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Conserved domains on  [gi|1572616313|ref|NP_001355351|]
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collagen alpha-1(XIV) chain isoform 1 precursor [Mus musculus]

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 ...
 1032-1196 2.83e-88

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: 284.18  E-value: 2.83e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNT 1111
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1112 KTGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQDDVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSRHVF 1191
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1572616313 1192 FVDDF 1196
Cdd:cd01482    160 NVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 158-321 8.39e-83

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: 268.77  E-value: 8.39e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL 237
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTHVYN 317
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1572616313  318 VAEF 321
Cdd:cd01482    161 VADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1230-1425 3.10e-53

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.87  E-value: 3.10e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1230 GFKMMEMFGLVEKDFSAVEGVSMEPGtfnlFPCYQIHKDALVSQPTKYLHPEGLPSDYTMSFLFRIlpdTPQEPFALWEI 1309
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1310 LNKNSEPLVGIILDNGGKTLTYFNYDYTGDFQTVTFEGpdiRKMFYGSFHKLHVVVSKTLAKVVVDCKEVGQKAINASA- 1388
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1572616313  1389 -NITSDGVEVLGRMVRSRGPngnsAPFQLQMFDIVCST 1425
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
372-769 7.89e-18

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 89.68  E-value: 7.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  372 VNWTQSPGKVEKYRVVYYPTRGGKPEEVVVDGSVSSTVLK-----NLMSSTEYQIAVFAVSAHTASEGLRGAETTLA--L 444
Cdd:COG3401    153 ANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLvdgggDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPttP 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  445 PMA-SDLELYDVTENSMRVRWDAVP--GATGYLILYAPlteglAGDEKEMKIGETH----TDielSGLFPNTEYTVTVYA 517
Cdd:COG3401    233 PSApTGLTATADTPGSVTLSWDPVTesDATGYRVYRSN-----SGDGPFTKVATVTttsyTD---TGLTNGTTYYYRVTA 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  518 M--FGEE--ASDPATGQETTLPLTPPRNLRISNVGSNSARLTWDPASGK-ISGYRIVYTSADGTEINEV-EVDPITTFPL 591
Cdd:COG3401    305 VdaAGNEsaPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIaETVTTTSYTD 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  592 KGLTPLTEYSIAIFSIYEEGQSLPLVGEFTTEEVPAQQ----YLEIDEVKTDSFRVTWHPLSAEEGQHKLMWIPVYGGKT 667
Cdd:COG3401    385 TGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASgeslTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  668 QEVDLKEEQDSYVIEGLDPGTEYEVSLLAVLDDGSESEVVTAVGTTLDDFWTEAPTAIEPTSPVTSVLQTGIRNLVVDDE 747
Cdd:COG3401    465 GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544

                          410       420
                   ....*....|....*....|..
gi 1572616313  748 TATSLRVSWDISDSNVEQFRVT 769
Cdd:COG3401    545 VLITDLVSLTTSASSSVSGAGL 566
fn3 pfam00041
Fibronectin type III domain;
833-902 4.64e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 4.64e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1572616313  833 PQNLRVSEEWYNRVRITWDPP---SGPVKGYRIVYKPVSVPGQTLETFVGADINTIVMTNLLSGMDYNVKIFA 902
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 3.33e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 67.62  E-value: 3.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1479 QQGEQGPKGPEGPRGETGPagpqgppgpqgpsglsiQGMPGMPGDKGDKGDAGLPGPQGVPGGVGSPGRDGSPGQRGFPG 1558
Cdd:NF038329   166 PQGEAGPQGPAGKDGEAGA-----------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1559 KDGSSGPPGPPGpigipgapgvPGITGSMGPQGALGPPGVPGAKGERGERG 1609
Cdd:NF038329   229 PAGDGQQGPDGD----------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 6.77e-11

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVAPASGGKTNQMNLQN-TATKAIIQGLLPEQNYTVQLIAYYKDKE 107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ....*
gi 1572616313  108 SKPAQ 112
Cdd:cd00063     83 SPPSE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 740-818 1.84e-10

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


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 1.84e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572616313   740 RNLVVDDETATSLRVSWDISDSNVEQFRVTYLKAQGDPMEEVVGTVMVPGVQNSLLLKALLPDTEYKVTVTPVYTVGEG 818
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 923-998 4.52e-04

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


The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain]  Cd Length: 85  Bit Score: 40.86  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  923 VTDLQANQVEMTSLCARWQI----HRHATAYRIVLESLQDTQA-QESTVGGGVNRHCFYGLQPDSEYKISVYTKLQELEG 997
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 1572616313  998 P 998
Cdd:pfam00041   83 P 83
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1032-1196 2.83e-88

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: 284.18  E-value: 2.83e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNT 1111
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1112 KTGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQDDVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSRHVF 1191
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1572616313 1192 FVDDF 1196
Cdd:cd01482    160 NVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 158-321 8.39e-83

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: 268.77  E-value: 8.39e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL 237
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTHVYN 317
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1572616313  318 VAEF 321
Cdd:cd01482    161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
159-329 4.19e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 221.38  E-value: 4.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  159 DIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL- 237
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQD-DIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTHVY 316
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|...
gi 1572616313  317 NVAEFDLMHTVVE 329
Cdd:pfam00092  161 TVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1033-1205 6.05e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 220.99  E-value: 6.05e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1033 DLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNTK 1112
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1113 -TGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQD-DVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSRHV 1190
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 1572616313 1191 FFVDDFDAFKKIEDE 1205
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1230-1425 3.10e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.87  E-value: 3.10e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1230 GFKMMEMFGLVEKDFSAVEGVSMEPGtfnlFPCYQIHKDALVSQPTKYLHPEGLPSDYTMSFLFRIlpdTPQEPFALWEI 1309
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1310 LNKNSEPLVGIILDNGGKTLTYFNYDYTGDFQTVTFEGpdiRKMFYGSFHKLHVVVSKTLAKVVVDCKEVGQKAINASA- 1388
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1572616313  1389 -NITSDGVEVLGRMVRSRGPngnsAPFQLQMFDIVCST 1425
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1033-1199 2.60e-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: 2.60e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1033 DLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYK-GGNT 1111
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1112 KTGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQD---DVNKISREMQADGFNIFAIGV-ADADYSELVQIGSKPSS 1187
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|..
gi 1572616313  1188 RHVFFVDDFDAF 1199
Cdd:smart00327  160 VYVFLPELLDLL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 159-324 4.14e-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: 175.72  E-value: 4.14e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   159 DIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYK-GGNTL 237
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQD---DIIPPSRNLRESGVELFAIGVKNA-DLSELQEIASEPDST 313
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1572616313   314 HVYNVAEFDLM 324
Cdd:smart00327  161 YVFLPELLDLL 171
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
372-769 7.89e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 89.68  E-value: 7.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  372 VNWTQSPGKVEKYRVVYYPTRGGKPEEVVVDGSVSSTVLK-----NLMSSTEYQIAVFAVSAHTASEGLRGAETTLA--L 444
Cdd:COG3401    153 ANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLvdgggDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPttP 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  445 PMA-SDLELYDVTENSMRVRWDAVP--GATGYLILYAPlteglAGDEKEMKIGETH----TDielSGLFPNTEYTVTVYA 517
Cdd:COG3401    233 PSApTGLTATADTPGSVTLSWDPVTesDATGYRVYRSN-----SGDGPFTKVATVTttsyTD---TGLTNGTTYYYRVTA 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  518 M--FGEE--ASDPATGQETTLPLTPPRNLRISNVGSNSARLTWDPASGK-ISGYRIVYTSADGTEINEV-EVDPITTFPL 591
Cdd:COG3401    305 VdaAGNEsaPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIaETVTTTSYTD 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  592 KGLTPLTEYSIAIFSIYEEGQSLPLVGEFTTEEVPAQQ----YLEIDEVKTDSFRVTWHPLSAEEGQHKLMWIPVYGGKT 667
Cdd:COG3401    385 TGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASgeslTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  668 QEVDLKEEQDSYVIEGLDPGTEYEVSLLAVLDDGSESEVVTAVGTTLDDFWTEAPTAIEPTSPVTSVLQTGIRNLVVDDE 747
Cdd:COG3401    465 GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544

                          410       420
                   ....*....|....*....|..
gi 1572616313  748 TATSLRVSWDISDSNVEQFRVT 769
Cdd:COG3401    545 VLITDLVSLTTSASSSVSGAGL 566
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 538-622 8.88e-16

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 8.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  538 PPRNLRISNVGSNSARLTWDPAS---GKISGYRIVYTSADGTEINEVEVDPI--TTFPLKGLTPLTEYSIAIFSIYEEGQ 612
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNGGGE 82

                           90
                   ....*....|.
gi 1572616313  613 SLPL-VGEFTT 622
Cdd:cd00063     83 SPPSeSVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
538-615 1.32e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 1.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  538 PPRNLRISNVGSNSARLTWDPA---SGKISGYRIVYTSADGTEI-NEVEVDP-ITTFPLKGLTPLTEYSIAIFSIYEEGQ 612
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPwNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1572616313  613 SLP 615
Cdd:pfam00041   82 GPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 538-613 1.82e-13

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.82e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   538 PPRNLRISNVGSNSARLTWDPAS-----GKISGYRIVYTSADGTEINEVEVDPITTFPLKGLTPLTEYSIAIFSIYEEGQ 612
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1572616313   613 S 613
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
833-902 4.64e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 4.64e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1572616313  833 PQNLRVSEEWYNRVRITWDPP---SGPVKGYRIVYKPVSVPGQTLETFVGADINTIVMTNLLSGMDYNVKIFA 902
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 831-913 2.17e-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: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  831 SGPQNLRVSEEWYNRVRITWDPPS---GPVKGYRIVYKPVSVPGQTLETFVGADINTIVMTNLLSGMDYNVKIFASQASG 907
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ....*.
gi 1572616313  908 FSDALT 913
Cdd:cd00063     82 ESPPSE 87
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 158-309 3.02e-11

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: 65.73  E-value: 3.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFN-FRLVRNFLENLVTAFnvgSEKTRIGLAQYSGdpRIEWHLNAFNTKDEVIDAVRSLPYKGGNT 236
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGGTP 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  237 LT---GLALNFIfensfkpeAGSRSGVSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGV--KNADLSELQEIAS 308
Cdd:COG1240    168 LGdalALALELL--------KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVgtEAVDEGLLREIAE 239


                   .
gi 1572616313  309 E 309
Cdd:COG1240    240 A 240
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 3.33e-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: 67.62  E-value: 3.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1479 QQGEQGPKGPEGPRGETGPagpqgppgpqgpsglsiQGMPGMPGDKGDKGDAGLPGPQGVPGGVGSPGRDGSPGQRGFPG 1558
Cdd:NF038329   166 PQGEAGPQGPAGKDGEAGA-----------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1559 KDGSSGPPGPPGpigipgapgvPGITGSMGPQGALGPPGVPGAKGERGERG 1609
Cdd:NF038329   229 PAGDGQQGPDGD----------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 6.77e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVAPASGGKTNQMNLQN-TATKAIIQGLLPEQNYTVQLIAYYKDKE 107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ....*
gi 1572616313  108 SKPAQ 112
Cdd:cd00063     83 SPPSE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 740-818 1.84e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 1.84e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572616313   740 RNLVVDDETATSLRVSWDISDSNVEQFRVTYLKAQGDPMEEVVGTVMVPGVQNSLLLKALLPDTEYKVTVTPVYTVGEG 818
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
740-818 2.17e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 2.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  740 RNLVVDDETATSLRVSWDIS---DSNVEQFRVTYLKAQGdpmEEVVGTVMVPGVQNSLLLKALLPDTEYKVTVTPVYTVG 816
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNS---GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1572616313  817 EG 818
Cdd:pfam00041   81 EG 82
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1032-1202 2.89e-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: 63.03  E-value: 2.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDN-FNKIINFLYSTVGALDKigadGTQVAMVQFTDDPRTEFKLDSykTKETLLDAIRHISYKGGn 1110
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPGGG- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1111 TKTGKAIKHVRDTLFTSDSGTRrgipKVIVVITDGR---SQDDVNKISREMQADGFNIFAIGVADADYSE--LVQIgSKP 1185
Cdd:COG1240    166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREI-AEA 240

                          170
                   ....*....|....*..
gi 1572616313 1186 SSRHVFFVDDFDAFKKI 1202
Cdd:COG1240    241 TGGRYFRADDLSELAAI 257
fn3 pfam00041
Fibronectin type III domain;
32-110 5.81e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 5.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   32 PPTRLRYNVISHDSIQISWKAPR---GKFGGYKLLVAPA-SGGKTNQMNLQNTATKAIIQGLLPEQNYTVQLIAYYKDKE 107
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1572616313  108 SKP 110
Cdd:pfam00041   82 GPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 740-827 1.11e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.12  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  740 RNLVVDDETATSLRVSWD---ISDSNVEQFRVTYLKAQGDPMEEVVGTvmvPGVQNSLLLKALLPDTEYKVTVTPVYTVG 816
Cdd:cd00063      5 TNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYREKGSGDWKEVEVT---PGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1572616313  817 EGV-SVSAPGKT 827
Cdd:cd00063     82 ESPpSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 831-909 2.31e-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: 2.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   831 SGPQNLRVSEEWYNRVRITWDPPS-----GPVKGYRIVYKPVSVPGQTLEtfVGADINTIVMTNLLSGMDYNVKIFASQA 905
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVN--VTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1572616313   906 SGFS 909
Cdd:smart00060   80 AGEG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 1.81e-07

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: 55.68  E-value: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1479 QQGEQGPKGPEGPRGEtgpagpqgppgpqgpsglsiQGMPGMPGDKGDKGDAglpgpqgvpggvgspgrdGSPGQRGFPG 1558
Cdd:NF038329   118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPA------------------GPPGPQGERG 159

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1559 KDGSSGPPGPpgpigipgapgvPGITGSMGPQGALGPPGVPGAKGERGERG 1609
Cdd:NF038329   160 EKGPAGPQGE------------AGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 32-108 6.94e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.76  E-value: 6.94e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313    32 PPTRLRYNVISHDSIQISWKAP-RGKFGGYKL---LVAPASGGKTNQMNLQNTATKAIIQGLLPEQNYTVQLIAYYKDKE 107
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1572616313   108 S 108
Cdd:smart00060   83 G 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 4.46e-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: 51.44  E-value: 4.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1479 QQGEQGPKGPEGPRGETGPAGPQGPPGPQGPSGLSIQGMPGMPGDKGDKGDAGLpgpqgvpggvgspgrDGSPGQRGFPG 1558
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE---------------DGPQGPDGPAG 257

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1559 KDGSSGPPGPpgpigipgapgvPGITGSMGPQGALGPPGVPGAKGERGERG 1609
Cdd:NF038329   258 KDGPRGDRGE------------AGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1024-1197 1.98e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 49.58  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1024 KEVCKAaKADLVFMVDGSWSIGDDNF-NKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKL--DSYKTKETLLDA 1100
Cdd:PTZ00441    36 EEVCNE-EVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLN-LSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALII 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1101 IRHISyKG----GNTKTGKAIKHVRDTLftSDSGTRRGIPKVIVVITDG--RSQDDVNKISREMQADGFNIFAIGVA--- 1171
Cdd:PTZ00441   114 VKSLR-KTylpyGKTNMTDALLEVRKHL--NDRVNRENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgi 190

                          170       180
                   ....*....|....*....|....*.
gi 1572616313 1172 DADYSELVqIGSKPSSRHVFFVDDFD 1197
Cdd:PTZ00441   191 NHQFNRLL-AGCRPREGKCKFYSDAD 215
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1516-1605 5.65e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1516 GMPGMPGDKGDKGDAglpgpqgvpggvgspgrdGSPGQRGFPGKDGSSGPPgppgpigipgapgvpGITGSMGPQGALGP 1595
Cdd:pfam01391    1 GPPGPPGPPGPPGPP------------------GPPGPPGPPGPPGPPGEP---------------GPPGPPGPPGPPGP 47

                           90
                   ....*....|
gi 1572616313 1596 PGVPGAKGER 1605
Cdd:pfam01391   48 PGAPGAPGPP 57
fn3 pfam00041
Fibronectin type III domain;
923-998 4.52e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.86  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  923 VTDLQANQVEMTSLCARWQI----HRHATAYRIVLESLQDTQA-QESTVGGGVNRHCFYGLQPDSEYKISVYTKLQELEG 997
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 1572616313  998 P 998
Cdd:pfam00041   83 P 83
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1032-1196 2.83e-88

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: 284.18  E-value: 2.83e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNT 1111
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1112 KTGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQDDVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSRHVF 1191
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1572616313 1192 FVDDF 1196
Cdd:cd01482    160 NVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 158-321 8.39e-83

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: 268.77  E-value: 8.39e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL 237
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTHVYN 317
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1572616313  318 VAEF 321
Cdd:cd01482    161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 158-321 6.37e-75

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: 245.99  E-value: 6.37e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL 237
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTHVYN 317
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                   ....
gi 1572616313  318 VAEF 321
Cdd:cd01472    161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1032-1196 1.05e-74

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 245.60  E-value: 1.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNT 1111
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLD-IGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1112 KTGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQDDVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSRHVF 1191
Cdd:cd01472     80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159


                   ....*
gi 1572616313 1192 FVDDF 1196
Cdd:cd01472    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
159-329 4.19e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 221.38  E-value: 4.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  159 DIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL- 237
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQD-DIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTHVY 316
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|...
gi 1572616313  317 NVAEFDLMHTVVE 329
Cdd:pfam00092  161 TVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1033-1205 6.05e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 220.99  E-value: 6.05e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1033 DLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNTK 1112
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1113 -TGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQD-DVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSRHV 1190
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 1572616313 1191 FFVDDFDAFKKIEDE 1205
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 158-316 2.68e-54

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 187.11  E-value: 2.68e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGN-T 236
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  237 LTGLALNFIFENSFKPeAGSRSGVSKIGILITDGKSQD--DIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTH 314
Cdd:cd01450     81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                   ..
gi 1572616313  315 VY 316
Cdd:cd01450    160 VF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1032-1191 2.17e-53

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: 184.42  E-value: 2.17e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGN- 1110
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1111 TKTGKAIKHVRDTLFTSdSGTRRGIPKVIVVITDGRSQD--DVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSR 1188
Cdd:cd01450     80 TNTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                   ...
gi 1572616313 1189 HVF 1191
Cdd:cd01450    159 HVF 161
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1230-1425 3.10e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.87  E-value: 3.10e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1230 GFKMMEMFGLVEKDFSAVEGVSMEPGtfnlFPCYQIHKDALVSQPTKYLHPEGLPSDYTMSFLFRIlpdTPQEPFALWEI 1309
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1310 LNKNSEPLVGIILDNGGKTLTYFNYDYTGDFQTVTFEGpdiRKMFYGSFHKLHVVVSKTLAKVVVDCKEVGQKAINASA- 1388
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1572616313  1389 -NITSDGVEVLGRMVRSRGPngnsAPFQLQMFDIVCST 1425
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 158-321 2.98e-51

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: 178.29  E-value: 2.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL 237
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 -TGLALNFIFENSFKPEAGSR--SGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDstH 314
Cdd:cd01481     81 nTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                   ....*..
gi 1572616313  315 VYNVAEF 321
Cdd:cd01481    159 VFQVSDF 165
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 158-336 1.79e-50

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: 178.35  E-value: 1.79e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTL 237
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  238 TGLALNFIFENSFKPEAGSRSG---VSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADLSELQEIASEPDSTH 314
Cdd:cd01475     83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                          170       180
                   ....*....|....*....|..
gi 1572616313  315 VYNVAEFDLMHTVVESLTRTVC 336
Cdd:cd01475    163 VFYVEDFSTIEELTKKFQGKIC 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1033-1199 2.60e-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: 2.60e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1033 DLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYK-GGNT 1111
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  1112 KTGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQD---DVNKISREMQADGFNIFAIGV-ADADYSELVQIGSKPSS 1187
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|..
gi 1572616313  1188 RHVFFVDDFDAF 1199
Cdd:smart00327  160 VYVFLPELLDLL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 159-324 4.14e-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: 175.72  E-value: 4.14e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   159 DIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYK-GGNTL 237
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   238 TGLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQD---DIIPPSRNLRESGVELFAIGVKNA-DLSELQEIASEPDST 313
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1572616313   314 HVYNVAEFDLM 324
Cdd:smart00327  161 YVFLPELLDLL 171
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1032-1215 1.55e-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: 172.95  E-value: 1.55e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNT 1111
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLD-VGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1112 KTGKAIKHVRDTLFTSDSGTRRG---IPKVIVVITDGRSQDDVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSSR 1188
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....*..
gi 1572616313 1189 HVFFVDDFDAFKKIEDELITFVCETAS 1215
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICVVPD 188
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1032-1196 4.13e-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: 157.87  E-value: 4.13e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNT 1111
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLD-VGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1112 -KTGKAIKHVRDTLFTSDSGTR--RGIPKVIVVITDGRSQDDVNKISREMQADGFNIFAIGVADADYSELVQIGSKPSsr 1188
Cdd:cd01481     80 lNTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS-- 157


                   ....*...
gi 1572616313 1189 HVFFVDDF 1196
Cdd:cd01481    158 FVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1033-1202 3.24e-43

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: 155.98  E-value: 3.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1033 DLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGNTK 1112
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLD-IGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1113 TGKAIKHVRDTLFTSDSGTRRGIPKVIVVITDGRSQDDVNKISREMQADGFNI--FAIGVADA-----DYSELVQIGSKP 1185
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIirYAIGVGGHfqrenSREELKTIASKP 160

                          170
                   ....*....|....*..
gi 1572616313 1186 SSRHVFFVDDFDAFKKI 1202
Cdd:cd01469    161 PEEHFFNVTDFAALKDI 177
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 159-322 6.86e-37

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: 137.87  E-value: 6.86e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  159 DIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGGNTLT 238
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  239 GLALNFIFENSFKPEAGSRSGVSKIGILITDGKSQDD-----IIPPSrnlRESGVELFAIGV-----KNADLSELQEIAS 308
Cdd:cd01469     82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDpllkdVIPQA---EREGIIRYAIGVgghfqRENSREELKTIAS 158

                          170
                   ....*....|....
gi 1572616313  309 EPDSTHVYNVAEFD 322
Cdd:cd01469    159 KPPEEHFFNVTDFA 172
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 158-316 8.29e-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: 8.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYK-GGNT 236
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  237 LTGLALNFIFENSFKPEagsRSGVSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGVKN-ADLSELQEIASEPDS 312
Cdd:cd00198     81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                   ....
gi 1572616313  313 THVY 316
Cdd:cd00198    158 GAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1032-1191 1.27e-29

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 116.51  E-value: 1.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYK-GGN 1110
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLS-ASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1111 TKTGKAIKHVRDTLFtsdSGTRRGIPKVIVVITDGRSQDD---VNKISREMQADGFNIFAIGV-ADADYSELVQIGSKPS 1186
Cdd:cd00198     80 TNIGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTT 156


                   ....*
gi 1572616313 1187 SRHVF 1191
Cdd:cd00198    157 GGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1032-1192 3.60e-27

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: 109.41  E-value: 3.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIgDDNFNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRT--EFKLDSYKTKETLLDAIRHISYKGG 1109
Cdd:cd01476      1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLE-IGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1110 NTKTGKAIKhVRDTLFTSDSGTRRGIPKVIVVITDGRSQDDVNKISREMQAD-GFNIFAIGVAD---ADYSELVQIGSKP 1185
Cdd:cd01476     79 TTATGAAIE-VALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNE 157


                   ....*..
gi 1572616313 1186 ssRHVFF 1192
Cdd:cd01476    158 --DHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 158-313 1.97e-24

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: 101.32  E-value: 1.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIgRFNFRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPR--IEWHLNAFNTKDEVIDAVRSLPYKGGN 235
Cdd:cd01476      1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  236 TLTGLALNFIFeNSFKPEAGSRSGVSKIGILITDGKSQDDIIPPSRNLRES-GVELFAIGVK---NADLSELQEIASEPD 311
Cdd:cd01476     80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGNED 158


                   ..
gi 1572616313  312 ST 313
Cdd:cd01476    159 HI 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 159-295 1.21e-20

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: 91.29  E-value: 1.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  159 DIVILVDGSWSIGRFN-FRLVRNFLENLVTAFNVGSEKTRIGLAQYSGDPRIEWHLNAFNTKDE-----VIDAVRSLPYK 232
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYYP 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572616313  233 GGNTLTGLALNFIFENSFKPeAGSRSGVSKIGILITDGKSQDD--IIPPSRNLRESGVELFAIGV 295
Cdd:cd01471     82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGV 145
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
372-769 7.89e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 89.68  E-value: 7.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  372 VNWTQSPGKVEKYRVVYYPTRGGKPEEVVVDGSVSSTVLK-----NLMSSTEYQIAVFAVSAHTASEGLRGAETTLA--L 444
Cdd:COG3401    153 ANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLvdgggDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPttP 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  445 PMA-SDLELYDVTENSMRVRWDAVP--GATGYLILYAPlteglAGDEKEMKIGETH----TDielSGLFPNTEYTVTVYA 517
Cdd:COG3401    233 PSApTGLTATADTPGSVTLSWDPVTesDATGYRVYRSN-----SGDGPFTKVATVTttsyTD---TGLTNGTTYYYRVTA 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  518 M--FGEE--ASDPATGQETTLPLTPPRNLRISNVGSNSARLTWDPASGK-ISGYRIVYTSADGTEINEV-EVDPITTFPL 591
Cdd:COG3401    305 VdaAGNEsaPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIaETVTTTSYTD 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  592 KGLTPLTEYSIAIFSIYEEGQSLPLVGEFTTEEVPAQQ----YLEIDEVKTDSFRVTWHPLSAEEGQHKLMWIPVYGGKT 667
Cdd:COG3401    385 TGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASgeslTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  668 QEVDLKEEQDSYVIEGLDPGTEYEVSLLAVLDDGSESEVVTAVGTTLDDFWTEAPTAIEPTSPVTSVLQTGIRNLVVDDE 747
Cdd:COG3401    465 GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544

                          410       420
                   ....*....|....*....|..
gi 1572616313  748 TATSLRVSWDISDSNVEQFRVT 769
Cdd:COG3401    545 VLITDLVSLTTSASSSVSGAGL 566
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1033-1170 5.63e-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: 80.89  E-value: 5.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1033 DLVFMVDGSWSIGDDN-FNKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKLDSYKT--KETLLDAIRH---ISY 1106
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLN-ISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRAllsLYY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1572616313 1107 KGGNTKTGKAIKHVRDTLFTSdSGTRRGIPKVIVVITDGRSQDDVN--KISREMQADGFNIFAIGV 1170
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 ...
 1032-1195 5.26e-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: 77.81  E-value: 5.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDNFN-------KIINFLYSTvgALDKIGADGTQVAMVQFTDDPRTEF-KLDSYKTKETLLDAIRH 1103
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDitknfvkRVAERFLKD--YYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1104 ISYKGGNTKTGKAIKHVRDTLFTSDSGTRRgipKVIVVITDGRSQ---DDVNKIS-REMQADGFNIFAIGVADADYSELV 1179
Cdd:cd01480     81 LEYIGGGTFTDCALKYATEQLLEGSHQKEN---KFLLVITDGHSDgspDGGIEKAvNEADHLGIKIFFVAVGSQNEEPLS 157

                          170       180
                   ....*....|....*....|....*.
gi 1572616313 1180 QIGSKPSSRHV----------FFVDD 1195
Cdd:cd01480    158 RIACDGKSALYrenfaellwsFFIDD 183
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1032-1211 5.60e-16

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: 77.94  E-value: 5.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDdNFNKIINFLYSTVgalDKIGADGTQVAMVQFTDDPRTEFKLDSYKTKETL-LDAIRHISyKGGN 1110
Cdd:cd01474      5 FDLYFVLDKSGSVAA-NWIEIYDFVEQLV---DRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVT-PSGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1111 TKTGKAIKHVRDTLFTSDSGTRRgIPKVIVVITDGRSQDDV-------NKISREMqadGFNIFAIGVADADYSELVQIGS 1183
Cdd:cd01474     80 TYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNGhkypeheAKLSRKL---GAIVYCVGVTDFLKSQLINIAD 155

                          170       180
                   ....*....|....*....|....*....
gi 1572616313 1184 kpSSRHVFFVDD-FDAFKKIEDELITFVC 1211
Cdd:cd01474    156 --SKEYVFPVTSgFQALSGIIESVVKKAC 182
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 538-622 8.88e-16

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 74.46  E-value: 8.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  538 PPRNLRISNVGSNSARLTWDPAS---GKISGYRIVYTSADGTEINEVEVDPI--TTFPLKGLTPLTEYSIAIFSIYEEGQ 612
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNGGGE 82

                           90
                   ....*....|.
gi 1572616313  613 SLPL-VGEFTT 622
Cdd:cd00063     83 SPPSeSVTVTT 93
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 158-320 7.56e-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: 74.73  E-value: 7.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFNFRLVRNF----LENLVTAFNV--GSEKTRIGLAQYSGDPRIEWHLNAF-NTKDEVIDAVRSLP 230
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFvkrvAERFLKDYYRkdPAGSWRVGVVQYSDQQEVEAGFLRDiRNYTSLKEAVDNLE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  231 YKGGNTLTGLALNFIFENSFKpeaGSRSGVSKIGILITDGKSQ---DDIIPPSRNLRES-GVELFAIGVkNADLSE-LQE 305
Cdd:cd01480     83 YIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgspDGGIEKAVNEADHlGIKIFFVAV-GSQNEEpLSR 158

                          170
                   ....*....|....*.
gi 1572616313  306 IASEPDSTHV-YNVAE 320
Cdd:cd01480    159 IACDGKSALYrENFAE 174
fn3 pfam00041
Fibronectin type III domain;
538-615 1.32e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 1.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  538 PPRNLRISNVGSNSARLTWDPA---SGKISGYRIVYTSADGTEI-NEVEVDP-ITTFPLKGLTPLTEYSIAIFSIYEEGQ 612
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPwNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1572616313  613 SLP 615
Cdd:pfam00041   82 GPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 538-613 1.82e-13

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 67.25  E-value: 1.82e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   538 PPRNLRISNVGSNSARLTWDPAS-----GKISGYRIVYTSADGTEINEVEVDPITTFPLKGLTPLTEYSIAIFSIYEEGQ 612
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1572616313   613 S 613
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
355-433 1.32e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  355 GPPTELITSEVTARSFMVNWTQSP---GKVEKYRVVYYPTRGGKPE-EVVVDGSVSSTVLKNLMSSTEYQIAVFAVSAHT 430
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1572616313  431 ASE 433
Cdd:pfam00041   81 EGP 83
fn3 pfam00041
Fibronectin type III domain;
833-902 4.64e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 4.64e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1572616313  833 PQNLRVSEEWYNRVRITWDPP---SGPVKGYRIVYKPVSVPGQTLETFVGADINTIVMTNLLSGMDYNVKIFA 902
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
VWA_2 pfam13519
von Willebrand factor type A domain;
1034-1142 4.68e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 63.85  E-value: 4.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1034 LVFMVDGSWSIGDD-----NFNKIINFLYSTVGALDkigadGTQVAMVQFTDDPRTEFKLDsyKTKETLLDAIRHISYKG 1108
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLP-----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1572616313 1109 GNTKTGKAIKHVRDTLFTsdsgTRRGIPKVIVVI 1142
Cdd:pfam13519   74 GGTNLAAALQLARAALKH----RRKNQPRRIVLI 103
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 831-913 2.17e-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: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  831 SGPQNLRVSEEWYNRVRITWDPPS---GPVKGYRIVYKPVSVPGQTLETFVGADINTIVMTNLLSGMDYNVKIFASQASG 907
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ....*.
gi 1572616313  908 FSDALT 913
Cdd:cd00063     82 ESPPSE 87
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 158-309 3.02e-11

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: 65.73  E-value: 3.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  158 ADIVILVDGSWSIGRFN-FRLVRNFLENLVTAFnvgSEKTRIGLAQYSGdpRIEWHLNAFNTKDEVIDAVRSLPYKGGNT 236
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGGTP 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  237 LT---GLALNFIfensfkpeAGSRSGVSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGV--KNADLSELQEIAS 308
Cdd:COG1240    168 LGdalALALELL--------KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVgtEAVDEGLLREIAE 239


                   .
gi 1572616313  309 E 309
Cdd:COG1240    240 A 240
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 3.33e-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: 67.62  E-value: 3.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1479 QQGEQGPKGPEGPRGETGPagpqgppgpqgpsglsiQGMPGMPGDKGDKGDAGLPGPQGVPGGVGSPGRDGSPGQRGFPG 1558
Cdd:NF038329   166 PQGEAGPQGPAGKDGEAGA-----------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1559 KDGSSGPPGPPGpigipgapgvPGITGSMGPQGALGPPGVPGAKGERGERG 1609
Cdd:NF038329   229 PAGDGQQGPDGD----------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 6.77e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 6.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVAPASGGKTNQMNLQN-TATKAIIQGLLPEQNYTVQLIAYYKDKE 107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ....*
gi 1572616313  108 SKPAQ 112
Cdd:cd00063     83 SPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 355-433 7.61e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.20  E-value: 7.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  355 GPPTELITSEVTARSFMVNWTQSP---GKVEKYRVVYYPTRGGKPEEV-VVDGSVSSTVLKNLMSSTEYQIAVFAVSAHT 430
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1572616313  431 ASE 433
Cdd:cd00063     82 ESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 740-818 1.84e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.78  E-value: 1.84e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572616313   740 RNLVVDDETATSLRVSWDISDSNVEQFRVTYLKAQGDPMEEVVGTVMVPGVQNSLLLKALLPDTEYKVTVTPVYTVGEG 818
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
740-818 2.17e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 2.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  740 RNLVVDDETATSLRVSWDIS---DSNVEQFRVTYLKAQGdpmEEVVGTVMVPGVQNSLLLKALLPDTEYKVTVTPVYTVG 816
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNS---GEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1572616313  817 EG 818
Cdd:pfam00041   81 EG 82
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1032-1202 2.89e-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: 63.03  E-value: 2.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1032 ADLVFMVDGSWSIGDDN-FNKIINFLYSTVGALDKigadGTQVAMVQFTDDPRTEFKLDSykTKETLLDAIRHISYKGGn 1110
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPGGG- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1111 TKTGKAIKHVRDTLFTSDSGTRrgipKVIVVITDGR---SQDDVNKISREMQADGFNIFAIGVADADYSE--LVQIgSKP 1185
Cdd:COG1240    166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREI-AEA 240

                          170
                   ....*....|....*..
gi 1572616313 1186 SSRHVFFVDDFDAFKKI 1202
Cdd:COG1240    241 TGGRYFRADDLSELAAI 257
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 448-517 3.83e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.01  E-value: 3.83e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1572616313   448 SDLELYDVTENSMRVRWDAV--PGATGYLILYAPLTEGLAGDEKEMKIGETHTDIELSGLFPNTEYTVTVYA 517
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
32-110 5.81e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 5.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   32 PPTRLRYNVISHDSIQISWKAPR---GKFGGYKLLVAPA-SGGKTNQMNLQNTATKAIIQGLLPEQNYTVQLIAYYKDKE 107
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1572616313  108 SKP 110
Cdd:pfam00041   82 GPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
356-608 8.31e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.87  E-value: 8.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  356 PPTELITSEVTARSFMVNWTQSPGK-VEKYRVvYYPTRGGKPEEVVVDGSVSSTVLKNLMSSTEYQIAVFAVSAH----T 430
Cdd:COG3401    235 APTGLTATADTPGSVTLSWDPVTESdATGYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAgnesA 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  431 ASEGLRGAETTLALPMASDLELYDVTENSMRVRWDAVPG--ATGYLILYAPLTEGLAGdekemKIGETHTDIEL--SGLF 506
Cdd:COG3401    314 PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVYRSTSGGGTYT-----KIAETVTTTSYtdTGLT 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  507 PNTEYTVTVYAM----FGEEASDPATGQETTLP----LTPPRNLRISNVGSNSARLTWDPASGKISGYrIVYTSADGTEI 578
Cdd:COG3401    389 PGTTYYYKVTAVdaagNESAPSEEVSATTASAAsgesLTASVDAVPLTDVAGATAAASAASNPGVSAA-VLADGGDTGNA 467

                          250       260       270
                   ....*....|....*....|....*....|
gi 1572616313  579 NEVEVDPITTFPLKGLTPLTEYSIAIFSIY 608
Cdd:COG3401    468 VPFTTTSSTVTATTTDTTTANLSVTTGSLV 497
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 740-827 1.11e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.12  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  740 RNLVVDDETATSLRVSWD---ISDSNVEQFRVTYLKAQGDPMEEVVGTvmvPGVQNSLLLKALLPDTEYKVTVTPVYTVG 816
Cdd:cd00063      5 TNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYREKGSGDWKEVEVT---PGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1572616313  817 EGV-SVSAPGKT 827
Cdd:cd00063     82 ESPpSESVTVTT 93
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 157-336 2.57e-09

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: 58.68  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  157 IADIVILVDGSWSIGRfNFRLVRNFLENLVTAFNvgSEKTRIGLAQYSGDPRIEWHLNAFNTKD----EVIDAVrsLPyk 232
Cdd:cd01474      4 HFDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAIikglEVLKKV--TP-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  233 GGNTLTGLALNFIFENSFKPEAGSRSgVSKIGILITDGKSQDDiiPPSRNLRES------GVELFAIGVKNADLSELQEI 306
Cdd:cd01474     77 SGQTYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLN--GHKYPEHEAklsrklGAIVYCVGVTDFLKSQLINI 153

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1572616313  307 ASEPDstHVYNVAE-FDLMHTVVESLTRTVC 336
Cdd:cd01474    154 ADSKE--YVFPVTSgFQALSGIIESVVKKAC 182
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 448-533 3.16e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.58  E-value: 3.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  448 SDLELYDVTENSMRVRWDAVPGA----TGYLILYAPLTEGlaGDEKEMKIGETHTDIELSGLFPNTEYTVTVYAMFGEEA 523
Cdd:cd00063      5 TNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSG--DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82

                           90
                   ....*....|
gi 1572616313  524 SDPATGQETT 533
Cdd:cd00063     83 SPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
448-517 6.74e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 6.74e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1572616313  448 SDLELYDVTENSMRVRWDAVPGA----TGYLILYAPLTEGlaGDEKEMKIGETHTDIELSGLFPNTEYTVTVYA 517
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPDGngpiTGYEVEYRPKNSG--EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 159-336 1.80e-08

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: 56.17  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  159 DIVILVDGSWSIGRFNFRL-VRNFLENLVTAFNVGSEKTRIGLAQYSGDPR--IEWHLNAFNTKDEVIDAVRSLP--YK- 232
Cdd:cd01473      2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLKnsYRs 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  233 GGNTLTGLALNFIFENSFKPEaGSRSGVSKIGILITDG----KSQDDIIPPSRNLRESGVELFAIGVKNADLSELQEIA- 307
Cdd:cd01473     82 GGETYIVEALKYGLKNYTKHG-NRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAg 160

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1572616313  308 -SEPDSTHVYNV-AEFDLMHTVVESLTRTVC 336
Cdd:cd01473    161 cDINNDNCPNVIkTEWNNLNGISKFLTDKIC 191
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
447-770 1.88e-08

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 59.57  E-value: 1.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  447 ASDLELYDVTENS----MRVRWDAVPGATGYLILYapltegLAGDEKEMKIGETH-TDIELSGLFPNTeYTVTVYAM-FG 520
Cdd:COG4733    537 TTSESLSVVAQGTavttLTVSWDAPAGAVAYEVEW------RRDDGNWVSVPRTSgTSFEVPGIYAGD-YEVRVRAInAL 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  521 EEASDPATGQETTL-----PLTPPRNLRISNvGSNSARLTWDPASG-KISGYRIVYTSADGTEINEVEVD--PITTFPLK 592
Cdd:COG4733    610 GVSSAWAASSETTVtgktaPPPAPTGLTATG-GLGGITLSWSFPVDaDTLRTEIRYSTTGDWASATVAQAlyPGNTYTLA 688

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  593 GLTPLTEYSIAIFSIYEEGQSLPLVGEFTTEEVPAQQYLEIDEVKTDS------FRVTWHPLSAEEGQHKLMWIPVYGGK 666
Cdd:COG4733    689 GLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAGILDAITGQILETelgqelDAIIQNATVAEVVAATVTDVTAQIDT 768

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  667 TQEVDLKEEQDsyVIEGLDPGTEYEVSLLAVLDDGSESEVVtAVGTTLDDFWTEAPTAIEPTSPVTSVLQTGIRNLVVDD 746
Cdd:COG4733    769 AVLFAGVATAA--AIGAEARVAATVAESATAAAATGTAADA-AGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVV 845

                          330       340
                   ....*....|....*....|....
gi 1572616313  747 ETATSLRVSWDISDSNVEQFRVTY 770
Cdd:COG4733    846 VYGDAIIESGNTGDIVATGDIASA 869
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 831-909 2.31e-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: 2.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   831 SGPQNLRVSEEWYNRVRITWDPPS-----GPVKGYRIVYKPVSVPGQTLEtfVGADINTIVMTNLLSGMDYNVKIFASQA 905
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVN--VTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1572616313   906 SGFS 909
Cdd:smart00060   80 AGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 631-708 2.78e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 52.88  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  631 LEIDEVKTDSFRVTWHPLSAEEGQH---KLMWIPVYGGKTQEVDLKEEQD-SYVIEGLDPGTEYEVSLLAVLDDG----S 702
Cdd:cd00063      7 LRVTDVTSTSVTLSWTPPEDDGGPItgyVVEYREKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGGesppS 86


                   ....*.
gi 1572616313  703 ESEVVT 708
Cdd:cd00063     87 ESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 355-432 2.81e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.62  E-value: 2.81e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313   355 GPPTELITSEVTARSFMVNWTQSPGKVEKYRVVYY----PTRGGKPEEVVVDGSVSSTVLKNLMSSTEYQIAVFAVSAHT 430
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYrveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1572616313   431 AS 432
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 631-702 2.90e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.62  E-value: 2.90e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1572616313   631 LEIDEVKTDSFRVTW-HPLSAEEGQHKLMWIPVY---GGKTQEVDLKEEQDSYVIEGLDPGTEYEVSLLAVLDDGS 702
Cdd:smart00060    7 LRVTDVTSTSVTLSWePPPDDGITGYIVGYRVEYreeGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1033-1181 3.72e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 56.61  E-value: 3.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1033 DLVFMVDGSWSIGDDNFNKIINFLYSTVGALdkigADGTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHISYKGGnTK 1112
Cdd:COG2425    120 PVVLCVDTSGSMAGSKEAAAKAAALALLRAL----RPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TD 194

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1113 TGKAIKHVRDtLFTSDSGTRRgipkVIVVITDGRSQDDVNKISREMQAD--GFNIFAIGVADADYSELVQI 1181
Cdd:COG2425    195 IAPALRAALE-LLEEPDYRNA----DIVLITDGEAGVSPEELLREVRAKesGVRLFTVAIGDAGNPGLLEA 260
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 159-329 5.84e-08

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: 54.99  E-value: 5.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  159 DIVILVDGSWSIGRFNFRLVRNFLENLVT---AFNVgseKTRIGLAQYSGDPRIEWHLNAFNT--KDEVIDAVRSLPYK- 232
Cdd:cd01470      2 NIYIALDASDSIGEEDFDEAKNAIKTLIEkisSYEV---SPRYEIISYASDPKEIVSIRDFNSndADDVIKRLEDFNYDd 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  233 ---GGNTLTGLALNFIFENSFKPEAGSRSGVSKIG---ILITDGKSQ---------DDII------PPSRNLRESGVELF 291
Cdd:cd01470     79 hgdKTGTNTAAALKKVYERMALEKVRNKEAFNETRhviILFTDGKSNmggsplptvDKIKnlvyknNKSDNPREDYLDVY 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1572616313  292 AIGV-KNADLSELQEIASE-PDSTHVYNVAEFDLMHTVVE 329
Cdd:cd01470    159 VFGVgDDVNKEELNDLASKkDNERHFFKLKDYEDLQEVFD 198
fn3 pfam00041
Fibronectin type III domain;
626-701 1.12e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  626 PAQQYLEIDEVKTDSFRVTWHPLSAEEGQ---HKLMWIPVYGGK-TQEVDLKEEQDSYVIEGLDPGTEYEVSLLAVLDDG 701
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPitgYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 1.81e-07

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: 55.68  E-value: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1479 QQGEQGPKGPEGPRGEtgpagpqgppgpqgpsglsiQGMPGMPGDKGDKGDAglpgpqgvpggvgspgrdGSPGQRGFPG 1558
Cdd:NF038329   118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPA------------------GPPGPQGERG 159

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1559 KDGSSGPPGPpgpigipgapgvPGITGSMGPQGALGPPGVPGAKGERGERG 1609
Cdd:NF038329   160 EKGPAGPQGE------------AGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
679-918 2.46e-07

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 56.11  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  679 YVIEGLDPGTEYEVSLLAVLDDGSESEVVTAvgttlddfwtEAPTAIEPTSPVTSVLQTGIRNLVVDDETATSLRVSWDI 758
Cdd:COG4733    491 FRVVSIEENEDGTYTITAVQHAPEKYAAIDA----------GAFDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDA 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  759 SDSNVEqFRVTYLKAQGDpmeevvgTVMVPGVQNSLLLKALLPDTEYKVTVTPVYTVG------EGVSVSAPGKTLPSSG 832
Cdd:COG4733    561 PAGAVA-YEVEWRRDDGN-------WVSVPRTSGTSFEVPGIYAGDYEVRVRAINALGvssawaASSETTVTGKTAPPPA 632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  833 PQNLRVSEEwYNRVRITWDPPSGP-VKGYRIVYKPVSVPGQTLETFVGADINTIVMTNLLSGMDYNVKIFASQASGFSDA 911
Cdd:COG4733    633 PTGLTATGG-LGGITLSWSFPVDAdTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVSA 711


                   ....*..
gi 1572616313  912 LTGLVQT 918
Cdd:COG4733    712 WWVSGQA 718
VWA_2 pfam13519
von Willebrand factor type A domain;
160-267 5.64e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.60  E-value: 5.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  160 IVILVDGSWSI-----GRFNFRLVRNFLENLVTAFNvgseKTRIGLAQYSGDPRIEWHLNAfnTKDEVIDAVRSLPYKGG 234
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1572616313  235 NTLTGLALNFIFENSFKPeagsRSGVSKIGILI 267
Cdd:pfam13519   75 GTNLAAALQLARAALKHR----RKNQPRRIVLI 103
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 32-108 6.94e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.76  E-value: 6.94e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313    32 PPTRLRYNVISHDSIQISWKAP-RGKFGGYKL---LVAPASGGKTNQMNLQNTATKAIIQGLLPEQNYTVQLIAYYKDKE 107
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1572616313   108 S 108
Cdd:smart00060   83 G 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
684-941 4.36e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.54  E-value: 4.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  684 LDPGTEYEVSLLAVLDDGSESEVVTAVGTTLDDFWTEAPTAIEPTSPVTSVLQTGIRNLVVDDETATSLRVSWDISDSNV 763
Cdd:COG3401     87 APPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGA 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  764 EQFRVTYLKAQGDPmeeVVGTVMVPGVQNSLLLKALLPDTEYKVTVTPVYTVGEG-----VSVSAPGkTLPSSgPQNLRV 838
Cdd:COG3401    167 GVVVSPDTSATAAV---ATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESapsneVSVTTPT-TPPSA-PTGLTA 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  839 SEEWYNRVRITWDPPSGP-VKGYRIVYKpvSVPGQTLETFVGADINTIVMTNLLSGMDYNVKIFASQA----SGFSDALT 913
Cdd:COG3401    242 TADTPGSVTLSWDPVTESdATGYRVYRS--NSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAagneSAPSNVVS 319

                          250       260
                   ....*....|....*....|....*....
gi 1572616313  914 GLVQTLFLGV-TDLQANQVEMTSLCARWQ 941
Cdd:COG3401    320 VTTDLTPPAApSGLTATAVGSSSITLSWT 348
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 4.46e-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: 51.44  E-value: 4.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1479 QQGEQGPKGPEGPRGETGPAGPQGPPGPQGPSGLSIQGMPGMPGDKGDKGDAGLpgpqgvpggvgspgrDGSPGQRGFPG 1558
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE---------------DGPQGPDGPAG 257

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1572616313 1559 KDGSSGPPGPpgpigipgapgvPGITGSMGPQGALGPPGVPGAKGERGERG 1609
Cdd:NF038329   258 KDGPRGDRGE------------AGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 155-309 7.25e-06

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 49.68  E-value: 7.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  155 PAIADIVILVDGSWSIGRFNFRLVRNFLENLVTAFNvgsEKTRIGLAQYSGDPRIEWHLNAFNTKDEVIDAVRSLPYKGG 234
Cdd:COG2425    116 LLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG 192

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1572616313  235 nTLTGLALNFIFEnSFKPEAGSRSGVskigILITDGKSQDDIIPPSRNLR--ESGVELFAIGVKNADLSELQEIASE 309
Cdd:COG2425    193 -TDIAPALRAALE-LLEEPDYRNADI----VLITDGEAGVSPEELLREVRakESGVRLFTVAIGDAGNPGLLEALAD 263
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1024-1197 1.98e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 49.58  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1024 KEVCKAaKADLVFMVDGSWSIGDDNF-NKIINFLYSTVGALDkIGADGTQVAMVQFTDDPRTEFKL--DSYKTKETLLDA 1100
Cdd:PTZ00441    36 EEVCNE-EVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLN-LSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALII 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1101 IRHISyKG----GNTKTGKAIKHVRDTLftSDSGTRRGIPKVIVVITDG--RSQDDVNKISREMQADGFNIFAIGVA--- 1171
Cdd:PTZ00441   114 VKSLR-KTylpyGKTNMTDALLEVRKHL--NDRVNRENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgi 190

                          170       180
                   ....*....|....*....|....*.
gi 1572616313 1172 DADYSELVqIGSKPSSRHVFFVDDFD 1197
Cdd:PTZ00441   191 NHQFNRLL-AGCRPREGKCKFYSDAD 215
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1035-1202 2.14e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 47.23  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1035 VFMVDGSWSIGDDNFNKI---INFLYSTVGAlDKIGADGTQVAMVQFTDDPRTEFKLdsyktkeTLLDAIR--HISYkGG 1109
Cdd:COG4245      9 YLLLDTSGSMSGEPIEALnegLQALIDELRQ-DPYALETVEVSVITFDGEAKVLLPL-------TDLEDFQppDLSA-SG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1110 NTKTGKAIKHVRDTLfTSDSGTRRGIPK-----VIVVITDGRSQDD-----VNKISREMQADGFNIFAIGV-ADADYSEL 1178
Cdd:COG4245     80 GTPLGAALELLLDLI-ERRVQKYTAEGKgdwrpVVFLITDGEPTDSdweaaLQRLKDGEAAKKANIFAIGVgPDADTEVL 158

                          170       180
                   ....*....|....*....|....
gi 1572616313 1179 VQIGskPSSRhVFFVDDFDAFKKI 1202
Cdd:COG4245    159 KQLT--DPVR-ALDALDGLDFREF 179
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1516-1605 5.65e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1516 GMPGMPGDKGDKGDAglpgpqgvpggvgspgrdGSPGQRGFPGKDGSSGPPgppgpigipgapgvpGITGSMGPQGALGP 1595
Cdd:pfam01391    1 GPPGPPGPPGPPGPP------------------GPPGPPGPPGPPGPPGEP---------------GPPGPPGPPGPPGP 47

                           90
                   ....*....|
gi 1572616313 1596 PGVPGAKGER 1605
Cdd:pfam01391   48 PGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1581-1610 2.92e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.92e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1572616313 1581 PGITGSMGPQGALGPPGVPGAKGERGERGD 1610
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1033-1184 3.21e-04

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: 43.57  E-value: 3.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1033 DLVFMVDGSWSIGDDNFNKIINFLYSTVGALDKIGAD-----GTQVAMVQFTDDPRTEFKLDSYKTKETLLDAIRHI--- 1104
Cdd:cd01477     21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprSTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSltd 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1105 --SYKGGNTKTGkaIKHVRDTLFTSDSGTRRGIPKVIVVIT---DGRSQDDVNKISREMQADGFNIfaIGVA---DADY- 1175
Cdd:cd01477    101 vsSTNASYLDTG--LQAAEQMLAAGKRTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAI--ITVAftqDESSn 176

                          170
                   ....*....|.
gi 1572616313 1176 --SELVQIGSK 1184
Cdd:cd01477    177 llDKLGKIASP 187
fn3 pfam00041
Fibronectin type III domain;
923-998 4.52e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.86  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  923 VTDLQANQVEMTSLCARWQI----HRHATAYRIVLESLQDTQA-QESTVGGGVNRHCFYGLQPDSEYKISVYTKLQELEG 997
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 1572616313  998 P 998
Cdd:pfam00041   83 P 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1481-1601 1.28e-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: 38.63  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1481 GEQGPKGPEGPRGEtgpagpqgppgpqgpsglsiQGMPGMPGDKGDKGDAglpgpqgvpggvgspgrdGSPGQRGFPGKD 1560
Cdd:pfam01391    1 GPPGPPGPPGPPGP--------------------PGPPGPPGPPGPPGPP------------------GEPGPPGPPGPP 42

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1572616313 1561 gssgppgppgpigipgapgvpgitgsmGPQGALGPPGVPGA 1601
Cdd:pfam01391   43 ---------------------------GPPGPPGAPGAPGP 56
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
537-604 4.88e-03

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 41.30  E-value: 4.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313  537 TPPRNLRISNVGSNSARLTWDPASG--KISGYRiVYTsaDGTEINevEVDPITTFPLKGLTPLTEYSIAI 604
Cdd:COG3979      4 TAPTGLTASNVTSSSVSLSWDASTDnvGVTGYD-VYR--GGDQVA--TVTGLTAWTVTGLTPGTEYTFTV 68
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1033-1182 5.69e-03

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: 39.99  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1033 DLVFMVDGSWSIGDDNFNK-IINFLYSTVGALdKIGADGTQVAMVQFTDDPRTEFKLD---SYKtKETLLDAIRHI--SY 1106
Cdd:cd01473      2 DLTLILDESASIGYSNWRKdVIPFTEKIINNL-NISKDKVHVGILLFAEKNRDVVPFSdeeRYD-KNELLKKINDLknSY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616313 1107 K-GGNTKTGKAIKHVRDTlFTSDSGTRRGIPKVIVVITDG----RSQDDVNKISREMQADGFNIFAIGVADADYSELVQI 1181
Cdd:cd01473     80 RsGGETYIVEALKYGLKN-YTKHGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLL 158


                   .
gi 1572616313 1182 G 1182
Cdd:cd01473    159 A 159
 
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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