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Conserved domains on  [gi|93141049|ref|NP_542376|]
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collagen alpha-1(XII) chain short isoform precursor [Homo sapiens]

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 ...
 34-197 8.50e-93

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: 297.28  E-value: 8.50e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 113
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 193
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                 ....
gi 93141049  194 VADF 197
Cdd:cd01482  161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1158-1322 4.34e-84

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


:

Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 272.24  E-value: 4.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFdEISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 1237
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAF-EIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 1317
Cdd:cd01482   80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                 ....*
gi 93141049 1318 IVDDF 1322
Cdd:cd01482  160 NVADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1356-1548 3.16e-59

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 202.20  E-value: 3.16e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1356 GFKMLEAYNLTEKNFASVQGVSLEsgsfPSYSAYRIQKNAFVNQPTADLHPNGLPPSYTIILLFRLlpeTPSDPFAIWQI 1435
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPE----PGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1436 TDRDYKPQVGVIADPSSKTLSFFNKDTRGEVQTVTFdteEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAG- 1514
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 93141049    1515 -NITTDGYEILGKLLKGeRKSAAFQIQSFDIVCSP 1548
Cdd:smart00210  151 pPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
fn3 pfam00041
Fibronectin type III domain;
592-670 1.42e-15

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.60  E-value: 1.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    592 PRNLQVYNATSNSLTVKWDPA---SGRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDGEG 668
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 93141049    669 GR 670
Cdd:pfam00041   83 PP 84
fn3 pfam00041
Fibronectin type III domain;
223-301 1.83e-15

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    223 APSNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKR-QEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEY 298
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGngpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 93141049    299 SEP 301
Cdd:pfam00041   82 GPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 954-1033 1.10e-14

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 71.37  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  954 PPQNIHISDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEA--FVGEMTSYTLHNLNPSTTYDVNVYAQYDSGL 1028
Cdd:cd00063    3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                 ....*
gi 93141049 1029 SVPLT 1033
Cdd:cd00063   83 SPPSE 87
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
255-822 1.14e-14

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 79.66  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  255 YYPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEYSEPLKGTEKTLPVPVVSLNIYDVGPTTMHVQWQPVG 334
Cdd:COG3401    5 YLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  335 GATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVqavlhdltsepVTVREVTLPLPRPQDLKLRDVT 414
Cdd:COG3401   85 AAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAV-----------AGGAATAGTYALGAGLYGVDGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  415 HSTMNVFWEPVPGKVRKYIVRYKTPEEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEGESPP---VTAQETTRPV 491
Cdd:COG3401  154 NASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPsneVSVTTPTTPP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  492 PAPTNLKITEVTSEGFRGTWD-HGASDVSLYRITWAPfGSSDKMETILNGDENTLVFENLNPNTIYEVSITAIYPDESES 570
Cdd:COG3401  234 SAPTGLTATADTPGSVTLSWDpVTESDATGYRVYRSN-SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNES 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  571 DDligSErTLPILTTQAPKSGPRNLQVYNATSNSLTVKWDPASG-RVQKYRItYQPSTGEGNEQTTTIGGRQNSVVLQKL 649
Cdd:COG3401  313 AP---SN-VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGL 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  650 KPDTPYTITVSSLYPDGEGGRMTGRGKTKPLNTVRNLRVYDPSTSTLNVRWDHAEGNPRQYKLFYAPAAGGPEELVPIPG 729
Cdd:COG3401  388 TPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA 467

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  730 NTNYAILRNLQPDTSYTVTVVPVYTEGDGGRTSDTGR-----TLMRGLARNVQVYNPTPNSLDVRWDPAPGPVLQYRVVY 804
Cdd:COG3401  468 VPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSvtnsvSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLI 547

                        570
                 ....*....|....*...
gi 93141049  805 SPVDGTRPSESIVVPGNT 822
Cdd:COG3401  548 TDLVSLTTSASSSVSGAG 565
fn3 pfam00041
Fibronectin type III domain;
864-941 3.07e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 3.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    864 PRNLRVFGETTNSLSVAW---DHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDGDG 940
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 93141049    941 G 941
Cdd:pfam00041   83 P 83
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1600-1733 2.02e-08

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: 58.76  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1600 RGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLSIP-GEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRG 1678
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPaGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 93141049  1679 FTGKDGamgprgpPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRGD 1733
Cdd:NF038329  217 EAGPAG-------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
fn3 pfam00041
Fibronectin type III domain;
1043-1118 8.22e-07

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 8.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1043 VTDLKTYQIGWDTFCVKWSP----HRAATSYRLKLSPADGTRG-QEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLEG 1117
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 93141049   1118 P 1118
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 ...
 34-197 8.50e-93

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: 297.28  E-value: 8.50e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 113
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 193
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                 ....
gi 93141049  194 VADF 197
Cdd:cd01482  161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1158-1322 4.34e-84

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 272.24  E-value: 4.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFdEISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 1237
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAF-EIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 1317
Cdd:cd01482   80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                 ....*
gi 93141049 1318 IVDDF 1322
Cdd:cd01482  160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
35-206 1.42e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 222.54  E-value: 1.42e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     35 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL- 113
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQD-DVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAY 192
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 93141049    193 NVADFESLSRIVDD 206
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1159-1331 8.69e-62

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.05  E-value: 8.69e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1159 DIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTR 1238
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1239 -TGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD-EVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHV 1316
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 93141049   1317 FIVDDFESFEKIEDN 1331
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1356-1548 3.16e-59

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 202.20  E-value: 3.16e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1356 GFKMLEAYNLTEKNFASVQGVSLEsgsfPSYSAYRIQKNAFVNQPTADLHPNGLPPSYTIILLFRLlpeTPSDPFAIWQI 1435
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPE----PGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1436 TDRDYKPQVGVIADPSSKTLSFFNKDTRGEVQTVTFdteEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAG- 1514
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 93141049    1515 -NITTDGYEILGKLLKGeRKSAAFQIQSFDIVCSP 1548
Cdd:smart00210  151 pPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 35-204 1.74e-49

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: 173.79  E-value: 1.74e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049      35 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYK-GGNTL 113
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQD---DVEAPSKKLKDEGVELFAIGIKNA-DEVELKMIATDPDDT 189
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 93141049     190 HAYNVADFESLSRIV 204
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1159-1328 1.86e-45

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: 162.24  E-value: 1.86e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1159 DIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYR-GGNT 1237
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1238 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD---EVKKAALVIQQSGFSVFVVGV-ADVDYNELANIASKPSE 1313
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 93141049    1314 RHVFIVDDFESFEKI 1328
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
fn3 pfam00041
Fibronectin type III domain;
592-670 1.42e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.60  E-value: 1.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    592 PRNLQVYNATSNSLTVKWDPA---SGRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDGEG 668
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 93141049    669 GR 670
Cdd:pfam00041   83 PP 84
fn3 pfam00041
Fibronectin type III domain;
223-301 1.83e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    223 APSNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKR-QEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEY 298
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGngpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 93141049    299 SEP 301
Cdd:pfam00041   82 GPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 954-1033 1.10e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 71.37  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  954 PPQNIHISDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEA--FVGEMTSYTLHNLNPSTTYDVNVYAQYDSGL 1028
Cdd:cd00063    3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                 ....*
gi 93141049 1029 SVPLT 1033
Cdd:cd00063   83 SPPSE 87
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
255-822 1.14e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 79.66  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  255 YYPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEYSEPLKGTEKTLPVPVVSLNIYDVGPTTMHVQWQPVG 334
Cdd:COG3401    5 YLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  335 GATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVqavlhdltsepVTVREVTLPLPRPQDLKLRDVT 414
Cdd:COG3401   85 AAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAV-----------AGGAATAGTYALGAGLYGVDGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  415 HSTMNVFWEPVPGKVRKYIVRYKTPEEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEGESPP---VTAQETTRPV 491
Cdd:COG3401  154 NASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPsneVSVTTPTTPP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  492 PAPTNLKITEVTSEGFRGTWD-HGASDVSLYRITWAPfGSSDKMETILNGDENTLVFENLNPNTIYEVSITAIYPDESES 570
Cdd:COG3401  234 SAPTGLTATADTPGSVTLSWDpVTESDATGYRVYRSN-SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNES 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  571 DDligSErTLPILTTQAPKSGPRNLQVYNATSNSLTVKWDPASG-RVQKYRItYQPSTGEGNEQTTTIGGRQNSVVLQKL 649
Cdd:COG3401  313 AP---SN-VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGL 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  650 KPDTPYTITVSSLYPDGEGGRMTGRGKTKPLNTVRNLRVYDPSTSTLNVRWDHAEGNPRQYKLFYAPAAGGPEELVPIPG 729
Cdd:COG3401  388 TPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA 467

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  730 NTNYAILRNLQPDTSYTVTVVPVYTEGDGGRTSDTGR-----TLMRGLARNVQVYNPTPNSLDVRWDPAPGPVLQYRVVY 804
Cdd:COG3401  468 VPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSvtnsvSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLI 547

                        570
                 ....*....|....*...
gi 93141049  805 SPVDGTRPSESIVVPGNT 822
Cdd:COG3401  548 TDLVSLTTSASSSVSGAG 565
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 31-207 5.99e-14

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: 73.82  E-value: 5.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   31 RAEADIVLLVDGSWSIGRAN-FRTVRSFISRIVEVFdigPKRVQIALAQYSGDPrtEWQLNAHRDKKSLLQAVANLPYKG 109
Cdd:COG1240   90 QRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  110 GNTLT---GMALNFIRQQNfrtqagmrPRARKIGVLITDGK---SQDDVEAPSKKLKDEGVELFAIGI--KNADEVELKM 181
Cdd:COG1240  165 GTPLGdalALALELLKRAD--------PARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLRE 236

                        170       180
                 ....*....|....*....|....*...
gi 93141049  182 IAtdpDDTHA--YNVADFESLSRIVDDL 207
Cdd:COG1240  237 IA---EATGGryFRADDLSELAAIYREI 261
fn3 pfam00041
Fibronectin type III domain;
774-852 6.86e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    774 RNVQVYNPTPNSLDVRWDPAP---GPVLQYRVVYSPVDGTRPSESIVVPGNTRMVHLERLIPDTLYSVNLVALYSDGEGN 850
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83


                   ..
gi 93141049    851 PS 852
Cdd:pfam00041   84 PS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 222-306 1.70e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 1.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  222 EAPSNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKRQEFYVSRM-ETSTVLKDLKPETEYVVNVYSVVEDE 297
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGGG 81


                 ....*....
gi 93141049  298 YSEPLKGTE 306
Cdd:cd00063   82 ESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 590-668 2.47e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  590 SGPRNLQVYNATSNSLTVKWDPAS---GRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDG 666
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                 ..
gi 93141049  667 EG 668
Cdd:cd00063   82 ES 83
fn3 pfam00041
Fibronectin type III domain;
954-1031 7.40e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 7.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    954 PPQNIHISDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEAF--VGEMTSYTLHNLNPSTTYDVNVYAQYDSGL 1028
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 93141049   1029 SVP 1031
Cdd:pfam00041   82 GPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 405-488 1.23e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.60  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  405 PQDLKLRDVTHSTMNVFWEPVP---GKVRKYIVRYK-TPEEDVKEVEVDR-SETSTSLKDLFSQTLYTVSVSAVHDEGES 479
Cdd:cd00063    4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYReKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                 ....*....
gi 93141049  480 PPVTAQETT 488
Cdd:cd00063   84 PPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 310-384 1.95e-12

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: 64.56  E-value: 1.95e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93141049     310 PVPVVSLNIYDVGPTTMHVQWQPV--GGATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVQAV 384
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 954-1029 2.79e-12

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: 64.17  E-value: 2.79e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     954 PPQNIHISDEWYTRFRVSWDPSP-----SPVLGYKIVYKPVGSNEPMEAFVGEMTSYTLHNLNPSTTYDVNVYAQYDSGL 1028
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 93141049    1029 S 1029
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
864-941 3.07e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 3.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    864 PRNLRVFGETTNSLSVAW---DHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDGDG 940
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 93141049    941 G 941
Cdd:pfam00041   83 P 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 590-668 5.91e-12

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: 63.02  E-value: 5.91e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     590 SGPRNLQVYNATSNSLTVKWD-PASGRVQKYRITYQPSTGEGNEQTTTI--GGRQNSVVLQKLKPDTPYTITVSSLYPDG 666
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 93141049     667 EG 668
Cdd:smart00060   82 EG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 862-940 8.31e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.90  E-value: 8.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  862 SGPRNLRVFGETTNSLSVAWDHAD---GPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDG 938
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                 ..
gi 93141049  939 DG 940
Cdd:cd00063   82 ES 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 223-293 1.70e-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: 59.17  E-value: 1.70e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93141049     223 APSNLVISERTHRSFRVSWTPP-SDSVDRYKVEY---YPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSV 293
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYrveYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1158-1328 1.19e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.11  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKfifNTVGGFDEISPAGIQVSFVQYSDEVksEFKLNTYNDKALALGALQNIRYRGGnT 1237
Cdd:COG1240   93 RDVVLVVDASGSMAAENRLEAAK---GALLDFLDDYRPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGGG-T 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 RTGKALtfikEKVLTWESGMRKNVPKVLVVVTDGR---SQDEVKKAALVIQQSGFSVFVVGVAD--VDYNELANIASKpS 1312
Cdd:COG1240  167 PLGDAL----ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA-T 241

                        170
                 ....*....|....*.
gi 93141049 1313 ERHVFIVDDFESFEKI 1328
Cdd:COG1240  242 GGRYFRADDLSELAAI 257
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 862-940 3.75e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 3.75e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     862 SGPRNLRVFGETTNSLSVAWDHADGPVQQ-YRIIYSPTVGDPIDEYTTV--PGRRNNVILQPLQPDTPYKITVIAVYEDG 938
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 93141049     939 DG 940
Cdd:smart00060   82 EG 83
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 33-238 1.76e-08

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 59.59  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    33 EADIVLLVDGSWSIGRANFRT-VRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQL--NAHRDKKSLLQAV-----AN 104
Cdd:PTZ00441   42 EVDLYLLVDGSGSIGYHNWIThVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALIIVkslrkTY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   105 LPYkgGNTLTGMALNFIRQQ-NFRTQagmRPRARKIGVLITDG--KSQDDVEAPSKKLKDEGVELFAIGIKNADEVELK- 180
Cdd:PTZ00441  122 LPY--GKTNMTDALLEVRKHlNDRVN---RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGQGINHQFNr 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93141049   181 -MIATDPDDTHA--YNVADFESLSRIVDDLTINLCNSVK-----GPGDLEAPSNLVISERTHRSFR 238
Cdd:PTZ00441  197 lLAGCRPREGKCkfYSDADWEEAKNLIKPFIAKVCTEVErtascGPWDEWTPCSVTCGKGTHSRSR 262
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1600-1733 2.02e-08

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: 58.76  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1600 RGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLSIP-GEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRG 1678
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPaGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 93141049  1679 FTGKDGamgprgpPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRGD 1733
Cdd:NF038329  217 EAGPAG-------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1600-1732 4.82e-08

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: 57.61  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1600 RGERGISG---AIGPPGPRGDIGPPGPQGPPGPQGPNGLsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGD 1676
Cdd:NF038329  119 KGEPGPAGpagPAGEQGPRGDRGETGPAGPAGPPGPQGE--RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 93141049  1677 RGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKP--GDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDG 254
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1600-1732 4.05e-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: 54.53  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1600 RGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGpmgppgdrgf 1679
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGP---------- 243

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 93141049  1680 TGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
fn3 pfam00041
Fibronectin type III domain;
1043-1118 8.22e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 8.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1043 VTDLKTYQIGWDTFCVKWSP----HRAATSYRLKLSPADGTRG-QEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLEG 1117
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 93141049   1118 P 1118
Cdd:pfam00041   83 P 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1601-1732 3.03e-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: 51.83  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1601 GERGISGAIGPPGPRGDigppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPGRTGTPGLpgppgpmgppgdrgfT 1680
Cdd:NF038329  117 GEKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGE---------------K 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 93141049  1681 GKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1601-1732 4.20e-05

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: 48.36  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1601 GERGISGAIGPPGPRGDIGPPGPQGPP--GPQGPNG-LSIPGEQGRQGMKGDAGEPGLPGRTGTPGLPgppgpmgppgdr 1677
Cdd:NF038329  201 GPAGEQGPAGPAGPDGEAGPAGEDGPAgpAGDGQQGpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------ 268

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 93141049  1678 gftGKDGAMGPRgppgppgspgspgvtGPSGKPGKPGDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  269 ---GPDGPDGKD---------------GERGPVGPAGKDGQNGKDGLPGKDGKDG 305
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1042-1127 6.30e-05

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: 43.64  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1042 NVTDLKTYQIGWDTFCVKWSP----HRAATSYRLKLSPADGTRGQEITVRGSETSHC-FTGLSPDTDYGVTVFVQTPNLE 1116
Cdd:cd00063    3 PPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEVEVTPGSETSYtLTGLKPGTEYEFRVRAVNGGGE 82

                         90
                 ....*....|.
gi 93141049 1117 GPGVSVKEHTT 1127
Cdd:cd00063   83 SPPSESVTVTT 93
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1705-1733 6.59e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.59e-05
                           10        20
                   ....*....|....*....|....*....
gi 93141049   1705 GPSGKPGKPGDHGRPGPSGLKGEKGDRGD 1733
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1042-1117 3.32e-04

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: 41.06  E-value: 3.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1042 NVTDLKTYQIGWDTFCVKWSP--HRAATSYRLKLSPADGTRG---QEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLE 1116
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 93141049    1117 G 1117
Cdd:smart00060   83 G 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 ...
 34-197 8.50e-93

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: 297.28  E-value: 8.50e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 113
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 193
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                 ....
gi 93141049  194 VADF 197
Cdd:cd01482  161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1158-1322 4.34e-84

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 272.24  E-value: 4.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFdEISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 1237
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAF-EIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 1317
Cdd:cd01482   80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                 ....*
gi 93141049 1318 IVDDF 1322
Cdd:cd01482  160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 34-197 9.41e-79

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: 257.16  E-value: 9.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 113
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 193
Cdd:cd01472   81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                 ....
gi 93141049  194 VADF 197
Cdd:cd01472  161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1158-1322 4.84e-71

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: 235.20  E-value: 4.84e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 1237
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLD-IGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 1317
Cdd:cd01472   80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159


                 ....*
gi 93141049 1318 IVDDF 1322
Cdd:cd01472  160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
35-206 1.42e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 222.54  E-value: 1.42e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     35 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL- 113
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQD-DVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAY 192
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 93141049    193 NVADFESLSRIVDD 206
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1159-1331 8.69e-62

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.05  E-value: 8.69e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1159 DIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTR 1238
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1239 -TGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD-EVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSERHV 1316
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 93141049   1317 FIVDDFESFEKIEDN 1331
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1356-1548 3.16e-59

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 202.20  E-value: 3.16e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1356 GFKMLEAYNLTEKNFASVQGVSLEsgsfPSYSAYRIQKNAFVNQPTADLHPNGLPPSYTIILLFRLlpeTPSDPFAIWQI 1435
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPE----PGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1436 TDRDYKPQVGVIADPSSKTLSFFNKDTRGEVQTVTFdteEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAG- 1514
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 93141049    1515 -NITTDGYEILGKLLKGeRKSAAFQIQSFDIVCSP 1548
Cdd:smart00210  151 pPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 34-192 6.42e-54

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 185.96  E-value: 6.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGN-T 112
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  113 LTGMALNFIRQQNFrTQAGMRPRARKIGVLITDGKSQD--DVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTH 190
Cdd:cd01450   81 NTGKALQYALEQLF-SESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                 ..
gi 93141049  191 AY 192
Cdd:cd01450  160 VF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1158-1317 4.24e-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: 183.65  E-value: 4.24e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGN- 1236
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1237 TRTGKALTFIKEKVLTwESGMRKNVPKVLVVVTDGRSQD--EVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSER 1314
Cdd:cd01450   80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                 ...
gi 93141049 1315 HVF 1317
Cdd:cd01450  159 HVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 35-204 1.74e-49

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: 173.79  E-value: 1.74e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049      35 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYK-GGNTL 113
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     114 TGMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQD---DVEAPSKKLKDEGVELFAIGIKNA-DEVELKMIATDPDDT 189
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 93141049     190 HAYNVADFESLSRIV 204
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 34-197 5.68e-46

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: 163.26  E-value: 5.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 113
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  114 -TGMALNFIRQQNFRTQAGMRPR--ARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDdtH 190
Cdd:cd01481   81 nTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                 ....*..
gi 93141049  191 AYNVADF 197
Cdd:cd01481  159 VFQVSDF 165
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 34-212 1.26e-45

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: 164.48  E-value: 1.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 113
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  114 TGMALNFIRQQNFRTQAGMRPRAR---KIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTH 190
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                        170       180
                 ....*....|....*....|..
gi 93141049  191 AYNVADFESLSRIVDDLTINLC 212
Cdd:cd01475  163 VFYVEDFSTIEELTKKFQGKIC 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1159-1328 1.86e-45

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: 162.24  E-value: 1.86e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1159 DIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYR-GGNT 1237
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1238 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD---EVKKAALVIQQSGFSVFVVGV-ADVDYNELANIASKPSE 1313
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 93141049    1314 RHVFIVDDFESFEKI 1328
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1158-1361 2.44e-42

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: 155.24  E-value: 2.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 1237
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLD-VGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 RTGKALTFIKEKVLTWESGMRK---NVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSER 1314
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEGARPgseRVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1315 HVFIVDDFESFEKIEDNL-------------ITFVCETATSSCPLIYLDGYTSpGFKMLE 1361
Cdd:cd01475  162 HVFYVEDFSTIEELTKKFqgkicvvpdlcatLSHVCQQVCISTPGSYLCACTE-GYALLE 220
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 35-203 1.38e-40

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: 148.27  E-value: 1.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   35 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTLT 114
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  115 GMALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQDDVEAPS--KKLKDEGVELFAIGI------KNADEvELKMIATDP 186
Cdd:cd01469   82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDviPQAEREGIIRYAIGVgghfqrENSRE-ELKTIASKP 160

                        170
                 ....*....|....*..
gi 93141049  187 DDTHAYNVADFESLSRI 203
Cdd:cd01469  161 PEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1158-1322 6.61e-39

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: 143.23  E-value: 6.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 1237
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLD-VGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 -RTGKALTFIKEKVLTWESG--MRKNVPKVLVVVTDGRSQDEVKKAALVIQQSGFSVFVVGVADVDYNELANIASKPSer 1314
Cdd:cd01481   80 lNTGSALDYVVKNLFTKSAGsrIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS-- 157


                 ....*...
gi 93141049 1315 HVFIVDDF 1322
Cdd:cd01481  158 FVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1159-1328 9.18e-38

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: 140.18  E-value: 9.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1159 DIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTR 1238
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLD-IGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1239 TGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAAlVIQQS---GFSVFVVGVADV-----DYNELANIASK 1310
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKD-VIPQAereGIIRYAIGVGGHfqrenSREELKTIASK 159

                        170
                 ....*....|....*...
gi 93141049 1311 PSERHVFIVDDFESFEKI 1328
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 34-192 7.53e-31

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: 119.98  E-value: 7.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYK-GGNT 112
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  113 LTGMALNFIRQQNFRTQagmRPRARKIGVLITDGKSQDD---VEAPSKKLKDEGVELFAIGIKN-ADEVELKMIATDPDD 188
Cdd:cd00198   81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                 ....
gi 93141049  189 THAY 192
Cdd:cd00198  158 GAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1158-1318 6.03e-29

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: 114.42  E-value: 6.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIgDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKS--EFKLNTYNDKALALGALQNIRYRGG 1235
Cdd:cd01476    1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLE-IGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1236 NTRTGKALTFiKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQ-QSGFSVFVVGVAD---VDYNELANIASkp 1311
Cdd:cd01476   79 TTATGAAIEV-ALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDpgtVDTEELHSITG-- 155


                 ....*..
gi 93141049 1312 SERHVFI 1318
Cdd:cd01476  156 NEDHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 34-187 6.01e-26

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: 105.94  E-value: 6.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIgRANFRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRT--EWQLNAHRDKKSLLQAVANLPYKGGN 111
Cdd:cd01476    1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  112 TLTGMALNFIRQQnFRTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDE-GVELFAIGIKN---ADEVELKMIATDPD 187
Cdd:cd01476   80 TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNED 158
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1158-1317 2.61e-24

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: 101.10  E-value: 2.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYR-GGN 1236
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLS-ASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1237 TRTGKALTFIKEkvlTWESGMRKNVPKVLVVVTDGRSQDEVKKAALVIQQ---SGFSVFVVGV-ADVDYNELANIASKPS 1312
Cdd:cd00198   80 TNIGAALRLALE---LLKSAKRPNARRVIILLTDGEPNDGPELLAEAARElrkLGITVYTIGIgDDANEDELKEIADKTT 156


                 ....*
gi 93141049 1313 ERHVF 1317
Cdd:cd00198  157 GGAVF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 35-171 7.15e-22

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: 95.14  E-value: 7.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   35 DIVLLVDGSWSIGRAN-FRTVRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQLNAHR--DKKSLLQAVA---NLPYK 108
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstNKDLALNAIRallSLYYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93141049  109 GGNTLTGMALNFIRQQNFRTqAGMRPRARKIGVLITDGKSQDDVEA--PSKKLKDEGVELFAIGI 171
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGVIIAVLGV 145
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 34-209 1.09e-18

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 85.90  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVF------DIGPKRVQIALAQYSGDPRTEWQ-LNAHRDKKSLLQAVANLP 106
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  107 YKGGNTLTGMALNFIRQQnfrTQAGMRPRARKIGVLITDGKSQ-DDVEAPSKKLKD---EGVELFAIGIKNADEVELKMI 182
Cdd:cd01480   83 YIGGGTFTDCALKYATEQ---LLEGSHQKENKFLLVITDGHSDgSPDGGIEKAVNEadhLGIKIFFVAVGSQNEEPLSRI 159

                        170       180
                 ....*....|....*....|....*...
gi 93141049  183 ATDPDDTH-AYNVADfESLSRIVDDLTI 209
Cdd:cd01480  160 ACDGKSALyRENFAE-LLWSFFIDDETA 186
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1158-1316 3.66e-17

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 81.28  E-value: 3.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGGF-----DEISPAGIQVSFVQYSDEVKSEFKL--NTYNDKALAlGALQNI 1230
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyRKDPAGSWRVGVVQYSDQQEVEAGFlrDIRNYTSLK-EAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1231 RYRGGNTRTGKALTFIKEKVLtweSGMRKNVPKVLVVVTDGRSQDE----VKKAALVIQQSGFSVFVVGVADVDYNELAN 1306
Cdd:cd01480   82 EYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDGSpdggIEKAVNEADHLGIKIFFVAVGSQNEEPLSR 158

                        170
                 ....*....|
gi 93141049 1307 IASKPSERHV 1316
Cdd:cd01480  159 IACDGKSALY 168
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1153-1337 8.39e-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: 77.55  E-value: 8.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1153 CKGAkADIVFLTDASWSIGDdNFNKVVKFIFNTVGGFdeISPaGIQVSFVQYSDEVKSEFKLNTYNDKAL-ALGALQNIr 1231
Cdd:cd01474    1 CAGH-FDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRF--NSP-GLRFSFITFSTRATKILPLTDDSSAIIkGLEVLKKV- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1232 YRGGNTRTGKALTFIKEKVLTWESGMRKNVpKVLVVVTDGRSQDEV----KKAALVIQQSGFSVFVVGVADVDYNELANI 1307
Cdd:cd01474   75 TPSGQTYIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINI 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 93141049 1308 ASkpSERHVFIVDD-FESFEKIEDNLITFVC 1337
Cdd:cd01474  154 AD--SKEYVFPVTSgFQALSGIIESVVKKAC 182
fn3 pfam00041
Fibronectin type III domain;
592-670 1.42e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.60  E-value: 1.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    592 PRNLQVYNATSNSLTVKWDPA---SGRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDGEG 668
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 93141049    669 GR 670
Cdd:pfam00041   83 PP 84
fn3 pfam00041
Fibronectin type III domain;
223-301 1.83e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.22  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    223 APSNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKR-QEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEY 298
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGngpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 93141049    299 SEP 301
Cdd:pfam00041   82 GPP 84
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1159-1296 4.60e-15

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: 75.50  E-value: 4.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1159 DIVFLTDASWSIGDDN-FNKVVKFIFNTVGGFDeISPAGIQVSFVQYSDEVKSEFKLNTYN--DKALALGALQNIR---Y 1232
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLN-ISPDEINLYLVTFSTNAKELIRLSSPNstNKDLALNAIRALLslyY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93141049 1233 RGGNTRTGKALTFIkEKVLTWESGMRKNVPKVLVVVTDGRSQDEVK--KAALVIQQSGFSVFVVGV 1296
Cdd:cd01471   81 PNGSTNTTSALLVV-EKHLFDTRGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 954-1033 1.10e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 71.37  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  954 PPQNIHISDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEA--FVGEMTSYTLHNLNPSTTYDVNVYAQYDSGL 1028
Cdd:cd00063    3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                 ....*
gi 93141049 1029 SVPLT 1033
Cdd:cd00063   83 SPPSE 87
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
255-822 1.14e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 79.66  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  255 YYPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSVVEDEYSEPLKGTEKTLPVPVVSLNIYDVGPTTMHVQWQPVG 334
Cdd:COG3401    5 YLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  335 GATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVqavlhdltsepVTVREVTLPLPRPQDLKLRDVT 414
Cdd:COG3401   85 AAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAV-----------AGGAATAGTYALGAGLYGVDGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  415 HSTMNVFWEPVPGKVRKYIVRYKTPEEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEGESPP---VTAQETTRPV 491
Cdd:COG3401  154 NASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPsneVSVTTPTTPP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  492 PAPTNLKITEVTSEGFRGTWD-HGASDVSLYRITWAPfGSSDKMETILNGDENTLVFENLNPNTIYEVSITAIYPDESES 570
Cdd:COG3401  234 SAPTGLTATADTPGSVTLSWDpVTESDATGYRVYRSN-SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNES 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  571 DDligSErTLPILTTQAPKSGPRNLQVYNATSNSLTVKWDPASG-RVQKYRItYQPSTGEGNEQTTTIGGRQNSVVLQKL 649
Cdd:COG3401  313 AP---SN-VVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGL 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  650 KPDTPYTITVSSLYPDGEGGRMTGRGKTKPLNTVRNLRVYDPSTSTLNVRWDHAEGNPRQYKLFYAPAAGGPEELVPIPG 729
Cdd:COG3401  388 TPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNA 467

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  730 NTNYAILRNLQPDTSYTVTVVPVYTEGDGGRTSDTGR-----TLMRGLARNVQVYNPTPNSLDVRWDPAPGPVLQYRVVY 804
Cdd:COG3401  468 VPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSvtnsvSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLI 547

                        570
                 ....*....|....*...
gi 93141049  805 SPVDGTRPSESIVVPGNT 822
Cdd:COG3401  548 TDLVSLTTSASSSVSGAG 565
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 31-207 5.99e-14

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: 73.82  E-value: 5.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   31 RAEADIVLLVDGSWSIGRAN-FRTVRSFISRIVEVFdigPKRVQIALAQYSGDPrtEWQLNAHRDKKSLLQAVANLPYKG 109
Cdd:COG1240   90 QRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  110 GNTLT---GMALNFIRQQNfrtqagmrPRARKIGVLITDGK---SQDDVEAPSKKLKDEGVELFAIGI--KNADEVELKM 181
Cdd:COG1240  165 GTPLGdalALALELLKRAD--------PARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLRE 236

                        170       180
                 ....*....|....*....|....*...
gi 93141049  182 IAtdpDDTHA--YNVADFESLSRIVDDL 207
Cdd:COG1240  237 IA---EATGGryFRADDLSELAAIYREI 261
fn3 pfam00041
Fibronectin type III domain;
774-852 6.86e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    774 RNVQVYNPTPNSLDVRWDPAP---GPVLQYRVVYSPVDGTRPSESIVVPGNTRMVHLERLIPDTLYSVNLVALYSDGEGN 850
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83


                   ..
gi 93141049    851 PS 852
Cdd:pfam00041   84 PS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 222-306 1.70e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.91  E-value: 1.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  222 EAPSNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKRQEFYVSRM-ETSTVLKDLKPETEYVVNVYSVVEDE 297
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGGG 81


                 ....*....
gi 93141049  298 YSEPLKGTE 306
Cdd:cd00063   82 ESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 590-668 2.47e-13

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 67.52  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  590 SGPRNLQVYNATSNSLTVKWDPAS---GRVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDG 666
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                 ..
gi 93141049  667 EG 668
Cdd:cd00063   82 ES 83
fn3 pfam00041
Fibronectin type III domain;
954-1031 7.40e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.90  E-value: 7.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    954 PPQNIHISDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEAF--VGEMTSYTLHNLNPSTTYDVNVYAQYDSGL 1028
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 93141049   1029 SVP 1031
Cdd:pfam00041   82 GPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 405-488 1.23e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.60  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  405 PQDLKLRDVTHSTMNVFWEPVP---GKVRKYIVRYK-TPEEDVKEVEVDR-SETSTSLKDLFSQTLYTVSVSAVHDEGES 479
Cdd:cd00063    4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYReKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                 ....*....
gi 93141049  480 PPVTAQETT 488
Cdd:cd00063   84 PPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 774-853 1.45e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  774 RNVQVYNPTPNSLDVRWDPAP---GPVLQYRVVYSPVDGTRPSESIVVPGNTRMVHLERLIPDTLYSVNLVALYSDGEGN 850
Cdd:cd00063    5 TNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84


                 ...
gi 93141049  851 PSP 853
Cdd:cd00063   85 PSE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 310-384 1.95e-12

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: 64.56  E-value: 1.95e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93141049     310 PVPVVSLNIYDVGPTTMHVQWQPV--GGATGYILSYKPVKDTEPTRPKEVRLGPTVNDMQLTDLVPNTEYAVTVQAV 384
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 954-1029 2.79e-12

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: 64.17  E-value: 2.79e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     954 PPQNIHISDEWYTRFRVSWDPSP-----SPVLGYKIVYKPVGSNEPMEAFVGEMTSYTLHNLNPSTTYDVNVYAQYDSGL 1028
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 93141049    1029 S 1029
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
864-941 3.07e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 3.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    864 PRNLRVFGETTNSLSVAW---DHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDGDG 940
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 93141049    941 G 941
Cdd:pfam00041   83 P 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 590-668 5.91e-12

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: 63.02  E-value: 5.91e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     590 SGPRNLQVYNATSNSLTVKWD-PASGRVQKYRITYQPSTGEGNEQTTTI--GGRQNSVVLQKLKPDTPYTITVSSLYPDG 666
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 93141049     667 EG 668
Cdd:smart00060   82 EG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 862-940 8.31e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.90  E-value: 8.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  862 SGPRNLRVFGETTNSLSVAWDHAD---GPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDG 938
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                 ..
gi 93141049  939 DG 940
Cdd:cd00063   82 ES 83
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 31-215 8.50e-12

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: 65.99  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   31 RAEADIVLLVDGSWSIGrANFRTVRSFISRIVEVFdIGPKrVQIALAQYSGDPRTEWQLNAHRDK--KSLLQAVANLPyk 108
Cdd:cd01474    2 AGHFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAiiKGLEVLKKVTP-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  109 GGNTLTGMALNFIRQQNFRTQAGMRpRARKIGVLITDGKSQDDV----EAPSKKLKDEGVELFAIGIKNADEVELKMIAT 184
Cdd:cd01474   77 SGQTYIHEGLENANEQIFNRNGGGR-ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIAD 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 93141049  185 DPDdtHAYNVAD-FESLSRIVDDLTINLCNSV 215
Cdd:cd01474  156 SKE--YVFPVTSgFQALSGIIESVVKKACIEI 185
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 310-399 1.35e-11

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.51  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  310 PVPVVSLNIYDVGPTTMHVQWQPV----GGATGYILSYKPVKDTEPTRPKEVRlgPTVNDMQLTDLVPNTEYAVTVQAVL 385
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPeddgGPITGYVVEYREKGSGDWKEVEVTP--GSETSYTLTGLKPGTEYEFRVRAVN 78

                         90
                 ....*....|....
gi 93141049  386 HDLTSEPVTVREVT 399
Cdd:cd00063   79 GGGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
222-473 1.71e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.26  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  222 EAPSNLVISERTHRSFRVSWTPPSDS-VDRYKVEYYPVSGGKRQEFYVSRmETSTVLKDLKPETEYVVNVYSV----VED 296
Cdd:COG3401  234 SAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGPFTKVATVT-TTSYTDTGLTNGTTYYYRVTAVdaagNES 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  297 EYSEPLKGT-EKTLPVPVVSLNIYDVGPTTMHVQWQPV--GGATGYILSYKPVKDTEPTRPKEVRLGPTVNDmqlTDLVP 373
Cdd:COG3401  313 APSNVVSVTtDLTPPAAPSGLTATAVGSSSITLSWTASsdADVTGYNVYRSTSGGGTYTKIAETVTTTSYTD---TGLTP 389

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  374 NTEYAVTVQAV----LHDLTSEPVTVREVTLP----LPRPQDLKLRDVTHSTMNVFWEPVPGKVRKYIVRYKTPEEDVKE 445
Cdd:COG3401  390 GTTYYYKVTAVdaagNESAPSEEVSATTASAAsgesLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVP 469

                        250       260
                 ....*....|....*....|....*...
gi 93141049  446 VEVDRSETSTSLKDLFSQTLYTVSVSAV 473
Cdd:COG3401  470 FTTTSSTVTATTTDTTTANLSVTTGSLV 497
fn3 pfam00041
Fibronectin type III domain;
403-481 2.48e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 2.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    403 PRPQDLKLRDVTHSTMNVFWEPVP---GKVRKYIVRYKTP--EEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEG 477
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 93141049    478 ESPP 481
Cdd:pfam00041   81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 405-479 3.53e-11

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 61.09  E-value: 3.53e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     405 PQDLKLRDVTHSTMNVFWEPVP-----GKVRKYIVRYKTPEEDVKEVEVDRSETSTSLKDLFSQTLYTVSVSAVHDEGES 479
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 223-293 1.70e-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: 59.17  E-value: 1.70e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93141049     223 APSNLVISERTHRSFRVSWTPP-SDSVDRYKVEY---YPVSGGKRQEFYVSRMETSTVLKDLKPETEYVVNVYSV 293
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYrveYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
683-761 2.76e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.58  E-value: 2.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    683 VRNLRVYDPSTSTLNVRWDHAE---GNPRQYKLFYAPAAGGPEEL-VPIPGNTNYAILRNLQPDTSYTVTVVPVYTEGDG 758
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ...
gi 93141049    759 GRT 761
Cdd:pfam00041   83 PPS 85
fn3 pfam00041
Fibronectin type III domain;
312-392 5.52e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.42  E-value: 5.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    312 PVVSLNIYDVGPTTMHVQWQPV----GGATGYILSYKPVKDTEPtrPKEVRLGPTVNDMQLTDLVPNTEYAVTVQAVLHD 387
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGEP--WNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*
gi 93141049    388 LTSEP 392
Cdd:pfam00041   80 GEGPP 84
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1158-1328 1.19e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 61.11  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1158 ADIVFLTDASWSIGDDNFNKVVKfifNTVGGFDEISPAGIQVSFVQYSDEVksEFKLNTYNDKALALGALQNIRYRGGnT 1237
Cdd:COG1240   93 RDVVLVVDASGSMAAENRLEAAK---GALLDFLDDYRPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGGG-T 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1238 RTGKALtfikEKVLTWESGMRKNVPKVLVVVTDGR---SQDEVKKAALVIQQSGFSVFVVGVAD--VDYNELANIASKpS 1312
Cdd:COG1240  167 PLGDAL----ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA-T 241

                        170
                 ....*....|....*.
gi 93141049 1313 ERHVFIVDDFESFEKI 1328
Cdd:COG1240  242 GGRYFRADDLSELAAI 257
fn3 pfam00041
Fibronectin type III domain;
492-564 1.34e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 1.34e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93141049    492 PAPTNLKITEVTSEGFRGTW---DHGASDVSLYRITWAPFGSSDKM-ETILNGDENTLVFENLNPNTIYEVSITAIY 564
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 862-940 3.75e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 55.31  E-value: 3.75e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     862 SGPRNLRVFGETTNSLSVAWDHADGPVQQ-YRIIYSPTVGDPIDEYTTV--PGRRNNVILQPLQPDTPYKITVIAVYEDG 938
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 93141049     939 DG 940
Cdd:smart00060   82 EG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 683-758 1.09e-08

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  683 VRNLRVYDPSTSTLNVRWDHAE---GNPRQYKLFYAPA-AGGPEELVPIPGNTNYAILRNLQPDTSYTVTVVPVYTEGDG 758
Cdd:cd00063    4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
VWA_2 pfam13519
von Willebrand factor type A domain;
36-143 1.41e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     36 IVLLVDGSWSI-----GRANFRTVRSFISRIVEVFdigpKRVQIALAQYSGDPRTEWQLNahRDKKSLLQAVANLPYKGG 110
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 93141049    111 NTLTGMALNFIRQqnfrTQAGMRPRARKIGVLI 143
Cdd:pfam13519   75 GTNLAAALQLARA----ALKHRRKNQPRRIVLI 103
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 774-849 1.43e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 1.43e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     774 RNVQVYNPTPNSLDVRWDPAP-----GPVLQYRVVYSPVDGTrpSESIVVPGNTRMVHLERLIPDTLYSVNLVALYSDGE 848
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSE--WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 93141049     849 G 849
Cdd:smart00060   83 G 83
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 33-238 1.76e-08

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 59.59  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    33 EADIVLLVDGSWSIGRANFRT-VRSFISRIVEVFDIGPKRVQIALAQYSGDPRTEWQL--NAHRDKKSLLQAV-----AN 104
Cdd:PTZ00441   42 EVDLYLLVDGSGSIGYHNWIThVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALIIVkslrkTY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   105 LPYkgGNTLTGMALNFIRQQ-NFRTQagmRPRARKIGVLITDG--KSQDDVEAPSKKLKDEGVELFAIGIKNADEVELK- 180
Cdd:PTZ00441  122 LPY--GKTNMTDALLEVRKHlNDRVN---RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGQGINHQFNr 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93141049   181 -MIATDPDDTHA--YNVADFESLSRIVDDLTINLCNSVK-----GPGDLEAPSNLVISERTHRSFR 238
Cdd:PTZ00441  197 lLAGCRPREGKCkfYSDADWEEAKNLIKPFIAKVCTEVErtascGPWDEWTPCSVTCGKGTHSRSR 262
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1600-1733 2.02e-08

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: 58.76  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1600 RGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLSIP-GEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRG 1678
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPaGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 93141049  1679 FTGKDGamgprgpPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRGD 1733
Cdd:NF038329  217 EAGPAG-------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1600-1732 4.82e-08

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: 57.61  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1600 RGERGISG---AIGPPGPRGDIGPPGPQGPPGPQGPNGLsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGD 1676
Cdd:NF038329  119 KGEPGPAGpagPAGEQGPRGDRGETGPAGPAGPPGPQGE--RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 93141049  1677 RGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKP--GDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDG 254
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1159-1330 7.62e-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: 54.60  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1159 DIVFLTDASWSIGDDNFNKVVKFIFNTVggfDEISPAGIQVSF--VQYSDEVKSEFKLNTY--NDKALALGALQNIRYRG 1234
Cdd:cd01470    2 NIYIALDASDSIGEEDFDEAKNAIKTLI---EKISSYEVSPRYeiISYASDPKEIVSIRDFnsNDADDVIKRLEDFNYDD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1235 GNTRTGkalTFIKEKVLTWESGMR--KNVPK--------VLVVVTDGRSQ---------DEVKkAALVIQQSGFS----- 1290
Cdd:cd01470   79 HGDKTG---TNTAAALKKVYERMAleKVRNKeafnetrhVIILFTDGKSNmggsplptvDKIK-NLVYKNNKSDNpredy 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 93141049 1291 --VFVVGV-ADVDYNELANIAS-KPSERHVFIVDDFESFEKIED 1330
Cdd:cd01470  155 ldVYVFGVgDDVNKEELNDLASkKDNERHFFKLKDYEDLQEVFD 198
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 35-213 7.86e-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: 54.25  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   35 DIVLLVDGSWSIGRANFRT-VRSFISRIVEVFDIGPKRVQIALAQYSGDPRT--EWQLNAHRDKKSLLQAVANLP--YK- 108
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDvvPFSDEERYDKNELLKKINDLKnsYRs 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  109 GGNTLTGMALNFIRQQNFRtQAGMRPRARKIGVLITDG----KSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIAt 184
Cdd:cd01473   82 GGETYIVEALKYGLKNYTK-HGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLA- 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 93141049  185 dpdDTHAYNV-------ADFESLSRIVDDLTINLCN 213
Cdd:cd01473  160 ---GCDINNDncpnvikTEWNNLNGISKFLTDKICD 192
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 31-183 1.10e-07

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 55.07  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   31 RAEADIVLLVDGSWSIGRANFRTVRSFISRIVEVFdigPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGG 110
Cdd:COG2425  116 LLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRAL---RPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 93141049  111 NTLTG---MALNFIRQQNFRtqagmrpraRKIGVLITDGKSQDDVEAPSKKL--KDEGVELFAIGIKNADEVEL-KMIA 183
Cdd:COG2425  193 TDIAPalrAALELLEEPDYR---------NADIVLITDGEAGVSPEELLREVraKESGVRLFTVAIGDAGNPGLlEALA 262
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 683-758 1.57e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 50.69  E-value: 1.57e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049     683 VRNLRVYDPSTSTLNVRWDHAEGNPR-----QYKLFYAPAaGGPEELVPIPGNTNYAILRNLQPDTSYTVTVVPVYTEGD 757
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 93141049     758 G 758
Cdd:smart00060   83 G 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
553-1069 1.85e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.16  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  553 NTIYEVSITAIYPDESESDDLIGSERTLPILTTQAPKSGPRNLQVYNATSNSLTVKWDPASGR-VQKYRITYQPSTGEGN 631
Cdd:COG3401   15 ASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSgVAAVAVAAAPPTATGL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  632 EQTTTIGGRQNSVVLQKLKPDTPYTITVSSLYPDGEGGRMTGRGKTKPLNTVRNLRVYDPSTSTLNVRWDHAEGNPRQYK 711
Cdd:COG3401   95 TTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  712 LFYAPAAGGPeelVPIPGNTNYAILRNLQPDTSYTVTVVPVYTEGDGGRTSDTGRTLMRGLAR---NVQVYNPTPNSLDV 788
Cdd:COG3401  175 SATAAVATTS---LTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSaptGLTATADTPGSVTL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  789 RWDPAPGPVLQ-YRVVYSPVDGTrPSESIVVPGNTRMVHLErLIPDTLYSVNLVALYSDGEG----NPSPAQGRTLPRSG 863
Cdd:COG3401  252 SWDPVTESDATgYRVYRSNSGDG-PFTKVATVTTTSYTDTG-LTNGTTYYYRVTAVDAAGNEsapsNVVSVTTDLTPPAA 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  864 PRNLRVFGETTNSLSVAWDHADGP-VQQYRIIYSPTVGDPIDEYTTVPgRRNNVILQPLQPDTPYKITVIAVYEDGDGGH 942
Cdd:COG3401  330 PSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIAETV-TTTSYTDTGLTPGTTYYYKVTAVDAAGNESA 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  943 LTGNGRTVGLLPPQNIHISDEWYTRFRVSWDPSPSPVL--------------GYKIVYKPVGSNEPMEAFVGEMTSYTL- 1007
Cdd:COG3401  409 PSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASaasnpgvsaavladGGDTGNAVPFTTTSSTVTATTTDTTTAn 488

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93141049 1008 ------HNLNPSTTYDVNVYAQYDSGLSVPLTDQGTTLYLNVTDLKTYQIGWDTFCVKWSPHRAATSY 1069
Cdd:COG3401  489 lsvttgSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTS 556
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1600-1732 4.05e-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: 54.53  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1600 RGERGISGAIGPPGPRGDIGPPGPQGPPGPQGPNGLsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGpmgppgdrgf 1679
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP--AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGP---------- 243

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 93141049  1680 TGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 492-564 5.43e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.42  E-value: 5.43e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93141049  492 PAPTNLKITEVTSEGFRGTWD---HGASDVSLYRITWAPFGSSDKME-TILNGDENTLVFENLNPNTIYEVSITAIY 564
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
fn3 pfam00041
Fibronectin type III domain;
1043-1118 8.22e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 8.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1043 VTDLKTYQIGWDTFCVKWSP----HRAATSYRLKLSPADGTRG-QEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLEG 1117
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 93141049   1118 P 1118
Cdd:pfam00041   83 P 83
VWA_2 pfam13519
von Willebrand factor type A domain;
1160-1268 2.78e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.67  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1160 IVFLTDASWSIGDD-----NFNKVVKFIFNTVGGFdeispAGIQVSFVQYSDEVKSEFKLNTynDKALALGALQNIRYRG 1234
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSL-----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 93141049   1235 GNTRTGKALtfikEKVLTWESGMRKNVPKVLVVV 1268
Cdd:pfam13519   74 GGTNLAAAL----QLARAALKHRRKNQPRRIVLI 103
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1601-1732 3.03e-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: 51.83  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1601 GERGISGAIGPPGPRGDigppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPGRTGTPGLpgppgpmgppgdrgfT 1680
Cdd:NF038329  117 GEKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGE---------------K 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 93141049  1681 GKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 492-564 1.00e-05

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: 45.30  E-value: 1.00e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 93141049     492 PAPTNLKITEVTSEGFRGTWDHGASDVSL-----YRITWAPfGSSDKMETILNGDENTLVFENLNPNTIYEVSITAIY 564
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgyivgYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1159-1308 2.18e-05

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: 47.31  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1159 DIVFLTDASWSIGDDNFNK-VVKFIFNTVGGFdEISPAGIQVSFVQYSDEVKSEFKL---NTYNDKAL--ALGALQNIRY 1232
Cdd:cd01473    2 DLTLILDESASIGYSNWRKdVIPFTEKIINNL-NISKDKVHVGILLFAEKNRDVVPFsdeERYDKNELlkKINDLKNSYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1233 RGGNTRTGKALTFIKEKVlTWESGMRKNVPKVLVVVTDGRSQDEVKKA----ALVIQQSGFSVFVVGVADVDYNELANIA 1308
Cdd:cd01473   81 SGGETYIVEALKYGLKNY-TKHGNRRKDAPKVTMLFTDGNDTSASKKElqdiSLLYKEENVKLLVVGVGAASENKLKLLA 159
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1601-1732 4.20e-05

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: 48.36  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  1601 GERGISGAIGPPGPRGDIGPPGPQGPP--GPQGPNG-LSIPGEQGRQGMKGDAGEPGLPGRTGTPGLPgppgpmgppgdr 1677
Cdd:NF038329  201 GPAGEQGPAGPAGPDGEAGPAGEDGPAgpAGDGQQGpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------ 268

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 93141049  1678 gftGKDGAMGPRgppgppgspgspgvtGPSGKPGKPGDHGRPGPSGLKGEKGDRG 1732
Cdd:NF038329  269 ---GPDGPDGKD---------------GERGPVGPAGKDGQNGKDGLPGKDGKDG 305
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1042-1127 6.30e-05

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: 43.64  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1042 NVTDLKTYQIGWDTFCVKWSP----HRAATSYRLKLSPADGTRGQEITVRGSETSHC-FTGLSPDTDYGVTVFVQTPNLE 1116
Cdd:cd00063    3 PPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEVEVTPGSETSYtLTGLKPGTEYEFRVRAVNGGGE 82

                         90
                 ....*....|.
gi 93141049 1117 GPGVSVKEHTT 1127
Cdd:cd00063   83 SPPSESVTVTT 93
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1705-1733 6.59e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.59e-05
                           10        20
                   ....*....|....*....|....*....
gi 93141049   1705 GPSGKPGKPGDHGRPGPSGLKGEKGDRGD 1733
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
862-1108 2.07e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 46.15  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  862 SGPRNLRVFGETTNSLSVAWDHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYEDGDG- 940
Cdd:COG3401  140 TYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESa 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  941 --GHLTGNGRTVGLLPPQNIHISDEWYTRFRVSWDPSPSP-VLGYKIVYKPVGSNEPMEAFVGEMTSYTLHNLNPSTTYD 1017
Cdd:COG3401  220 psNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYY 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049 1018 VNVYAQYD----SGLSVPLTDQGTTLYLNV-TDLKTYQIGWDTFCVKW--SPHRAATSYRLKLSPADGTRGQEITVRGSE 1090
Cdd:COG3401  300 YRVTAVDAagneSAPSNVVSVTTDLTPPAApSGLTATAVGSSSITLSWtaSSDADVTGYNVYRSTSGGGTYTKIAETVTT 379

                        250
                 ....*....|....*...
gi 93141049 1091 TSHCFTGLSPDTDYGVTV 1108
Cdd:COG3401  380 TSYTDTGLTPGTTYYYKV 397
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1042-1117 3.32e-04

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: 41.06  E-value: 3.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049    1042 NVTDLKTYQIGWDTFCVKWSP--HRAATSYRLKLSPADGTRG---QEITVRGSETSHCFTGLSPDTDYGVTVFVQTPNLE 1116
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 93141049    1117 G 1117
Cdd:smart00060   83 G 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1601-1727 3.83e-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: 40.17  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   1601 GERGISGAIGPPGPRGDigppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPGrtgtpglpgppgpmgppgdrgft 1680
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGP--------------------PGPPGPPGPPGPPGEPGPPG----------------------- 37

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 93141049   1681 gkdgamgprgppgPpgspgspgvtgpsgkPGKPGDHGRPGPSGLKGE 1727
Cdd:pfam01391   38 -------------P---------------PGPPGPPGPPGAPGAPGP 56
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
467-655 1.75e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 43.40  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  467 TVSVSAV-HDEGESPPVT--AQETTRPVPAPTNLKITEVTSEGFRG--------TWDHGASDVSlYRITWAPFGSS--DK 533
Cdd:COG4733  503 TYTITAVqHAPEKYAAIDagAFDDVPPQWPPVNVTTSESLSVVAQGtavttltvSWDAPAGAVA-YEVEWRRDDGNwvSV 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  534 METILNGDEntlvFENLNPNTiYEVSITAIYPDESESDDLIGSERTLPILTTQAPKsgPRNLQVyNATSNSLTVKWDPAS 613
Cdd:COG4733  582 PRTSGTSFE----VPGIYAGD-YEVRVRAINALGVSSAWAASSETTVTGKTAPPPA--PTGLTA-TGGLGGITLSWSFPV 653

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 93141049  614 G-RVQKYRITYQPSTGEGNEQTTTIGGRQNSVVLQKLKPDTPY 655
Cdd:COG4733  654 DaDTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTY 696
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
35-208 2.49e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 41.06  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   35 DIVLLVDGSWS-----IGRANfRTVRSFISRIVEVfDIGPKRVQIALAQYSGDPRTewqlnaHRDKKSLLQ-AVANLPYk 108
Cdd:COG4245    7 PVYLLLDTSGSmsgepIEALN-EGLQALIDELRQD-PYALETVEVSVITFDGEAKV------LLPLTDLEDfQPPDLSA- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  109 GGNTLTG----MALNFIRQQNFRTQAGMRPRARKIGVLITDGKSQD-DVEAPSKKLKD----EGVELFAIGI-KNADEVE 178
Cdd:COG4245   78 SGGTPLGaaleLLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKDgeaaKKANIFAIGVgPDADTEV 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 93141049  179 LKMIAtdpDDTHAYNVADFESLSRIVDDLT 208
Cdd:COG4245  158 LKQLT---DPVRALDALDGLDFREFFKWLS 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1597-1657 2.56e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 93141049   1597 KGPRGERGISGAIGPPGPRGDigppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPG 1657
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGP--------------------PGEPGPPGPPGPPGPPGPPG 49
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 34-192 3.12e-03

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 40.33  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049   34 ADIVLLVDGSWSIGRANFRTVRSFISRIVEvfDIGPKRvQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 113
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVD--QLRPDD-RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  114 -TGMALNfIRQqnfrTQAGMRPRARKIGVLITDGK------SQDDVEAPSKKLKDEGVELFAIGI-KNADEVELKMIATD 185
Cdd:cd01465   78 gAGIQLG-YQE----AQKHFVPGGVNRILLATDGDfnvgetDPDELARLVAQKRESGITLSTLGFgDNYNEDLMEAIADA 152


                 ....*..
gi 93141049  186 PDDTHAY 192
Cdd:cd01465  153 GNGNTAY 159
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 109-200 3.16e-03

VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 40.40  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  109 GGNTLTGMALN-FIRQQNFRTQagmRPRARKIG------VLITDGKSQDDVEAPSKKLK---DEGVELFAIGI-KNADEV 177
Cdd:cd01464   76 SGGTSMGAALElALDCIDRRVQ---RYRADQKGdwrpwvFLLTDGEPTDDLTAAIERIKearDSKGRIVACAVgPKADLD 152

                         90       100
                 ....*....|....*....|....
gi 93141049  178 ELKMIATD-PDDTHAYNVADFESL 200
Cdd:cd01464  153 TLKQITEGvPLLDDALSGLNFFKW 176
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
784-963 5.22e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 41.85  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  784 NSLDVRWDPAPGpVLQYRVVYSPVDGTRpsesIVVPGNTRMVHLERLIPDTLYSVNLVALYSDG-EGNPSPA-----QGR 857
Cdd:COG4733  552 TTLTVSWDAPAG-AVAYEVEWRRDDGNW----VSVPRTSGTSFEVPGIYAGDYEVRVRAINALGvSSAWAASsettvTGK 626

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93141049  858 TLPRSGPRNLRVFGeTTNSLSVAWDHADGP-VQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAVYE 936
Cdd:COG4733  627 TAPPPAPTGLTATG-GLGGITLSWSFPVDAdTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDR 705

                        170       180
                 ....*....|....*....|....*..
gi 93141049  937 DGDGGHLTGNGRTVGLLPPQNIHISDE 963
Cdd:COG4733  706 SGNVSAWWVSGQASADAAGILDAITGQ 732
 
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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