYDEALTSMRVRWELVKGASGYLLNYN--AINASVPSGMMEMRVGADVNDVQLLQLLPNTAYSISLFALHGEA 389
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEveYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1207157718  390 ASQP 393
Cdd:pfam00041   81 EGPP 84
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
695-846 1.82e-03

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 43.78  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  695 TTLNVRWEPAEGKVkEYKVVYVPAAGgaeSMVGLEQVSgaTTNTVLRGLQSDTlYTVTLIPVYAEGEGQRMSE------N 768
Cdd:COG4733    552 TTLTVSWDAPAGAV-AYEVEWRRDDG---NWVSVPRTS--GTSFEVPGIYAGD-YEVRVRAINALGVSSAWAAssettvT 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718  769 GKTRALGGVKNLRVTdPTMTSLNVKWD-PADGAVRQYKIFFVPAAGGTEA-METVPGPQNTIVLRNLQPDTVYTVSVVPV 846
Cdd:COG4733    625 GKTAPPPAPTGLTAT-GGLGGITLSWSfPVDADTLRTEIRYSTTGDWASAtVAQALYPGNTYTLAGLKAGQTYYYRARAV 703
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1226-1289 2.60e-03

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: 39.40  E-value: 2.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207157718 1226 GGVKNLQVTDPTTSSLKVRWEPAE---GNVRQYRIFYVPA-SGGAEDMEQVSGGTTNTILRNLLSDTV 1289
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTE 69
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1226-1289 5.01e-03

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: 38.36  E-value: 5.01e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207157718  1226 GGVKNLQVTDPTTSSLKVRWE-PAEGNVRQYRIFYVPASGGAEDMEQ---VSGGTTNTILRNLLSDTV 1289
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTE 69
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
2110-2241 6.12e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 6.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 2110 PSMRDESKCPALPNACTCTSDSSGPPGPQGPVGAPGSKGPRGERGEPGQVGPVGTrGEMGMPGPMGPPGPQGPSGRSIP- 2188
Cdd:COG5164    119 PPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGS-TTPPDDGGSTTPPNKGETGTDIPt 197

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207157718 2189 GEAGRQGPKGDPGDAGLPGQKGPPGPTGAI-GPVGPAGIRGPPGKEGPVGPMGP 2241
Cdd:COG5164    198 GGTPRQGPDGPVKKDDKNGKGNPPDDRGGKtGPKDQRPKTNPIERRGPERPEAA 251
fn3 pfam00041
Fibronectin type III domain;
1588-1665 8.68e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 37.39  E-value: 8.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207157718 1588 VTNLESYDVGYNRFCIKWTP----HRAATSYRIKLNPVDpSAKGQQEITITASQSQYCFEGLSQDSLYTATVFVQTPNLE 1663
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKN-SGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ..
gi 1207157718 1664 GP 1665
Cdd:pfam00041   82 GP 83
 
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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