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Conserved domains on  [gi|2024367818|ref|XP_040532711|]
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collagen alpha-1(XIV) chain isoform X1 [Gallus gallus]

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 ...
157-320 2.62e-87

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: 281.48  E-value: 2.62e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL 236
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQDDVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTHVYN 316
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160

                   ....
gi 2024367818  317 VADF 320
Cdd:cd01482    161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
1044-1208 1.87e-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: 279.17  E-value: 1.87e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNT 1123
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1124 KTGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQDDVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSERHVF 1203
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159

                   ....*
gi 2024367818 1204 FVDDF 1208
Cdd:cd01482    160 NVADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
1242-1437 6.07e-59

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 201.43  E-value: 6.07e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1242 GFKMMEMFGLVEKEFSAIDGVSMEPGtfnvYPCYRLHKDALVSQPTKYLHPEGLPSDYTITFLFRIlpdTPQEPFALWEI 1321
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1322 LNEQYEPLVGVILDNGGKTLTFFNYDYKGDFQTVTFEGpeiRKIFYGSFHKLHVVISKTTAKIIIDCKEAGEKTINAAG- 1400
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 2024367818  1401 -NISSDGIEVLGRMVRSRGPrdnsAPLQLQMFDIVCAT 1437
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1490-1718 7.13e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.75  E-value: 7.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1490 GHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiQGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQRGLP 1569
Cdd:NF038329   117 GEKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1570 GKDGPTGPQGPPGPVGIPGAPGVPGITGSQGPQGDVGAPGAPGPKGERGERG-DLQSQAMVRAVARQVCEQLIQGhmary 1648
Cdd:NF038329   177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpAGDGQQGPDGDPGPTGEDGPQG----- 251
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1649 nsilnqipsqsvstrtiagppgepgrpgapgpqgEQGSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG 1718
Cdd:NF038329   252 ----------------------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
316-714 3.61e-21

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 3.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  316 NVADFNFMNSIVEGLTRTVCSRVEEQEKEIKGTIAASLGAPTDLVTSDITARGFRVSWTHSPG-KVEKYRVVYYPTRGGQ 394
Cdd:COG3401     12 GIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGtTSGVAAVAVAAAPPTA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  395 PEEVVVDGSSSTAVLKNlmSLTEYQIAVFAIYSNAASEGLRGTETTLALPMASDLKLYDVSHSSMRAKWNGVAGATGYMI 474
Cdd:COG3401     92 TGLTTLTGSGSVGGATN--TGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  475 LYAPLTEGLAADEKEIKIGEASTELELDGLLPNTEYTVTVYAMFGEEASDPLTG----QETTLPlSPPSNLKFSDVGHNS 550
Cdd:COG3401    170 VSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPP-SAPTGLTATADTPGS 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  551 AKLTWDPAS-KNVKGYRIMYVKTDGTETNEVEVGPVSTHTLKSLTALTEYTVAIFSLYDEG----QSEPLTGsfTTRKVP 625
Cdd:COG3401    249 VTLSWDPVTeSDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnesaPSNVVSV--TTDLTP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  626 P--PQHLEVDEASTDSFRVSWKPTSS-DIAFYRLAWIPLDGGESEEVVLSGDADSYVIEGLLPNTEYEVSLLAVFDDETE 702
Cdd:COG3401    327 PaaPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE 406
                          410
                   ....*....|..
gi 2024367818  703 SEVVAVLGATIV 714
Cdd:COG3401    407 SAPSEEVSATTA 418
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31-112 1.90e-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: 62.13  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   31 SPPTRLRYNVVNPDSVQISWKAPK---GQFSGYKLLVTPSSGGKTNQLILQN-TATKAIIQGLIPDQNYALQIIAFSDDK 106
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                   ....*.
gi 2024367818  107 ESKPAQ 112
Cdd:cd00063     82 ESPPSE 87
fn3 pfam00041
Fibronectin type III domain;
837-915 2.15e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  837 SAPRNLRVSDEWYNRLRISWDAPPSPTM---GYRIVYKSINVPGPALETFVGDDINTILILNLFSGTEYSVKVFASYSTG 913
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ..
gi 2024367818  914 FS 915
Cdd:pfam00041   81 EG 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
745-824 8.32e-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: 54.16  E-value: 8.32e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   745 VRNLVIDDETTSSLRVVWDISDHNAQQFRVTYLTAKGDRAEEAVRTIMVPGRQNTLLLQPLLPDTEYKVTITPIYADGEG 824
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1685-1770 8.00e-08

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


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 8.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1685 GSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPGvgtqgprgppgstgppgesrtgspgppgSpgprgpaghTGPPGSQG 1764
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG----------------------------P---------PGPPGPPG 43

                   ....*.
gi 2024367818 1765 PAGPPG 1770
Cdd:pfam01391   44 PPGPPG 49
 
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 ...
157-320 2.62e-87

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: 281.48  E-value: 2.62e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL 236
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQDDVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTHVYN 316
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160

                   ....
gi 2024367818  317 VADF 320
Cdd:cd01482    161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
1044-1208 1.87e-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: 279.17  E-value: 1.87e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNT 1123
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1124 KTGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQDDVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSERHVF 1203
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159

                   ....*
gi 2024367818 1204 FVDDF 1208
Cdd:cd01482    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
158-328 9.92e-70

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 231.78  E-value: 9.92e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL- 236
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQD-DVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTHVY 315
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160
                          170
                   ....*....|...
gi 2024367818  316 NVADFNFMNSIVE 328
Cdd:pfam00092  161 TVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1045-1217 2.77e-69

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 230.62  E-value: 2.77e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1045 DLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNTK 1124
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1125 -TGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQD-DVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSERHV 1202
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159
                          170
                   ....*....|....*
gi 2024367818 1203 FFVDDFDAFTKIEDE 1217
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
1242-1437 6.07e-59

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 201.43  E-value: 6.07e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1242 GFKMMEMFGLVEKEFSAIDGVSMEPGtfnvYPCYRLHKDALVSQPTKYLHPEGLPSDYTITFLFRIlpdTPQEPFALWEI 1321
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1322 LNEQYEPLVGVILDNGGKTLTFFNYDYKGDFQTVTFEGpeiRKIFYGSFHKLHVVISKTTAKIIIDCKEAGEKTINAAG- 1400
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 2024367818  1401 -NISSDGIEVLGRMVRSRGPrdnsAPLQLQMFDIVCAT 1437
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1045-1214 2.85e-52

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: 181.88  E-value: 2.85e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1045 DLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYK-GGNT 1123
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1124 KTGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQD---DVNKVSREMQLDGFSFFAIGV-ADADYSELVNIGSKPSE 1199
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159
                           170
                    ....*....|....*
gi 2024367818  1200 RHVFFVDDFDAFTKI 1214
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
158-327 2.40e-50

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: 176.11  E-value: 2.40e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   158 DIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYK-GGNTL 236
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQD---DVIPPAKNLRDAGIELFAIGVKNA-DINELKEIASEPDST 312
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160
                           170
                    ....*....|....*
gi 2024367818   313 HVYNVADFNFMNSIV 327
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1490-1718 7.13e-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: 100.75  E-value: 7.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1490 GHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiQGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQRGLP 1569
Cdd:NF038329   117 GEKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1570 GKDGPTGPQGPPGPVGIPGAPGVPGITGSQGPQGDVGAPGAPGPKGERGERG-DLQSQAMVRAVARQVCEQLIQGhmary 1648
Cdd:NF038329   177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpAGDGQQGPDGDPGPTGEDGPQG----- 251
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1649 nsilnqipsqsvstrtiagppgepgrpgapgpqgEQGSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG 1718
Cdd:NF038329   252 ----------------------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
316-714 3.61e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 3.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  316 NVADFNFMNSIVEGLTRTVCSRVEEQEKEIKGTIAASLGAPTDLVTSDITARGFRVSWTHSPG-KVEKYRVVYYPTRGGQ 394
Cdd:COG3401     12 GIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGtTSGVAAVAVAAAPPTA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  395 PEEVVVDGSSSTAVLKNlmSLTEYQIAVFAIYSNAASEGLRGTETTLALPMASDLKLYDVSHSSMRAKWNGVAGATGYMI 474
Cdd:COG3401     92 TGLTTLTGSGSVGGATN--TGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  475 LYAPLTEGLAADEKEIKIGEASTELELDGLLPNTEYTVTVYAMFGEEASDPLTG----QETTLPlSPPSNLKFSDVGHNS 550
Cdd:COG3401    170 VSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPP-SAPTGLTATADTPGS 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  551 AKLTWDPAS-KNVKGYRIMYVKTDGTETNEVEVGPVSTHTLKSLTALTEYTVAIFSLYDEG----QSEPLTGsfTTRKVP 625
Cdd:COG3401    249 VTLSWDPVTeSDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnesaPSNVVSV--TTDLTP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  626 P--PQHLEVDEASTDSFRVSWKPTSS-DIAFYRLAWIPLDGGESEEVVLSGDADSYVIEGLLPNTEYEVSLLAVFDDETE 702
Cdd:COG3401    327 PaaPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE 406
                          410
                   ....*....|..
gi 2024367818  703 SEVVAVLGATIV 714
Cdd:COG3401    407 SAPSEEVSATTA 418
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1487-1718 1.87e-20

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: 96.51  E-value: 1.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1487 GAKGHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiQGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDG---AQ 1563
Cdd:NF038329   162 GPAGPQGEAGPQGPAGKDGE--------------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGeagPA 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1564 GQRGLPGKDGPTGPQGPPGpvgipgapgvPGITGSQGPQGDVGAPGAPGPKGERGERGdLQSQAMVRAVARQVCEQLIQG 1643
Cdd:NF038329   222 GEDGPAGPAGDGQQGPDGD----------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG-PDGPDGKDGERGPVGPAGKDG 290
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024367818 1644 HMARynsilNQIPSQSvstrtiagppgepgrpgapgpqGEQGSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG 1718
Cdd:NF038329   291 QNGK-----DGLPGKD----------------------GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
fn3 pfam00041
Fibronectin type III domain;
625-696 1.97e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 1.97e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818  625 PPPQHLEVDEASTDSFRVSWKP---TSSDIAFYRLAWIPLDGGESE-EVVLSGDADSYVIEGLLPNTEYEVSLLAV 696
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
536-621 4.17e-14

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: 69.45  E-value: 4.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  536 SPPSNLKFSDVGHNSAKLTWDPAS---KNVKGYRIMYVKTDGTETNEVEVGPVST--HTLKSLTALTEYTVAIFSLYDEG 610
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSEtsYTLTGLKPGTEYEFRVRAVNGGG 81
                           90
                   ....*....|..
gi 2024367818  611 QSEPLT-GSFTT 621
Cdd:cd00063     82 ESPPSEsVTVTT 93
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1486-1621 1.53e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.94  E-value: 1.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1486 RGAKGHRGDPGPKGPDGPRGEIGVPGPQGPPGPQGPSGLSIQ----GLPGPPG--EKGEKGDLGFPGLQGVPGASGSPGR 1559
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPagedGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGK 258
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024367818 1560 DGAQGQRGLPGKDGPTGPqgppgpvgipgapgvPGITGSQGPQGDVGAPGAPGPKGERGERG 1621
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKdge---------rgpVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1486-1614 3.48e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.17  E-value: 3.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1486 RGAKGHRGDPGPKGPDGPRGEIGVPgpqgppgpqgpsglsiqGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQ 1565
Cdd:NF038329   244 TGEDGPQGPDGPAGKDGPRGDRGEA-----------------GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024367818 1566 R---GLPGKDGPTGPqgppgpvgipgapgvPGITGSQGPQGDVGAPGAPGPK 1614
Cdd:NF038329   307 NgkdGLPGKDGKDGQ---------------PGKDGLPGKDGKDGQPGKPAPK 343
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
157-308 4.83e-13

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: 71.12  E-value: 4.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFN-FRLVRLFLENLVSAFnvgSEKTRVGLAQYSGDPRIEWHLnaygTKD--AVLDAVRNLPYKGG 233
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPL----TRDreALKRALDELPPGGG 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  234 nTLTGLALTYILEnSFKPEagaRPGVSKIGILITDGKSQDDVIPP---AKNLRDAGIELFAIGVKNADINE--LKEIASE 308
Cdd:COG1240    166 -TPLGDALALALE-LLKRA---DPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIAEA 240
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1528-1572 1.11e-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: 61.36  E-value: 1.11e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024367818 1528 GLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQRGLPGKD 1572
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31-112 1.90e-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: 62.13  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   31 SPPTRLRYNVVNPDSVQISWKAPK---GQFSGYKLLVTPSSGGKTNQLILQN-TATKAIIQGLIPDQNYALQIIAFSDDK 106
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                   ....*.
gi 2024367818  107 ESKPAQ 112
Cdd:cd00063     82 ESPPSE 87
fn3 pfam00041
Fibronectin type III domain;
837-915 2.15e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  837 SAPRNLRVSDEWYNRLRISWDAPPSPTM---GYRIVYKSINVPGPALETFVGDDINTILILNLFSGTEYSVKVFASYSTG 913
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ..
gi 2024367818  914 FS 915
Cdd:pfam00041   81 EG 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
837-921 2.64e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 61.74  E-value: 2.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  837 SAPRNLRVSDEWYNRLRISWDAPP---SPTMGYRIVYKSINVPGPALETFVGDDINTILILNLFSGTEYSVKVFASYSTG 913
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                   ....*...
gi 2024367818  914 FSDALTGV 921
Cdd:cd00063     82 ESPPSESV 89
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1541-1718 4.17e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 67.24  E-value: 4.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1541 DLGFPGLQGVPGASGSPGRDGAQGQRGlpgKDGPTGPQGPPGPVGIPGApgvPGITGSQGPQGDVGAPGAPGPKGERGER 1620
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRG---DRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1621 GDlQSQAMVRAVARQVCEQLIQGhmarynsilnqipSQSVSTRTIAGPPGEPGRPGAPGPQGEQGSPGMQGFPGNPGQPG 1700
Cdd:NF038329   186 GP-AGEKGPQGPRGETGPAGEQG-------------PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
                          170
                   ....*....|....*...
gi 2024367818 1701 RPGERGLPGEKGDRGNPG 1718
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAG 269
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
625-696 5.56e-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: 60.32  E-value: 5.56e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818   625 PPPQHLEVDEASTDSFRVSWKPTSSDIAF-YRLAWIPLDGGES---EEVVLSGDADSYVIEGLLPNTEYEVSLLAV 696
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
31-110 6.61e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 6.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   31 SPPTRLRYNVVNPDSVQISWKAPK---GQFSGYKLLVTP-SSGGKTNQLILQNTATKAIIQGLIPDQNYALQIIAFSDDK 106
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....
gi 2024367818  107 ESKP 110
Cdd:pfam00041   81 EGPP 84
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
1044-1189 3.71e-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: 62.65  E-value: 3.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDN-FNKIISFLYSTVGALDKigpdGTQVAIIQFSDDPRTEFKLNayKTKETLLEAIQQIAYKGGn 1122
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG- 165
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1123 TKTGKAIKHAREVLftgeAGMRKGIPKVLVVITDGR---SQDDVNKVSREMQLDGFSFFAIGVADADYSE 1189
Cdd:COG1240    166 TPLGDALALALELL----KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDE 231
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
837-915 5.15e-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: 54.93  E-value: 5.15e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   837 SAPRNLRVSDEWYNRLRISWDAPPSP-TMGYRIVYKSINVPGPALETFV--GDDINTILILNLFSGTEYSVKVFASYSTG 913
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81

                    ..
gi 2024367818   914 FS 915
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
745-824 8.32e-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: 54.16  E-value: 8.32e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   745 VRNLVIDDETTSSLRVVWDISDHNAQQFRVTYLTAKGDRAEEAVRTIMVPGRQNTLLLQPLLPDTEYKVTITPIYADGEG 824
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
745-824 2.12e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  745 VRNLVIDDETTSSLRVVWDISDHNA---QQFRVTYLTAKGdraEEAVRTIMVPGRQNTLLLQPLLPDTEYKVTITPIYAD 821
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNS---GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ...
gi 2024367818  822 GEG 824
Cdd:pfam00041   80 GEG 82
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1685-1770 8.00e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 8.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1685 GSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPGvgtqgprgppgstgppgesrtgspgppgSpgprgpaghTGPPGSQG 1764
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG----------------------------P---------PGPPGPPG 43

                   ....*.
gi 2024367818 1765 PAGPPG 1770
Cdd:pfam01391   44 PPGPPG 49
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31-108 1.67e-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: 1.67e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818    31 SPPTRLRYNVVNPDSVQISWKAPK-GQFSGYKL---LVTPSSGGKTNQLILQNTATKAIIQGLIPDQNYALQIIAFSDDK 106
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPdDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81

                    ..
gi 2024367818   107 ES 108
Cdd:smart00060   82 EG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
745-833 2.08e-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: 47.88  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  745 VRNLVIDDETTSSLRVVWDISDHNA---QQFRVTYLTAKGDRAEEAVRTimvPGRQNTLLLQPLLPDTEYKVTITPIYAD 821
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpiTGYVVEYREKGSGDWKEVEVT---PGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                           90
                   ....*....|...
gi 2024367818  822 GEGV-SVSAPGKT 833
Cdd:cd00063     81 GESPpSESVTVTT 93
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1560-1770 6.44e-06

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: 50.67  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1560 DGAQGQRGLpgkdgptgpQGPpgpvgipgapgvPGITGSQGPQGDVGAPGAPGPKGERGERGdlqsqamvravarQVCEQ 1639
Cdd:NF038329   116 DGEKGEPGP---------AGP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQG-------------ERGEK 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1640 LIQGhmarynsilnqipsqsvstrtiagppgepgrpgapgpqgEQGSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG- 1718
Cdd:NF038329   162 GPAG---------------------------------------PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGp 202
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024367818 1719 ---VGTQGPRGPPGSTGPPGESRTGSPGPPGSPGPRGPAGHTGPPGSQGPAGPPG 1770
Cdd:NF038329   203 ageQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAG 257
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
158-339 3.98e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 48.42  E-value: 3.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFNF--RLVRLfLENLVSAFNVGSEKTRVGLAQYSGDPR--IEWHLNAYGTKDAVLDAVR-----NL 228
Cdd:PTZ00441    44 DLYLLVDGSGSIGYHNWitHVIPM-LMGLIQQLNLSDDAINLYMSLFSNNTTelIRLGSGASKDKEQALIIVKslrktYL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  229 PYkgGNTLTGLALTYIlENSFKPEAGaRPGVSKIGILITDG--KSQDDVIPPAKNLRDAGIELFAIGVK---NADINELk 303
Cdd:PTZ00441   123 PY--GKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgiNHQFNRL- 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024367818  304 eIA----SEPdSTHVYNVADFNFMNSIVEGLTRTVCSRVE 339
Cdd:PTZ00441   198 -LAgcrpREG-KCKFYSDADWEEAKNLIKPFIAKVCTEVE 235
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31-112 4.38e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.91  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   31 SPPTRLRYNVVNPDSVQISWKAPKG-QFSGYKLLVTPSSGGKTNQLILQNTATKAIIQGLIPDQNYALQIIAFSDD-KES 108
Cdd:COG3401    328 AAPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAgNES 407

                   ....
gi 2024367818  109 KPAQ 112
Cdd:COG3401    408 APSE 411
 
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 ...
157-320 2.62e-87

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: 281.48  E-value: 2.62e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL 236
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQDDVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTHVYN 316
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160

                   ....
gi 2024367818  317 VADF 320
Cdd:cd01482    161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
1044-1208 1.87e-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: 279.17  E-value: 1.87e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNT 1123
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1124 KTGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQDDVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSERHVF 1203
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159

                   ....*
gi 2024367818 1204 FVDDF 1208
Cdd:cd01482    160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
157-320 6.14e-77

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: 251.76  E-value: 6.14e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL 236
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQDDVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTHVYN 316
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160

                   ....
gi 2024367818  317 VADF 320
Cdd:cd01472    161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
1044-1208 2.58e-73

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: 241.75  E-value: 2.58e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNT 1123
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLD-IGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1124 KTGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQDDVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSERHVF 1203
Cdd:cd01472     80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159

                   ....*
gi 2024367818 1204 FVDDF 1208
Cdd:cd01472    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
158-328 9.92e-70

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 231.78  E-value: 9.92e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL- 236
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQD-DVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTHVY 315
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160
                          170
                   ....*....|...
gi 2024367818  316 NVADFNFMNSIVE 328
Cdd:pfam00092  161 TVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1045-1217 2.77e-69

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 230.62  E-value: 2.77e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1045 DLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNTK 1124
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1125 -TGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQD-DVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSERHV 1202
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159
                          170
                   ....*....|....*
gi 2024367818 1203 FFVDDFDAFTKIEDE 1217
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
1242-1437 6.07e-59

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 201.43  E-value: 6.07e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1242 GFKMMEMFGLVEKEFSAIDGVSMEPGtfnvYPCYRLHKDALVSQPTKYLHPEGLPSDYTITFLFRIlpdTPQEPFALWEI 1321
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1322 LNEQYEPLVGVILDNGGKTLTFFNYDYKGDFQTVTFEGpeiRKIFYGSFHKLHVVISKTTAKIIIDCKEAGEKTINAAG- 1400
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 2024367818  1401 -NISSDGIEVLGRMVRSRGPrdnsAPLQLQMFDIVCAT 1437
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
157-315 3.57e-55

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: 189.42  E-value: 3.57e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGN-T 235
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  236 LTGLALTYILENSFKPeAGARPGVSKIGILITDGKSQD--DVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTH 313
Cdd:cd01450     81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159

                   ..
gi 2024367818  314 VY 315
Cdd:cd01450    160 VF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
157-347 4.96e-55

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: 191.83  E-value: 4.96e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL 236
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 TGLALTYILENSFKPEAGARPG---VSKIGILITDGKSQDDVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDSTH 313
Cdd:cd01475     83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2024367818  314 VYNVADFNFMNSIVEGLTRTVCSRVEEQEKEIKG 347
Cdd:cd01475    163 VFYVEDFSTIEELTKKFQGKICVVPDLCATLSHV 196
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1044-1203 5.10e-55

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: 189.04  E-value: 5.10e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGN- 1122
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1123 TKTGKAIKHAREVLFTgEAGMRKGIPKVLVVITDGRSQD--DVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSER 1200
Cdd:cd01450     80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158

                   ...
gi 2024367818 1201 HVF 1203
Cdd:cd01450    159 HVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1045-1214 2.85e-52

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: 181.88  E-value: 2.85e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1045 DLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYK-GGNT 1123
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  1124 KTGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQD---DVNKVSREMQLDGFSFFAIGV-ADADYSELVNIGSKPSE 1199
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159
                           170
                    ....*....|....*
gi 2024367818  1200 RHVFFVDDFDAFTKI 1214
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
158-327 2.40e-50

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: 176.11  E-value: 2.40e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   158 DIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYK-GGNTL 236
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   237 TGLALTYILENSFKPEAGARPGVSKIGILITDGKSQD---DVIPPAKNLRDAGIELFAIGVKNA-DINELKEIASEPDST 312
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160
                           170
                    ....*....|....*
gi 2024367818   313 HVYNVADFNFMNSIV 327
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
157-320 6.19e-50

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: 174.82  E-value: 6.19e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTL 236
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  237 -TGLALTYILENSFKPEAGAR--PGVSKIGILITDGKSQDDVIPPAKNLRDAGIELFAIGVKNADINELKEIASEPDstH 313
Cdd:cd01481     81 nTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158

                   ....*..
gi 2024367818  314 VYNVADF 320
Cdd:cd01481    159 VFQVSDF 165
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
1044-1227 4.30e-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: 171.80  E-value: 4.30e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNT 1123
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLD-VGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1124 KTGKAIKHAREVLFTGEAGMRKG---IPKVLVVITDGRSQDDVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSER 1200
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161
                          170       180
                   ....*....|....*....|....*..
gi 2024367818 1201 HVFFVDDFDAFTKIEDELITFVCETAS 1227
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICVVPD 188
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
1045-1214 1.26e-44

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: 159.83  E-value: 1.26e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1045 DLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNTK 1124
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLD-IGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1125 TGKAIKHAREVLFTGEAGMRKGIPKVLVVITDGRSQDD--VNKVSREMQLDGFSFFAIGVADA-----DYSELVNIGSKP 1197
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGGHfqrenSREELKTIASKP 160
                          170
                   ....*....|....*..
gi 2024367818 1198 SERHVFFVDDFDAFTKI 1214
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 ...
1044-1208 7.72e-44

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: 157.10  E-value: 7.72e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGNT 1123
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLD-VGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1124 -KTGKAIKHAREVLFTGEAG--MRKGIPKVLVVITDGRSQDDVNKVSREMQLDGFSFFAIGVADADYSELVNIGSKPSer 1200
Cdd:cd01481     80 lNTGSALDYVVKNLFTKSAGsrIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS-- 157

                   ....*...
gi 2024367818 1201 HVFFVDDF 1208
Cdd:cd01481    158 FVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
158-320 5.39e-42

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: 152.51  E-value: 5.39e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGGNTLT 237
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  238 GLALTYILENSFKPEAGARPGVSKIGILITDGKSQDD-----VIPPAKnlrDAGIELFAIGV-----KNADINELKEIAS 307
Cdd:cd01469     82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDpllkdVIPQAE---REGIIRYAIGVgghfqRENSREELKTIAS 158
                          170
                   ....*....|...
gi 2024367818  308 EPDSTHVYNVADF 320
Cdd:cd01469    159 KPPEEHFFNVTDF 171
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
157-315 8.83e-33

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: 125.37  E-value: 8.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYK-GGNT 235
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  236 LTGLALTYILENSFKPeagARPGVSKIGILITDGKSQDDVIPP---AKNLRDAGIELFAIGVKN-ADINELKEIASEPDS 311
Cdd:cd00198     81 NIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157

                   ....
gi 2024367818  312 THVY 315
Cdd:cd00198    158 GAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1044-1203 2.59e-30

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: 118.44  E-value: 2.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYK-GGN 1122
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLS-ASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1123 TKTGKAIKHAREVLFtgeAGMRKGIPKVLVVITDGRSQDD---VNKVSREMQLDGFSFFAIGV-ADADYSELVNIGSKPS 1198
Cdd:cd00198     80 TNIGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTT 156

                   ....*
gi 2024367818 1199 ERHVF 1203
Cdd:cd00198    157 GGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
1044-1204 4.54e-30

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: 117.89  E-value: 4.54e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIgDDNFNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRT--EFKLNAYKTKETLLEAIQQIAYKGG 1121
Cdd:cd01476      1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLE-IGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1122 NTKTGKAIKHAREvLFTGEAGMRKGIPKVLVVITDGRSQDDVNKVSREMQ-LDGFSFFAIGVAD---ADYSELVNIGSkp 1197
Cdd:cd01476     79 TTATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDpgtVDTEELHSITG-- 155

                   ....*..
gi 2024367818 1198 SERHVFF 1204
Cdd:cd01476    156 NEDHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
157-312 6.20e-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: 6.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIgRFNFRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPR--IEWHLNAYGTKDAVLDAVRNLPYKGGN 234
Cdd:cd01476      1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  235 TLTGLALTYILeNSFKPEAGARPGVSKIGILITDGKSQDDVIPPAKNLR-DAGIELFAIGVK---NADINELKEIASEPD 310
Cdd:cd01476     80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGdpgTVDTEELHSITGNED 158

                   ..
gi 2024367818  311 ST 312
Cdd:cd01476    159 HI 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
158-294 9.16e-23

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: 97.46  E-value: 9.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFN-FRLVRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIEWHLNAYGTKDA-----VLDAVRNLPYK 231
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYYP 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024367818  232 GGNTLTGLALTYILENSFKPeAGARPGVSKIGILITDGKSQDD--VIPPAKNLRDAGIELFAIGV 294
Cdd:cd01471     82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGV 145
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1490-1718 7.13e-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: 100.75  E-value: 7.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1490 GHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiQGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQRGLP 1569
Cdd:NF038329   117 GEKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1570 GKDGPTGPQGPPGPVGIPGAPGVPGITGSQGPQGDVGAPGAPGPKGERGERG-DLQSQAMVRAVARQVCEQLIQGhmary 1648
Cdd:NF038329   177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpAGDGQQGPDGDPGPTGEDGPQG----- 251
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1649 nsilnqipsqsvstrtiagppgepgrpgapgpqgEQGSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG 1718
Cdd:NF038329   252 ----------------------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
316-714 3.61e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 100.46  E-value: 3.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  316 NVADFNFMNSIVEGLTRTVCSRVEEQEKEIKGTIAASLGAPTDLVTSDITARGFRVSWTHSPG-KVEKYRVVYYPTRGGQ 394
Cdd:COG3401     12 GIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGtTSGVAAVAVAAAPPTA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  395 PEEVVVDGSSSTAVLKNlmSLTEYQIAVFAIYSNAASEGLRGTETTLALPMASDLKLYDVSHSSMRAKWNGVAGATGYMI 474
Cdd:COG3401     92 TGLTTLTGSGSVGGATN--TGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  475 LYAPLTEGLAADEKEIKIGEASTELELDGLLPNTEYTVTVYAMFGEEASDPLTG----QETTLPlSPPSNLKFSDVGHNS 550
Cdd:COG3401    170 VSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPP-SAPTGLTATADTPGS 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  551 AKLTWDPAS-KNVKGYRIMYVKTDGTETNEVEVGPVSTHTLKSLTALTEYTVAIFSLYDEG----QSEPLTGsfTTRKVP 625
Cdd:COG3401    249 VTLSWDPVTeSDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnesaPSNVVSV--TTDLTP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  626 P--PQHLEVDEASTDSFRVSWKPTSS-DIAFYRLAWIPLDGGESEEVVLSGDADSYVIEGLLPNTEYEVSLLAVFDDETE 702
Cdd:COG3401    327 PaaPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNE 406
                          410
                   ....*....|..
gi 2024367818  703 SEVVAVLGATIV 714
Cdd:COG3401    407 SAPSEEVSATTA 418
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1487-1718 1.87e-20

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: 96.51  E-value: 1.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1487 GAKGHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiQGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDG---AQ 1563
Cdd:NF038329   162 GPAGPQGEAGPQGPAGKDGE--------------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGeagPA 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1564 GQRGLPGKDGPTGPQGPPGpvgipgapgvPGITGSQGPQGDVGAPGAPGPKGERGERGdLQSQAMVRAVARQVCEQLIQG 1643
Cdd:NF038329   222 GEDGPAGPAGDGQQGPDGD----------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG-PDGPDGKDGERGPVGPAGKDG 290
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024367818 1644 HMARynsilNQIPSQSvstrtiagppgepgrpgapgpqGEQGSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG 1718
Cdd:NF038329   291 QNGK-----DGLPGKD----------------------GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
1044-1223 4.38e-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: 84.10  E-value: 4.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDdNFNKIISFLYSTVgalDKIGPDGTQVAIIQFSDDPRTEFKLNAYKTKETL-LEAIQQIAyKGGN 1122
Cdd:cd01474      5 FDLYFVLDKSGSVAA-NWIEIYDFVEQLV---DRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVT-PSGQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1123 TKTGKAIKHAREVLFTGEAGMRKgIPKVLVVITDGRSQDDV-------NKVSREMqldGFSFFAIGVADADYSELVNIGS 1195
Cdd:cd01474     80 TYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNGhkypeheAKLSRKL---GAIVYCVGVTDFLKSQLINIAD 155
                          170       180
                   ....*....|....*....|....*....
gi 2024367818 1196 kpSERHVFFVDD-FDAFTKIEDELITFVC 1223
Cdd:cd01474    156 --SKEYVFPVTSgFQALSGIIESVVKKAC 182
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
1045-1182 3.22e-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: 81.66  E-value: 3.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1045 DLVFLVDGSWSIGDDN-FNKIISFLYSTVGALDkIGPDGTQVAIIQFSDDPRTEFKLNAYKT--KETLLEAI---QQIAY 1118
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLN-ISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIralLSLYY 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818 1119 KGGNTKTGKAIKHAREVLFTGeAGMRKGIPKVLVVITDGRSQDDVN--KVSREMQLDGFSFFAIGV 1182
Cdd:cd01471     81 PNGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
157-314 5.20e-16

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: 78.20  E-value: 5.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFNF----RLVRLFLENLVSAFNV--GSEKTRVGLAQYSGDPRIEW-HLNAYGTKDAVLDAVRNLP 229
Cdd:cd01480      3 VDITFVLDSSESVGLQNFditkNFVKRVAERFLKDYYRkdPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  230 YKGGNTLTGLALTYILENSFKpeaGARPGVSKIGILITDGKSQ---DDVIPPAKNLRD-AGIELFAIGVKNADINELKEI 305
Cdd:cd01480     83 YIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgspDGGIEKAVNEADhLGIKIFFVAVGSQNEEPLSRI 159

                   ....*....
gi 2024367818  306 ASEPDSTHV 314
Cdd:cd01480    160 ACDGKSALY 168
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
1044-1160 1.72e-15

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: 76.66  E-value: 1.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDNFN-------KIISFLYSTvgALDKIGPDGTQVAIIQFSDDPRTEF-KLNAYKTKETLLEAIQQ 1115
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDitknfvkRVAERFLKD--YYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDN 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024367818 1116 IAYKGGNTKTGKAIKHAREVLFTGEagmRKGIPKVLVVITDGRSQ 1160
Cdd:cd01480     81 LEYIGGGTFTDCALKYATEQLLEGS---HQKENKFLLVITDGHSD 122
fn3 pfam00041
Fibronectin type III domain;
625-696 1.97e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 1.97e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818  625 PPPQHLEVDEASTDSFRVSWKP---TSSDIAFYRLAWIPLDGGESE-EVVLSGDADSYVIEGLLPNTEYEVSLLAV 696
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
536-621 4.17e-14

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: 69.45  E-value: 4.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  536 SPPSNLKFSDVGHNSAKLTWDPAS---KNVKGYRIMYVKTDGTETNEVEVGPVST--HTLKSLTALTEYTVAIFSLYDEG 610
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSEtsYTLTGLKPGTEYEFRVRAVNGGG 81
                           90
                   ....*....|..
gi 2024367818  611 QSEPLT-GSFTT 621
Cdd:cd00063     82 ESPPSEsVTVTT 93
VWA_2 pfam13519
von Willebrand factor type A domain;
1046-1154 4.76e-14

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 69.63  E-value: 4.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1046 LVFLVDGSWSIGDD-----NFNKIISFLYSTVGALDkigpdGTQVAIIQFSDDPRTEFKLNayKTKETLLEAIQQIAYKG 1120
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLP-----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKG 73
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024367818 1121 GNTKTGKAIKHAREVLFTgeagMRKGIPKVLVVI 1154
Cdd:pfam13519   74 GGTNLAAALQLARAALKH----RRKNQPRRIVLI 103
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1486-1621 1.53e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.94  E-value: 1.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1486 RGAKGHRGDPGPKGPDGPRGEIGVPGPQGPPGPQGPSGLSIQ----GLPGPPG--EKGEKGDLGFPGLQGVPGASGSPGR 1559
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPagedGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGK 258
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024367818 1560 DGAQGQRGLPGKDGPTGPqgppgpvgipgapgvPGITGSQGPQGDVGAPGAPGPKGERGERG 1621
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKdge---------rgpVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1486-1614 3.48e-13

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.17  E-value: 3.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1486 RGAKGHRGDPGPKGPDGPRGEIGVPgpqgppgpqgpsglsiqGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQ 1565
Cdd:NF038329   244 TGEDGPQGPDGPAGKDGPRGDRGEA-----------------GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024367818 1566 R---GLPGKDGPTGPqgppgpvgipgapgvPGITGSQGPQGDVGAPGAPGPK 1614
Cdd:NF038329   307 NgkdGLPGKDGKDGQ---------------PGKDGLPGKDGKDGQPGKPAPK 343
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
157-308 4.83e-13

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: 71.12  E-value: 4.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  157 ADIVILVDGSWSIGRFN-FRLVRLFLENLVSAFnvgSEKTRVGLAQYSGDPRIEWHLnaygTKD--AVLDAVRNLPYKGG 233
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPL----TRDreALKRALDELPPGGG 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  234 nTLTGLALTYILEnSFKPEagaRPGVSKIGILITDGKSQDDVIPP---AKNLRDAGIELFAIGVKNADINE--LKEIASE 308
Cdd:COG1240    166 -TPLGDALALALE-LLKRA---DPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIAEA 240
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
625-696 1.50e-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: 65.21  E-value: 1.50e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818  625 PPPQHLEVDEASTDSFRVSWKP---TSSDIAFYRLAWIPLDGGESEEV-VLSGDADSYVIEGLLPNTEYEVSLLAV 696
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPpedDGGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
354-432 7.73e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 7.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  354 GAPTDLVTSDITARGFRVSWTHSP---GKVEKYRVVYYPTRGGQPE-EVVVDGSSSTAVLKNLMSLTEYQIAVFAIYSNA 429
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ...
gi 2024367818  430 ASE 432
Cdd:pfam00041   81 EGP 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1528-1572 1.11e-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: 61.36  E-value: 1.11e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024367818 1528 GLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQRGLPGKD 1572
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
fn3 pfam00041
Fibronectin type III domain;
536-614 1.53e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.05  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  536 SPPSNLKFSDVGHNSAKLTWDPASKN---VKGYRIMYVKTDGTE--TNEVEVGPVSTHTLKSLTALTEYTVAIFSLYDEG 610
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGngpITGYEVEYRPKNSGEpwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....
gi 2024367818  611 QSEP 614
Cdd:pfam00041   81 EGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
31-112 1.90e-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: 62.13  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   31 SPPTRLRYNVVNPDSVQISWKAPK---GQFSGYKLLVTPSSGGKTNQLILQN-TATKAIIQGLIPDQNYALQIIAFSDDK 106
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                   ....*.
gi 2024367818  107 ESKPAQ 112
Cdd:cd00063     82 ESPPSE 87
fn3 pfam00041
Fibronectin type III domain;
837-915 2.15e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  837 SAPRNLRVSDEWYNRLRISWDAPPSPTM---GYRIVYKSINVPGPALETFVGDDINTILILNLFSGTEYSVKVFASYSTG 913
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ..
gi 2024367818  914 FS 915
Cdd:pfam00041   81 EG 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
837-921 2.64e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 61.74  E-value: 2.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  837 SAPRNLRVSDEWYNRLRISWDAPP---SPTMGYRIVYKSINVPGPALETFVGDDINTILILNLFSGTEYSVKVFASYSTG 913
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                   ....*...
gi 2024367818  914 FSDALTGV 921
Cdd:cd00063     82 ESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
354-432 3.37e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 61.36  E-value: 3.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  354 GAPTDLVTSDITARGFRVSWTHSP---GKVEKYRVVYYPTRGGQPEEV-VVDGSSSTAVLKNLMSLTEYQIAVFAIYSNA 429
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                   ...
gi 2024367818  430 ASE 432
Cdd:cd00063     82 ESP 84
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1541-1718 4.17e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 67.24  E-value: 4.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1541 DLGFPGLQGVPGASGSPGRDGAQGQRGlpgKDGPTGPQGPPGPVGIPGApgvPGITGSQGPQGDVGAPGAPGPKGERGER 1620
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRG---DRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1621 GDlQSQAMVRAVARQVCEQLIQGhmarynsilnqipSQSVSTRTIAGPPGEPGRPGAPGPQGEQGSPGMQGFPGNPGQPG 1700
Cdd:NF038329   186 GP-AGEKGPQGPRGETGPAGEQG-------------PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
                          170
                   ....*....|....*...
gi 2024367818 1701 RPGERGLPGEKGDRGNPG 1718
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAG 269
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
625-696 5.56e-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: 60.32  E-value: 5.56e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818   625 PPPQHLEVDEASTDSFRVSWKPTSSDIAF-YRLAWIPLDGGES---EEVVLSGDADSYVIEGLLPNTEYEVSLLAV 696
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
536-612 6.07e-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: 60.32  E-value: 6.07e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   536 SPPSNLKFSDVGHNSAKLTWD-PASKNVKGYRIMYV---KTDGTETNEVEVGPVST-HTLKSLTALTEYTVAIFSLYDEG 610
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRveyREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRVRAVNGAG 81

                    ..
gi 2024367818   611 QS 612
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
31-110 6.61e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 6.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   31 SPPTRLRYNVVNPDSVQISWKAPK---GQFSGYKLLVTP-SSGGKTNQLILQNTATKAIIQGLIPDQNYALQIIAFSDDK 106
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....
gi 2024367818  107 ESKP 110
Cdd:pfam00041   81 EGPP 84
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1528-1617 1.29e-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: 58.27  E-value: 1.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1528 GLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDGAQGQRGLPGkdgptgPQgppgpvgipgapgvpgitgsqgpqgdvGA 1607
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG------PP---------------------------GP 47
                           90
                   ....*....|
gi 2024367818 1608 PGAPGPKGER 1617
Cdd:pfam01391   48 PGAPGAPGPP 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
1044-1189 3.71e-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: 62.65  E-value: 3.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDDN-FNKIISFLYSTVGALDKigpdGTQVAIIQFSDDPRTEFKLNayKTKETLLEAIQQIAYKGGn 1122
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG- 165
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1123 TKTGKAIKHAREVLftgeAGMRKGIPKVLVVITDGR---SQDDVNKVSREMQLDGFSFFAIGVADADYSE 1189
Cdd:COG1240    166 TPLGDALALALELL----KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDE 231
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
1045-1193 1.15e-09

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 61.23  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1045 DLVFLVDGSWSIGDDNFNKIISFLYSTVGALdkigPDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYKGGnTK 1124
Cdd:COG2425    120 PVVLCVDTSGSMAGSKEAAAKAAALALLRAL----RPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TD 194
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024367818 1125 TGKAIKHAREVLFTGEAGmrkgiPKVLVVITDGRSQDDVNKVSREM--QLDGFSFFAIGVADADYSELVNI 1193
Cdd:COG2425    195 IAPALRAALELLEEPDYR-----NADIVLITDGEAGVSPEELLREVraKESGVRLFTVAIGDAGNPGLLEA 260
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
158-335 1.52e-09

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 59.64  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFNFRL-VRLFLENLVSAFNVGSEKTRVGLAQYSGDPRIewhLNAYG-----TKDAVLDAVRNLP-- 229
Cdd:cd01473      2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRD---VVPFSdeeryDKNELLKKINDLKns 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  230 YK-GGNTLTGLALTYILENSFKPEaGARPGVSKIGILITDGksqDDVIPPAKNLRDAGIE-------LFAIGVKNADINE 301
Cdd:cd01473     79 YRsGGETYIVEALKYGLKNYTKHG-NRRKDAPKVTMLFTDG---NDTSASKKELQDISLLykeenvkLLVVGVGAASENK 154
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2024367818  302 LKEIA--SEPDSTHVYNV-ADFNFMNSIVEGLTRTVC 335
Cdd:cd01473    155 LKLLAgcDINNDNCPNVIkTEWNNLNGISKFLTDKIC 191
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
1044-1182 1.55e-09

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 61.27  E-value: 1.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1044 ADLVFLVDGSWSIGDdnfNKIISFLYSTVGALDKIGPDGTqVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIaYKGGNT 1123
Cdd:COG2304     92 LNLVFVIDVSGSMSG---DKLELAKEAAKLLVDQLRPGDR-VSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAGGGT 166
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024367818 1124 KTGKAIKHAREVLftgEAGMRKGIPKVLVVITDGR------SQDDVNKVSREMQLDGFSFFAIGV 1182
Cdd:COG2304    167 ALGAGLELAYELA---RKHFIPGRVNRVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGV 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1490-1566 2.84e-09

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: 54.42  E-value: 2.84e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024367818 1490 GHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiqglPGPPGEKgekgdlGFPGLQGVPGASGSPGRDGAQGQR 1566
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGP-----------------------PGPPGEP------GPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1531-1620 4.50e-09

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: 54.04  E-value: 4.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1531 GPPGEkgekgdlgfPGLQGVPGASGSPGRDGAQGQRGLPgkdgptgpqgppgpvgipgapgvpGITGSQGPQGDVGAPGA 1610
Cdd:pfam01391    1 GPPGP---------PGPPGPPGPPGPPGPPGPPGPPGPP------------------------GEPGPPGPPGPPGPPGP 47
                           90
                   ....*....|
gi 2024367818 1611 PGPKGERGER 1620
Cdd:pfam01391   48 PGAPGAPGPP 57
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
837-915 5.15e-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: 54.93  E-value: 5.15e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   837 SAPRNLRVSDEWYNRLRISWDAPPSP-TMGYRIVYKSINVPGPALETFV--GDDINTILILNLFSGTEYSVKVFASYSTG 913
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81

                    ..
gi 2024367818   914 FS 915
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
745-824 8.32e-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: 54.16  E-value: 8.32e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   745 VRNLVIDDETTSSLRVVWDISDHNAQQFRVTYLTAKGDRAEEAVRTIMVPGRQNTLLLQPLLPDTEYKVTITPIYADGEG 824
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
156-335 1.28e-08

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: 56.75  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  156 IADIVILVDGSWSIGRfNFRLVRLFLENLVSAFNvgSEKTRVGLAQYSGDPRIEWHLNAYGTK--DAVLDAVRNLPykGG 233
Cdd:cd01474      4 HFDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAiiKGLEVLKKVTP--SG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  234 NTLTGLALTYILENSFKPEAGARPgVSKIGILITDGKSQDDV----IPPAKNLRDAGIELFAIGVKNADINELKEIASEP 309
Cdd:cd01474     79 QTYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSK 157
                          170       180
                   ....*....|....*....|....*..
gi 2024367818  310 DstHVYNVAD-FNFMNSIVEGLTRTVC 335
Cdd:cd01474    158 E--YVFPVTSgFQALSGIIESVVKKAC 182
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
354-433 1.75e-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: 53.39  E-value: 1.75e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   354 GAPTDLVTSDITARGFRVSWTHSPGKVEKYRVVYY----PTRGGQPEEVVVDGSSSTAVLKNLMSLTEYQIAVFAIysNA 429
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYrveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV--NG 79

                    ....
gi 2024367818   430 ASEG 433
Cdd:smart00060   80 AGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
447-516 2.06e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 2.06e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024367818   447 SDLKLYDVSHSSMRAKWNGVA--GATGYMILYAPLTEGLAADEKEIKIGEASTELELDGLLPNTEYTVTVYA 516
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPddGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
745-824 2.12e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  745 VRNLVIDDETTSSLRVVWDISDHNA---QQFRVTYLTAKGdraEEAVRTIMVPGRQNTLLLQPLLPDTEYKVTITPIYAD 821
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNS---GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

                   ...
gi 2024367818  822 GEG 824
Cdd:pfam00041   80 GEG 82
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1546-1621 3.12e-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: 3.12e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818 1546 GLQGVPGASGSPGRDGAQGQRGLPgkdgptgpqgppgpvgipgapgvpGITGSQGPQGDVGAPGAPGPKGERGERG 1621
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPP------------------------GPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
VWA_2 pfam13519
von Willebrand factor type A domain;
159-259 3.43e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.06  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  159 IVILVDGSWSIGRFNFRLVRL-----FLENLVSAFNvgseKTRVGLAQYSGDPRIEWHLNayGTKDAVLDAVRNLPYKGG 233
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRLeaakdAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74
                           90       100
                   ....*....|....*....|....*.
gi 2024367818  234 NTLTGLALTYILENSFKPEAGARPGV 259
Cdd:pfam13519   75 GTNLAAALQLARAALKHRRKNQPRRI 100
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1685-1770 8.00e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 8.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1685 GSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPGvgtqgprgppgstgppgesrtgspgppgSpgprgpaghTGPPGSQG 1764
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG----------------------------P---------PGPPGPPG 43

                   ....*.
gi 2024367818 1765 PAGPPG 1770
Cdd:pfam01391   44 PPGPPG 49
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
31-108 1.67e-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: 1.67e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818    31 SPPTRLRYNVVNPDSVQISWKAPK-GQFSGYKL---LVTPSSGGKTNQLILQNTATKAIIQGLIPDQNYALQIIAFSDDK 106
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPdDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81

                    ..
gi 2024367818   107 ES 108
Cdd:smart00060   82 EG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
447-532 2.68e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 50.19  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  447 SDLKLYDVSHSSMRAKWNGVAGA----TGYMILYAPLTEGlaaDEKEIKIGEAS-TELELDGLLPNTEYTVTVYAMFGEE 521
Cdd:cd00063      5 TNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSG---DWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNGGG 81
                           90
                   ....*....|.
gi 2024367818  522 ASDPLTGQETT 532
Cdd:cd00063     82 ESPPSESVTVT 92
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1593-1717 3.41e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 3.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1593 PGITGSQGPQGDVGAPGAPGPKGERGERgdlqsqamvravarqvceqliqghmarynsilnqipsqsvstrtiagppgep 1672
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPP---------------------------------------------------- 30
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024367818 1673 grpgapgpqgeqgspgmqGFPGNPGQPGRPGERGLPGEKGDRGNP 1717
Cdd:pfam01391   31 ------------------GEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1606-1718 4.90e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1606 GAPGAPGPKGERGERGdlqsqamvravarqvceqliqghmarynsilnqipsqsvstrtiagppgepgrpgapgPQGEQG 1685
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG----------------------------------------------------------PPGPPG 22
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2024367818 1686 SPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG 1718
Cdd:pfam01391   23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
fn3 pfam00041
Fibronectin type III domain;
447-516 1.20e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.18  E-value: 1.20e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024367818  447 SDLKLYDVSHSSMRAKWNGVAGA----TGYMILYAPLTEGLAadEKEIKIGEASTELELDGLLPNTEYTVTVYA 516
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPDGngpiTGYEVEYRPKNSGEP--WNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1487-1546 1.75e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 1.75e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1487 GAKGHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiQGLPGPPGEKGEKGDLGFPG 1546
Cdd:pfam01391   16 GPPGPPGPPGPPGPPGEPGP--------------------PGPPGPPGPPGPPGAPGAPG 55
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
745-833 2.08e-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: 47.88  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  745 VRNLVIDDETTSSLRVVWDISDHNA---QQFRVTYLTAKGDRAEEAVRTimvPGRQNTLLLQPLLPDTEYKVTITPIYAD 821
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpiTGYVVEYREKGSGDWKEVEVT---PGSETSYTLTGLKPGTEYEFRVRAVNGG 80
                           90
                   ....*....|...
gi 2024367818  822 GEGV-SVSAPGKT 833
Cdd:cd00063     81 GESPpSESVTVTT 93
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1560-1770 6.44e-06

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: 50.67  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1560 DGAQGQRGLpgkdgptgpQGPpgpvgipgapgvPGITGSQGPQGDVGAPGAPGPKGERGERGdlqsqamvravarQVCEQ 1639
Cdd:NF038329   116 DGEKGEPGP---------AGP------------AGPAGEQGPRGDRGETGPAGPAGPPGPQG-------------ERGEK 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1640 LIQGhmarynsilnqipsqsvstrtiagppgepgrpgapgpqgEQGSPGMQGFPGNPGQPGRPGERGLPGEKGDRGNPG- 1718
Cdd:NF038329   162 GPAG---------------------------------------PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGp 202
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024367818 1719 ---VGTQGPRGPPGSTGPPGESRTGSPGPPGSPGPRGPAGHTGPPGSQGPAGPPG 1770
Cdd:NF038329   203 ageQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAG 257
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
1045-1203 1.12e-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: 48.19  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1045 DLVFLVDGSWSIGDDNFNKIISFLYSTVGALDKIG-----PDGTQVAIIQFSDDPRTEFKLNAYKTKETLLEAIQQIAYK 1119
Cdd:cd01477     21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGtdyddPRSTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSLTD 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1120 GGNTKT---GKAIKHAREVLFTGEAGMRKGIPKVLVVIT---DGRSQDDVNKVSREMQLDGFSFfaIGVA---DADYSEL 1190
Cdd:cd01477    101 VSSTNAsylDTGLQAAEQMLAAGKRTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAI--ITVAftqDESSNLL 178
                          170
                   ....*....|...
gi 2024367818 1191 VNIGSKPSERHVF 1203
Cdd:cd01477    179 DKLGKIASPGMNF 191
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
154-306 1.23e-05

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 48.91  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  154 PAIADIVILVDGSWSIGRFNFRLVRLFLENLVSAFNvgsEKTRVGLAQYSGDPRIEWHLNAYGTKDAVLDAVRNLPYKGG 233
Cdd:COG2425    116 LLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG 192
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024367818  234 nTLTGLALTYILEnSFKPEAGARPGVskigILITDGKSQDDVIPPAKNLR--DAGIELFAIGVKNA-DINELKEIA 306
Cdd:COG2425    193 -TDIAPALRAALE-LLEEPDYRNADI----VLITDGEAGVSPEELLREVRakESGVRLFTVAIGDAgNPGLLEALA 262
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1047-1190 3.28e-05

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.84  E-value: 3.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1047 VFLVDGSWSIGDDN-------FNKIISFLYSTVGALDKIgpdgtQVAIIQFSDDPRTEFKLnayktkeTLLEAIQ-QIAY 1118
Cdd:COG4245      9 YLLLDTSGSMSGEPiealnegLQALIDELRQDPYALETV-----EVSVITFDGEAKVLLPL-------TDLEDFQpPDLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1119 KGGNTKTGKAIKHA-----REVLFTGEAGmrKGI-PKVLVVITDGRSQDD-----VNKVSREMQLDGFSFFAIGV-ADAD 1186
Cdd:COG4245     77 ASGGTPLGAALELLldlieRRVQKYTAEG--KGDwRPVVFLITDGEPTDSdweaaLQRLKDGEAAKKANIFAIGVgPDAD 154

                   ....
gi 2024367818 1187 YSEL 1190
Cdd:COG4245    155 TEVL 158
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
158-339 3.98e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 48.42  E-value: 3.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFNF--RLVRLfLENLVSAFNVGSEKTRVGLAQYSGDPR--IEWHLNAYGTKDAVLDAVR-----NL 228
Cdd:PTZ00441    44 DLYLLVDGSGSIGYHNWitHVIPM-LMGLIQQLNLSDDAINLYMSLFSNNTTelIRLGSGASKDKEQALIIVKslrktYL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  229 PYkgGNTLTGLALTYIlENSFKPEAGaRPGVSKIGILITDG--KSQDDVIPPAKNLRDAGIELFAIGVK---NADINELk 303
Cdd:PTZ00441   123 PY--GKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgiNHQFNRL- 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024367818  304 eIA----SEPdSTHVYNVADFNFMNSIVEGLTRTVCSRVE 339
Cdd:PTZ00441   198 -LAgcrpREG-KCKFYSDADWEEAKNLIKPFIAKVCTEVE 235
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
158-319 4.33e-05

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: 46.51  E-value: 4.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  158 DIVILVDGSWSIGRFNFRLVRLFLENL---VSAFNVgseKTRVGLAQYSGDP-RIEWHLNAYGTK-DAVLDAVRNLPYK- 231
Cdd:cd01470      2 NIYIALDASDSIGEEDFDEAKNAIKTLiekISSYEV---SPRYEIISYASDPkEIVSIRDFNSNDaDDVIKRLEDFNYDd 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  232 ---GGNTLTGLALTYILENSFKPEAGARPGVSKIG---ILITDGKS-------------QDDVI--PPAKNLRDAGIELF 290
Cdd:cd01470     79 hgdKTGTNTAAALKKVYERMALEKVRNKEAFNETRhviILFTDGKSnmggsplptvdkiKNLVYknNKSDNPREDYLDVY 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024367818  291 AIGV-KNADINELKEIASE-PDSTHVYNVAD 319
Cdd:cd01470    159 VFGVgDDVNKEELNDLASKkDNERHFFKLKD 189
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
1045-1194 4.75e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 43.07  E-value: 4.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1045 DLVFLVDGSWSIGDDNFNK-IISFLYSTVGALdKIGPDGTQVAIIQFSDDPRT--EFKLNAYKTKETLLEAIQQI--AYK 1119
Cdd:cd01473      2 DLTLILDESASIGYSNWRKdVIPFTEKIINNL-NISKDKVHVGILLFAEKNRDvvPFSDEERYDKNELLKKINDLknSYR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1120 -GGNTKTGKAIKHAREVlFTGEAGMRKGIPKVLVVITDGRSQDDVNKVSREMQL----DGFSFFAIGVADADYSELVNIG 1194
Cdd:cd01473     81 sGGETYIVEALKYGLKN-YTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLlykeENVKLLVVGVGAASENKLKLLA 159
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1527-1775 5.21e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1527 QGLPGPPGEKGEKGDLGFPGLQGVPGASGSPGRDG-----------AQGQRGLPGKDGPTGPQGPPGPVGIPGAPGVPGI 1595
Cdd:pfam09606  177 NGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGpadagaqmgqqAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQ 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1596 TGSQG------PQGDVGAPGAPGPKGERGERGDLQSQAMVRAVARQVCEQLIQGHMARYNSILNQIPSQSVSTRTIAGPP 1669
Cdd:pfam09606  257 LGMGInqmqqmPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQ 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1670 GEPGRPGAPGPQGEQGSPGMQGFPG-NPGQPGRPGERGLPgekgdrgNPGVGTQGprgppgstgppgesRTGSPGPPGSP 1748
Cdd:pfam09606  337 GGQVVALGGLNHLETWNPGNFGGLGaNPMQRGQPGMMSSP-------SPVPGQQV--------------RQVTPNQFMRQ 395
                          250       260
                   ....*....|....*....|....*..
gi 2024367818 1749 GPRGPAGHTGPPGSQGPAGPPGYCDPS 1775
Cdd:pfam09606  396 SPQPSVPSPQGPGSQPPQSHPGGMIPS 422
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1561-1705 2.31e-03

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: 37.86  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1561 GAQGQRGLPgkdgptgpqgppgpvgipgapgvpGITGSQGPQGDVGAPGAPGPKGERGergdlqsqamvravarqvceql 1640
Cdd:pfam01391    1 GPPGPPGPP------------------------GPPGPPGPPGPPGPPGPPGPPGEPG---------------------- 34
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024367818 1641 iqghmarynsilnqipsqsvstrtiagppgepgrpgapgpqgEQGSPGMQGFPGNPGQPGRPGER 1705
Cdd:pfam01391   35 ------------------------------------------PPGPPGPPGPPGPPGAPGAPGPP 57
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
232-320 3.32e-03

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 40.68  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818  232 GGNTLTGLALTYILE----NSFKPEAGARPGVSKIGILITDGKSQDDVIPPA-----KNLRDAGIELFAIGV-KNADINE 301
Cdd:COG4245     78 SGGTPLGAALELLLDlierRVQKYTAEGKGDWRPVVFLITDGEPTDSDWEAAlqrlkDGEAAKKANIFAIGVgPDADTEV 157
                           90
                   ....*....|....*....
gi 2024367818  302 LKEIASEPDSTHVYNVADF 320
Cdd:COG4245    158 LKQLTDPVRALDALDGLDF 176
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1486-1538 3.53e-03

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: 37.47  E-value: 3.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024367818 1486 RGAKGHRGDPGPKGPDGPRGEigvpgpqgppgpqgpsglsiqglPGPPGEKGE 1538
Cdd:pfam01391   27 PGPPGEPGPPGPPGPPGPPGP-----------------------PGAPGAPGP 56
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
1049-1209 4.27e-03

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: 40.35  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1049 LVDGSWSIGDDNFN---KIISFLYSTVGALDkIGPdgtQVAIIQFSDDPR-----TEFKLNaykTKETLLEAIQQIAYKG 1120
Cdd:cd01470      6 ALDASDSIGEEDFDeakNAIKTLIEKISSYE-VSP---RYEIISYASDPKeivsiRDFNSN---DADDVIKRLEDFNYDD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818 1121 GNTKTGKAIKHAREVLFTGEA--GMRKG-----IPKVLVVITDGRS-------------QDDVNK-----VSREMQLDGF 1175
Cdd:cd01470     79 HGDKTGTNTAAALKKVYERMAleKVRNKeafneTRHVIILFTDGKSnmggsplptvdkiKNLVYKnnksdNPREDYLDVY 158
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024367818 1176 SFfaiGVADADYSELVN-IGS-KPSERHVFFVDDFD 1209
Cdd:cd01470    159 VF---GVGDDVNKEELNdLASkKDNERHFFKLKDYE 191
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31-112 4.38e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.91  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024367818   31 SPPTRLRYNVVNPDSVQISWKAPKG-QFSGYKLLVTPSSGGKTNQLILQNTATKAIIQGLIPDQNYALQIIAFSDD-KES 108
Cdd:COG3401    328 AAPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAgNES 407

                   ....
gi 2024367818  109 KPAQ 112
Cdd:COG3401    408 APSE 411
 
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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