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Conserved domains on  [gi|507116137|ref|NP_001265227|]
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collagen alpha-5(VI) chain isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 627-787 3.02e-54

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: 187.44  E-value: 3.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL 706
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  707 TGKALNFV-GQYFTHSKGARLGAKKFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEIS--GDSSLVFH 783
Cdd:cd01472    81 TGKALKYVrENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIAsdPKELYVFN 160


                  ....
gi 507116137  784 VENF 787
Cdd:cd01472   161 VADF 164
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1730 2.67e-48

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: 180.10  E-value: 2.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1478 HGFPGIKGE---KGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQnnniKGQKGSKGEQGRQGRSGQKGVQGSPSSRGSR 1554
Cdd:NF038329  113 LKGDGEKGEpgpAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE----RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1555 GREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGeKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGL 1634
Cdd:NF038329  189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1635 PGDLGPVGQTGQRGRQGDSGipgygqmgRKGVKGPRGFPGDAGQKGDignpgipggpgpkgfrglALTVGLKGEEGSRGL 1714
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAG--------KDGQNGKDGLPGKDGKDGQ------------------NGKDGLPGKDGKDGQ 321

                         250
                  ....*....|....*.
gi 507116137 1715 PGPPGQRGIKGMAGQP 1730
Cdd:NF038329  322 PGKDGLPGKDGKDGQP 337
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 441-590 3.64e-46

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: 164.32  E-value: 3.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGTY 520
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  521 TGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIA 590
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIA 150
VWA pfam00092
von Willebrand factor type A domain;
814-985 2.14e-43

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 156.67  E-value: 2.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNTY 892
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   893 TAKALKHA-NALFTEEHGSRIkqNVKQMLIVITDGESHDHDqLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKNNT 971
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARP--GAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*.
gi 507116137   972 --IYVDNFDKLKDVFT 985
Cdd:pfam00092  158 hvFTVSDFEALEDLQD 173
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 29-195 2.43e-37

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


The actual alignment was detected with superfamily member cd01472:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 138.90  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLkKNFQFIGGSL 108
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAV-KNLRYIGGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  109 QIGKALQEAHRTYFSAPinGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATSHFHFN 188
Cdd:cd01472    80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                  ....*..
gi 507116137  189 LRTIRDL 195
Cdd:cd01472   158 VFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2290-2467 2.97e-35

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: 132.80  E-value: 2.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2290 MDVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSPpgympnteecPVYLEFDLVTYNSIHQ 2369
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPD------KTRVGLVQYSD----------DVRVEFSLNDYKSKDD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2370 MKHHLQDSQQLNGD-VFIGHALQWTIDNVFVGTP-NLRKNKVIFVISAGetNSLDKDVLRNVSLRAKCQGYSIFVFSFGP 2447
Cdd:cd01450    65 LLKAVKNLKYLGGGgTNTGKALQYALEQLFSESNaRENVPKVIIVLTDG--RSDDGGDPKEAAAKLKDEGIKVFVVGVGP 142

                         170       180
                  ....*....|....*....|
gi 507116137 2448 kHNDKELEELASHPLDHHLV 2467
Cdd:cd01450   143 -ADEEELREIASCPSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
236-404 3.22e-30

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.92  E-value: 3.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   236 DLVFLVDESLG-TGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQ-VGKSN 313
Cdd:pfam00092    1 DIVFLLDGSGSiGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   314 TGAAIDQMRRDGFSESYGSRRaqGVPQIAVLVTH-RPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPEQT 392
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDgRSQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|..
gi 507116137   393 ISTLKSYADLET 404
Cdd:pfam00092  159 VFTVSDFEALED 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1962-2137 6.46e-30

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


:

Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 117.78  E-value: 6.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1962 MDVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLM 2041
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPD------KTRVGLVQYS---------DDVRVEFSLNDYKSKDDL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2042 KNHIQtSFQQLNGEAT-IGRALLWTTENLFPETPY-LRKHKVIFVVSAGENYERKEFVKmMALRAKCQGYVIFVISLGST 2119
Cdd:cd01450    66 LKAVK-NLKYLGGGGTnTGKALQYALEQLFSESNArENVPKVIIVLTDGRSDDGGDPKE-AAAKLKDEGIKVFVVGVGPA 143

                         170
                  ....*....|....*...
gi 507116137 2120 RKDDMEELASYPLDQHLI 2137
Cdd:cd01450   144 DEEELREIASCPSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
1005-1172 5.76e-27

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 109.67  E-value: 5.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1005 DVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVS-KSGGFPR 1083
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRyLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1084 IDFALKKVSNMFNLHAGGRRnAGVPQTLVVITSGDPRY-DVADAVKTLKDLGICVLVLGIGDVYKEHLLPI--TGNSEKI 1160
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR-PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIasEPGEGHV 159

                          170
                   ....*....|..
gi 507116137  1161 ITFQDFDKLKNV 1172
Cdd:pfam00092  160 FTVSDFEALEDL 171
VWA pfam00092
von Willebrand factor type A domain;
1758-1918 2.89e-21

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 93.11  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1758 ELVFALDNSYDVTEESFNKTRDIITSIVNDLNIrennCPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQDt 1837
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLG- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1838 TEPRDVGNAMRFVTRNVFKRTY-AGANVRRVAVFFSNGQTASrSSIITATMEFSALDISPTVFAFDERVF--LEAFGFDN 1914
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAgARPGAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAVGVGNADDeeLRKIASEP 154


                   ....
gi 507116137  1915 TGTF 1918
Cdd:pfam00092  155 GEGH 158
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1394-1447 4.26e-13

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: 65.98  E-value: 4.26e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 507116137  1394 PGIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGA 1447
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 627-787 3.02e-54

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: 187.44  E-value: 3.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL 706
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  707 TGKALNFV-GQYFTHSKGARLGAKKFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEIS--GDSSLVFH 783
Cdd:cd01472    81 TGKALKYVrENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIAsdPKELYVFN 160


                  ....
gi 507116137  784 VENF 787
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
628-796 2.28e-50

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 176.70  E-value: 2.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   628 DIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL- 706
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   707 TGKALNFV-GQYFTHSKGARLGAKKFLILITDGVAQD-DVRDPARILRGKDVTIFSVGVYNANRSQLEEISGDSS--LVF 782
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegHVF 160

                          170
                   ....*....|....
gi 507116137   783 HVENFDHLKALERK 796
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1730 2.67e-48

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: 180.10  E-value: 2.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1478 HGFPGIKGE---KGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQnnniKGQKGSKGEQGRQGRSGQKGVQGSPSSRGSR 1554
Cdd:NF038329  113 LKGDGEKGEpgpAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE----RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1555 GREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGeKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGL 1634
Cdd:NF038329  189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1635 PGDLGPVGQTGQRGRQGDSGipgygqmgRKGVKGPRGFPGDAGQKGDignpgipggpgpkgfrglALTVGLKGEEGSRGL 1714
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAG--------KDGQNGKDGLPGKDGKDGQ------------------NGKDGLPGKDGKDGQ 321

                         250
                  ....*....|....*.
gi 507116137 1715 PGPPGQRGIKGMAGQP 1730
Cdd:NF038329  322 PGKDGLPGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1409-1680 3.58e-46

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: 173.94  E-value: 3.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1409 KGSQGLKGSrGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPkgghgddgidgldgeegchgfpgiKGEKG 1488
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE------------------------RGEKG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1489 DPGSQGSPGSRGAPGQYGEKGFPGDPgnpgqnnnikGQKGSKGEQGRQGRSGQKGVQGSPSSRGSRGREGQRGLRGVSGE 1568
Cdd:NF038329  163 PAGPQGEAGPQGPAGKDGEAGAKGPA----------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1569 pGNPGPTGTLGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLPGDLGPVGQTGQRG 1648
Cdd:NF038329  233 -GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                         250       260       270
                  ....*....|....*....|....*....|..
gi 507116137 1649 RQGDSGIPgyGQMGRKGVKGPrgfPGDAGQKG 1680
Cdd:NF038329  312 LPGKDGKD--GQPGKDGLPGK---DGKDGQPG 338
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 441-590 3.64e-46

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: 164.32  E-value: 3.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGTY 520
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  521 TGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIA 590
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIA 150
VWA pfam00092
von Willebrand factor type A domain;
442-608 8.19e-46

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.60  E-value: 8.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   442 DIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGT-Y 520
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   521 TGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTD-RVVEPAKRLRAEQITVHAVGIGAANKIELQEIAGK--EERVS 597
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgEGHVF 160

                          170
                   ....*....|.
gi 507116137   598 FGQNFDALKSI 608
Cdd:pfam00092  161 TVSDFEALEDL 171
VWA pfam00092
von Willebrand factor type A domain;
814-985 2.14e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 156.67  E-value: 2.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNTY 892
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   893 TAKALKHA-NALFTEEHGSRIkqNVKQMLIVITDGESHDHDqLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKNNT 971
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARP--GAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*.
gi 507116137   972 --IYVDNFDKLKDVFT 985
Cdd:pfam00092  158 hvFTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 628-788 5.06e-39

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: 144.13  E-value: 5.06e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    628 DIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEG-TL 706
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    707 TGKALNFVGQYFTH-SKGARLGAKKFLILITDGVAQD---DVRDPARILRGKDVTIFSVGVYNA-NRSQLEEISGDSSLV 781
Cdd:smart00327   81 LGAALQYALENLFSkSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160


                    ....*..
gi 507116137    782 FHVENFD 788
Cdd:smart00327  161 YVFLPEL 167
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 442-609 3.00e-38

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: 142.21  E-value: 3.00e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    442 DIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIK-QLTGGTY 520
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    521 TGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTD---RVVEPAKRLRAEQITVHAVGIG-AANKIELQEIAGKEERV 596
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                           170
                    ....*....|...
gi 507116137    597 SFGQNFDALKSIK 609
Cdd:smart00327  161 YVFLPELLDLLID 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 813-969 3.56e-38

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: 141.27  E-value: 3.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNT 891
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNlKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  892 YTAKALKHANALFTEEHGSRikQNVKQMLIVITDGESHDHDQLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKN 969
Cdd:cd01450    81 NTGKALQYALEQLFSESNAR--ENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 29-195 2.43e-37

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: 138.90  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLkKNFQFIGGSL 108
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAV-KNLRYIGGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  109 QIGKALQEAHRTYFSAPinGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATSHFHFN 188
Cdd:cd01472    80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                  ....*..
gi 507116137  189 LRTIRDL 195
Cdd:cd01472   158 VFNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 814-987 1.40e-36

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: 137.20  E-value: 1.40e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNTY 892
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    893 TAKALKHA-NALFTEEHGSRIkqNVKQMLIVITDGESHDHD-QLNDTALELRNKGITIFAVGVGKA-NQKELEGMAGNKN 969
Cdd:smart00327   81 LGAALQYAlENLFSKSAGSRR--GAPKVVILITDGESNDGPkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*...
gi 507116137    970 NTiYVDNFDKLKDVFTLV 987
Cdd:smart00327  159 GV-YVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2290-2467 2.97e-35

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: 132.80  E-value: 2.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2290 MDVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSPpgympnteecPVYLEFDLVTYNSIHQ 2369
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPD------KTRVGLVQYSD----------DVRVEFSLNDYKSKDD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2370 MKHHLQDSQQLNGD-VFIGHALQWTIDNVFVGTP-NLRKNKVIFVISAGetNSLDKDVLRNVSLRAKCQGYSIFVFSFGP 2447
Cdd:cd01450    65 LLKAVKNLKYLGGGgTNTGKALQYALEQLFSESNaRENVPKVIIVLTDG--RSDDGGDPKEAAAKLKDEGIKVFVVGVGP 142

                         170       180
                  ....*....|....*....|
gi 507116137 2448 kHNDKELEELASHPLDHHLV 2467
Cdd:cd01450   143 -ADEEELREIASCPSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
30-201 7.48e-35

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 132.40  E-value: 7.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    30 DVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSLQ 109
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   110 IGKALQEAHRTYFSAPINGRDRkqFPPILVVLASAESED-EVEEASKALQKDGVKIISVGVQKASEENLKAMATS----H 184
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgegH 158

                          170
                   ....*....|....*..
gi 507116137   185 FhFNLRTIRDLSTFSQN 201
Cdd:pfam00092  159 V-FTVSDFEALEDLQDQ 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1394-1574 1.03e-31

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: 131.18  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1394 PGIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPKGGHGDDgidgldg 1473
Cdd:NF038329  161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG------- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1474 EEGCHGFPGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQNNNI-----KGQKGSKGEQGRQGRSGQKGVQGSP 1548
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVgpagkDGQNGKDGLPGKDGKDGQNGKDGLP 313

                         170       180
                  ....*....|....*....|....*....
gi 507116137 1549 SSRGSRGREGQRGLR---GVSGEPGNPGP 1574
Cdd:NF038329  314 GKDGKDGQPGKDGLPgkdGKDGQPGKPAP 342
VWA pfam00092
von Willebrand factor type A domain;
236-404 3.22e-30

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.92  E-value: 3.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   236 DLVFLVDESLG-TGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQ-VGKSN 313
Cdd:pfam00092    1 DIVFLLDGSGSiGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   314 TGAAIDQMRRDGFSESYGSRRaqGVPQIAVLVTH-RPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPEQT 392
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDgRSQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|..
gi 507116137   393 ISTLKSYADLET 404
Cdd:pfam00092  159 VFTVSDFEALED 170
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1962-2137 6.46e-30

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 117.78  E-value: 6.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1962 MDVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLM 2041
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPD------KTRVGLVQYS---------DDVRVEFSLNDYKSKDDL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2042 KNHIQtSFQQLNGEAT-IGRALLWTTENLFPETPY-LRKHKVIFVVSAGENYERKEFVKmMALRAKCQGYVIFVISLGST 2119
Cdd:cd01450    66 LKAVK-NLKYLGGGGTnTGKALQYALEQLFSESNArENVPKVIIVLTDGRSDDGGDPKE-AAAKLKDEGIKVFVVGVGPA 143

                         170
                  ....*....|....*...
gi 507116137 2120 RKDDMEELASYPLDQHLI 2137
Cdd:cd01450   144 DEEELREIASCPSERHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 235-390 1.13e-29

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: 116.94  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVD--ESLGTGgNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKS 312
Cdd:cd01472     1 ADIVFLVDgsESIGLS-NFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  313 NTGAAIDQMRRDGFSESYGSRraQGVPQIAVLVTHRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPE 390
Cdd:cd01472    80 NTGKALKYVRENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKE 155
VWA pfam00092
von Willebrand factor type A domain;
2291-2485 2.84e-27

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 110.44  E-value: 2.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSppgympnTEecpVYLEFDLVTYNSIHQM 2370
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-------SD---VRTEFPLNDYSSKEEL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  2371 KHHLQD-SQQLNGDVFIGHALQWTIDNVFVGTPNLRKN--KVIFVISAGETNSLDkdvLRNVSLRAKCQGYSIFVFSFGp 2447
Cdd:pfam00092   65 LSAVDNlRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGD---PEEVARELKSAGVTVFAVGVG- 140

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 507116137  2448 KHNDKELEELASHPLDHHLVQLgrthkPDWNYIIKFVK 2485
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTV-----SDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1005-1172 5.76e-27

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 109.67  E-value: 5.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1005 DVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVS-KSGGFPR 1083
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRyLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1084 IDFALKKVSNMFNLHAGGRRnAGVPQTLVVITSGDPRY-DVADAVKTLKDLGICVLVLGIGDVYKEHLLPI--TGNSEKI 1160
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR-PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIasEPGEGHV 159

                          170
                   ....*....|..
gi 507116137  1161 ITFQDFDKLKNV 1172
Cdd:pfam00092  160 FTVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 30-199 8.08e-27

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: 109.08  E-value: 8.08e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137     30 DVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSLQ 109
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    110 IGKALQEAHRTYFSApiNGRDRKQFPPILVVLASAESED---EVEEASKALQKDGVKIISVGV-QKASEENLKAMATSH- 184
Cdd:smart00327   81 LGAALQYALENLFSK--SAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPg 158

                           170
                    ....*....|....*..
gi 507116137    185 --FHFNLRTIRDLSTFS 199
Cdd:smart00327  159 gvYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
1963-2135 8.64e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.51  E-value: 8.64e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS---------SDVRTEFPLNDYSSKEELL 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  2043 NHIQTSFQQLNGEATIGRALLWTTENLFPETPYLRKH--KVIFVVSAGENYERKefVKMMALRAKCQGYVIFVISLGSTR 2120
Cdd:pfam00092   66 SAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGD--PEEVARELKSAGVTVFAVGVGNAD 143

                          170
                   ....*....|....*
gi 507116137  2121 KDDMEELASYPLDQH 2135
Cdd:pfam00092  144 DEELRKIASEPGEGH 158
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2291-2459 1.55e-23

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: 99.84  E-value: 1.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSppgympnTEecpVYLEFDLVTYNSIHQM 2370
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPD------GDRVGLVTFS-------DD---ARVLFPLNDSRSKDAL 64

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   2371 KHHLQD-SQQLNGDVFIGHALQWTIDNVFVGTPNLRKN--KVIFVISAGETNSLDKDVLRnVSLRAKCQGYSIFVFSFGP 2447
Cdd:smart00327   65 LEALASlSYKLGGGTNLGAALQYALENLFSKSAGSRRGapKVVILITDGESNDGPKDLLK-AAKELKRSGVKVFVVGVGN 143

                           170
                    ....*....|..
gi 507116137   2448 KHNDKELEELAS 2459
Cdd:smart00327  144 DVDEEELKKLAS 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1005-1169 6.33e-23

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: 97.91  E-value: 6.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1005 DVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVS-KSGGFPR 1083
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1084 IDFALKKVSNMFNLHAGGRRnAGVPQTLVVITSG---DPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPI---TGNS 1157
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR-RGAPKVVILITDGesnDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKlasAPGG 159

                           170
                    ....*....|..
gi 507116137   1158 EKIITFQDFDKL 1169
Cdd:smart00327  160 VYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1004-1159 1.31e-22

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: 96.59  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFP- 1082
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGt 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507116137 1083 RIDFALKKVSNMFNLHAGGRRNagVPQTLVVITSG--DPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPITGNSEK 1159
Cdd:cd01450    81 NTGKALQYALEQLFSESNAREN--VPKVIIVLTDGrsDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
VWA pfam00092
von Willebrand factor type A domain;
1758-1918 2.89e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 93.11  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1758 ELVFALDNSYDVTEESFNKTRDIITSIVNDLNIrennCPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQDt 1837
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLG- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1838 TEPRDVGNAMRFVTRNVFKRTY-AGANVRRVAVFFSNGQTASrSSIITATMEFSALDISPTVFAFDERVF--LEAFGFDN 1914
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAgARPGAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAVGVGNADDeeLRKIASEP 154


                   ....
gi 507116137  1915 TGTF 1918
Cdd:pfam00092  155 GEGH 158
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1963-2129 8.16e-21

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: 92.13  E-value: 8.16e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNiasdplISDSGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD------IGPDGDRVGLVTFS---------DDARVLFPLNDSRSKDALL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   2043 NHIQTSFQQLNGEATIGRALLWTTENLFPETPYLRK--HKVIFVVSAGENYERKEFVKMMALRAKCQGYVIFVISLGS-T 2119
Cdd:smart00327   66 EALASLSYKLGGGTNLGAALQYALENLFSKSAGSRRgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNdV 145

                           170
                    ....*....|
gi 507116137   2120 RKDDMEELAS 2129
Cdd:smart00327  146 DEEELKKLAS 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 236-386 1.06e-20

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: 91.75  E-value: 1.06e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    236 DLVFLVDESLGTGG-NLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQ-VGKSN 313
Cdd:smart00327    1 DVVFLLDGSGSMGGnRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137    314 TGAAIDQMRRDGFSESYGSRRaqGVPQIAVLVT-HRPSDD--EVHDAALNLRLEDVNVFALSIQGANNT-QLEEIVS 386
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRR--GAPKVVILITdGESNDGpkDLLKAAKELKRSGVKVFVVGVGNDVDEeELKKLAS 155
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1395-1732 1.18e-19

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 96.56  E-value: 1.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1395 GIPGPHGTRGLQAMKGSQGLKGSRGHR---GEDGNPGVRGDTGPQGDKGIAGCPGAW---------GQKGLKGFSGPKGG 1462
Cdd:pfam03157  227 GQQGQQPGQGQQPGQGQQGQQPGQPQQlgqGQQGYYPISPQQPRQWQQSGQGQQGYYptslqqpgqGQSGYYPTSQQQAG 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1463 HGDDGIDGLDGEEGCHGFPGIKGEKGDPGSQGS-PGSRGAPGQYGEKGFPGDPGNPGQN-------NNIKGQKGSKGEQG 1534
Cdd:pfam03157  307 QLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQqPAQGQQPGQGQPGYYPTSPQQPGQGqpgyyptSQQQPQQGQQPEQG 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1535 RQGRSGQKGVQGSPSSRGSRGREGQRGLRGVS------GEPG----NPGPTGTLGAEGlQGPQGSQGNPGRKGEKGsQGQ 1604
Cdd:pfam03157  387 QQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSpqqsgqGQPGyyptSPQQSGQGQQPG-QGQQPGQEQPGQGQQPG-QGQ 464

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1605 KGPQGSPGLMGAKGSTGRPGLLgkKGEPGLPGDLGPVGQTGQRGrQGDSGI-------PGYGQMGRKGVKGPRgfPGDAG 1677
Cdd:pfam03157  465 QGQQPGQPEQGQQPGQGQPGYY--PTSPQQSGQGQQLGQWQQQG-QGQPGYyptsplqPGQGQPGYYPTSPQQ--PGQGQ 539

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  1678 QKGDIGNPGIPGGPGPKGFRGLALTVGLKGEEGSRGLPGP---PGQrGIKGMAGQPVY 1732
Cdd:pfam03157  540 QLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQgqqPGQ-GQQPGQGQPGY 596
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1759-1901 2.06e-19

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: 87.35  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1759 LVFALDNSYDVTEESFNKTRDIITSIVNDLNIRenncPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQDTT 1838
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507116137 1839 EPrDVGNAMRFVTRNVFKRTYAGANVRRVAVFFSNGQTASRSSIITATMEFSALDIspTVFAF 1901
Cdd:cd01450    79 GT-NTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGI--KVFVV 138
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1398-1621 1.73e-16

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 85.44  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1398 GPHGTRGLQAMKGSQGLKGSRGHRGEDGN--PGVRGdtgpqGDKGIAGCPGAWGQKGLKG-------FSGPKGGHGDDGI 1468
Cdd:cd21118   119 NSWQGSGGHGAYGSQGGPGVQGHGIPGGTggPWASG-----GNYGTNSLGGSVGQGGNGGplnygtnSQGAVAQPGYGTV 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1469 DGLDGEEGCHGFPGIKGEKG--DPGSQGSPGSRGAPGQYGEKGFP-----GDPGNPGQNNNIKGQKGSKGEQ--GRQGRS 1539
Cdd:cd21118   194 RGNNQNSGCTNPPPSGSHESfsNSGGSSSSGSSGSQGSHGSNGQGssgssGGQGNGGNNGSSSSNSGNSGGSngGSSGNS 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1540 GQKGVQGSPSSRGSRGREGQRGLRGVSG-----EPGNPGPTGtlGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLM 1614
Cdd:cd21118   274 GSGSGGSSSGGSNGWGGSSSSGGSGGSGggnkpECNNPGNDV--RMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTL 351


                  ....*..
gi 507116137 1615 GAKGSTG 1621
Cdd:cd21118   352 NSDASTL 358
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1759-1922 1.60e-15

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: 76.72  E-value: 1.60e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1759 LVFALDNSYDVTEESFNKTRDIITSIVNDLNIRenncPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYqDTT 1838
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIG----PDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSY-KLG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1839 EPRDVGNAMRFVTRNVFKRTYAG-ANVRRVAVFFSNGQ-TASRSSIITATMEFSALDISPTVFAFDERV---FLEAFGFD 1913
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSrRGAPKVVILITDGEsNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeeELKKLASA 156


                    ....*....
gi 507116137   1914 NTGTFQVIP 1922
Cdd:smart00327  157 PGGVYVFLP 165
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 813-985 7.38e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.83  E-value: 7.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGrDRvqFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGG-NT 891
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPG-DR--VSIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGGtAL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  892 YTA--KALKHANALFTEEHGSRIkqnvkqmlIVITDGE----SHDHDQLNDTALELRNKGITIFAVGVGKA-NQKELEGM 964
Cdd:COG2304   169 GAGleLAYELARKHFIPGRVNRV--------ILLTDGDanvgITDPEELLKLAEEAREEGITLTTLGVGSDyNEDLLERL 240

                         170       180
                  ....*....|....*....|..
gi 507116137  965 AGNKN-NTIYVDNFDKLKDVFT 985
Cdd:COG2304   241 ADAGGgNYYYIDDPEEAEKVFV 262
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 441-616 7.73e-15

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: 76.90  E-value: 7.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQ-FEQIKRFMLEVTEMFsigPDKVRVGVVQYSDDTEVefyITDYSNDID-LRKAIFNIkQLTGG 518
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEV---LLPLTRDREaLKRALDEL-PPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  519 TYTGKALDYILQIIKNGMKDRmSKVpcyLIVLTDGMSTDRVVEP---AKRLRAEQITVHAVGIGAANKIE--LQEIAgke 593
Cdd:COG1240   166 TPLGDALALALELLKRADPAR-RKV---IVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA--- 238

                         170       180
                  ....*....|....*....|....*
gi 507116137  594 eRVSFGQNFDA--LKSIKnEVVREI 616
Cdd:COG1240   239 -EATGGRYFRAddLSELA-AIYREI 261
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1394-1447 4.26e-13

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: 65.98  E-value: 4.26e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 507116137  1394 PGIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGA 1447
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 627-797 1.65e-12

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: 70.35  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNEN-FRKMKIFMKNLLTKIQigaDKTQIGVVQFSDKTKEEFQLNRyfTQQEISDAIDRMSlINEGT 705
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  706 LTGKALNFVGQYFthsKGARLGAKKFLILITDGVAQDDVRDP---ARILRGKDVTIFSVGVYNA--NRSQLEEISGDSS- 779
Cdd:COG1240   167 PLGDALALALELL---KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEavDEGLLREIAEATGg 243

                         170
                  ....*....|....*...
gi 507116137  780 LVFHVENFDHLKALERKL 797
Cdd:COG1240   244 RYFRADDLSELAAIYREI 261
PHA03169 PHA03169
hypothetical protein; Provisional
 1476-1680 1.80e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 56.13  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1476 GCHGfpgikGEKGDPGSQGSPGSRGAPGQygekgfPGDPGNPGQnnnikgQKGSKGEQGrQGRSGQKGVQGSPSSRGSRG 1555
Cdd:PHA03169   24 KRHG-----GTREQAGRRRGTAARAAKPA------PPAPTTSGP------QVRAVAEQG-HRQTESDTETAEESRHGEKE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1556 REGQrglrgvsgepgnPGPTGTlGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLP 1635
Cdd:PHA03169   86 ERGQ------------GGPSGS-GSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPP 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 507116137 1636 GDLGPVGqtgqrGRQGDSGIPGYGQMGRKGVKGPRGFPGDAGQKG 1680
Cdd:PHA03169  153 ESHNPSP-----NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGP 192
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 982-1143 9.46e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 51.12  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  982 DVFTLVQERMCTE---APEVCHlQEADVIFLCDGSDRVSNSDFVT-MTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSII 1057
Cdd:PTZ00441   19 SIFARGDNKIVDEvkyREEVCN-EEVDLYLLVDGSGSIGYHNWIThVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1058 ELKN--SLTKTQWKTQIQNVSKSG---GFPRIDFALKKVSNMFNLHAGgRRNAGvpQTLVVITSGDP--RYDVADAVKTL 1130
Cdd:PTZ00441   98 RLGSgaSKDKEQALIIVKSLRKTYlpyGKTNMTDALLEVRKHLNDRVN-RENAI--QLVILMTDGIPnsKYRALEESRKL 174

                         170
                  ....*....|...
gi 507116137 1131 KDLGICVLVLGIG 1143
Cdd:PTZ00441  175 KDRNVKLAVIGIG 187
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1946-2128 3.20e-05

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: 48.01  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1946 FPNACIREAFLPEDSYMDVVFLIDNSRN-IAKDEFKAVKALVSSVIDNFniasdplisDSGDRIALLSYSpwessrrkmG 2024
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---------RPRDRVGLVAFG---------G 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2025 TVKTEFDFiTYDNQLLMK--NHIQTsfqqlnGEAT-IGRALLwTTENLFPETPYlRKHKVIFVVSAGENYERKEFVKMMA 2101
Cdd:COG1240   139 EAEVLLPL-TRDREALKRalDELPP------GGGTpLGDALA-LALELLKRADP-ARRKVIVLLTDGRDNAGRIDPLEAA 209

                         170       180
                  ....*....|....*....|....*....
gi 507116137 2102 LRAKCQGYVIFVISLGSTRKDD--MEELA 2128
Cdd:COG1240   210 ELAAAAGIRIYTIGVGTEAVDEglLREIA 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 16-205 1.94e-03

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: 42.62  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   16 TLADQSPGPGPVYADVVFLVDSSDH-LGPKSFPFVKTFINKMINSLPIEAnkyRVALAQYSDEfhSE------FHLSTFK 88
Cdd:COG1240    80 ALAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGE--AEvllpltRDREALK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   89 GRspmLNHLKknfqfIGGSLQIGKALQEAHRTYFSAPINGRdrkqfpPILVVL---ASAESEDEVEEASKALQKDGVKI- 164
Cdd:COG1240   155 RA---LDELP-----PGGGTPLGDALALALELLKRADPARR------KVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIy 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 507116137  165 -ISVGVQKASEENLKAMAT----SHFHfnlrtIRDLSTFSQNMTQI 205
Cdd:COG1240   221 tIGVGTEAVDEGLLREIAEatggRYFR-----ADDLSELAAIYREI 261
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 627-787 3.02e-54

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: 187.44  E-value: 3.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL 706
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  707 TGKALNFV-GQYFTHSKGARLGAKKFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEIS--GDSSLVFH 783
Cdd:cd01472    81 TGKALKYVrENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIAsdPKELYVFN 160


                  ....
gi 507116137  784 VENF 787
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
628-796 2.28e-50

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 176.70  E-value: 2.28e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   628 DIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL- 706
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   707 TGKALNFV-GQYFTHSKGARLGAKKFLILITDGVAQD-DVRDPARILRGKDVTIFSVGVYNANRSQLEEISGDSS--LVF 782
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegHVF 160

                          170
                   ....*....|....
gi 507116137   783 HVENFDHLKALERK 796
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 627-787 1.17e-49

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: 174.40  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL 706
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  707 TGKALNFV-GQYFTHSKGARLGAKKFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEISGDSSL--VFH 783
Cdd:cd01482    81 TGKALTHVrEKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthVFN 160


                  ....
gi 507116137  784 VENF 787
Cdd:cd01482   161 VADF 164
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1730 2.67e-48

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: 180.10  E-value: 2.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1478 HGFPGIKGE---KGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQnnniKGQKGSKGEQGRQGRSGQKGVQGSPSSRGSR 1554
Cdd:NF038329  113 LKGDGEKGEpgpAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE----RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1555 GREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGeKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGL 1634
Cdd:NF038329  189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1635 PGDLGPVGQTGQRGRQGDSGipgygqmgRKGVKGPRGFPGDAGQKGDignpgipggpgpkgfrglALTVGLKGEEGSRGL 1714
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAG--------KDGQNGKDGLPGKDGKDGQ------------------NGKDGLPGKDGKDGQ 321

                         250
                  ....*....|....*.
gi 507116137 1715 PGPPGQRGIKGMAGQP 1730
Cdd:NF038329  322 PGKDGLPGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1409-1680 3.58e-46

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: 173.94  E-value: 3.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1409 KGSQGLKGSrGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPkgghgddgidgldgeegchgfpgiKGEKG 1488
Cdd:NF038329  108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE------------------------RGEKG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1489 DPGSQGSPGSRGAPGQYGEKGFPGDPgnpgqnnnikGQKGSKGEQGRQGRSGQKGVQGSPSSRGSRGREGQRGLRGVSGE 1568
Cdd:NF038329  163 PAGPQGEAGPQGPAGKDGEAGAKGPA----------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1569 pGNPGPTGTLGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLPGDLGPVGQTGQRG 1648
Cdd:NF038329  233 -GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                         250       260       270
                  ....*....|....*....|....*....|..
gi 507116137 1649 RQGDSGIPgyGQMGRKGVKGPrgfPGDAGQKG 1680
Cdd:NF038329  312 LPGKDGKD--GQPGKDGLPGK---DGKDGQPG 338
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 441-590 3.64e-46

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: 164.32  E-value: 3.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGTY 520
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  521 TGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIA 590
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIA 150
VWA pfam00092
von Willebrand factor type A domain;
442-608 8.19e-46

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.60  E-value: 8.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   442 DIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGT-Y 520
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   521 TGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTD-RVVEPAKRLRAEQITVHAVGIGAANKIELQEIAGK--EERVS 597
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgEGHVF 160

                          170
                   ....*....|.
gi 507116137   598 FGQNFDALKSI 608
Cdd:pfam00092  161 TVSDFEALEDL 171
VWA pfam00092
von Willebrand factor type A domain;
814-985 2.14e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 156.67  E-value: 2.14e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNTY 892
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   893 TAKALKHA-NALFTEEHGSRIkqNVKQMLIVITDGESHDHDqLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKNNT 971
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARP--GAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*.
gi 507116137   972 --IYVDNFDKLKDVFT 985
Cdd:pfam00092  158 hvFTVSDFEALEDLQD 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 627-779 2.38e-43

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: 155.91  E-value: 2.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLIN-EGT 705
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGgGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507116137  706 LTGKALNFVGQYFTHSKGARLGAKKFLILITDGVAQD--DVRDPARILRGKDVTIFSVGVYNANRSQLEEISGDSS 779
Cdd:cd01450    81 NTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 441-598 1.20e-42

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: 153.99  E-value: 1.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTG-GT 519
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  520 YTGKALDYILQIIKNGMKDRmSKVPCYLIVLTDGMSTDR--VVEPAKRLRAEQITVHAVGIGAANKIELQEIAGK-EERV 596
Cdd:cd01450    81 NTGKALQYALEQLFSESNAR-ENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCpSERH 159


                  ..
gi 507116137  597 SF 598
Cdd:cd01450   160 VF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 441-592 4.71e-40

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: 146.66  E-value: 4.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGTY 520
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507116137  521 TGKALDYILQII---KNGMKDRMSKVpcyLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIAGK 592
Cdd:cd01482    81 TGKALTHVREKNftpDAGARPGVPKV---VILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASK 152
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 627-787 6.84e-40

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: 146.31  E-value: 6.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL 706
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  707 -TGKALNFVGQ-YFTHSKGARL--GAKKFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEISGDSSLVF 782
Cdd:cd01481    81 nTGSALDYVVKnLFTKSAGSRIeeGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 507116137  783 HVENF 787
Cdd:cd01481   161 QVSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 628-788 5.06e-39

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: 144.13  E-value: 5.06e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    628 DIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEG-TL 706
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    707 TGKALNFVGQYFTH-SKGARLGAKKFLILITDGVAQD---DVRDPARILRGKDVTIFSVGVYNA-NRSQLEEISGDSSLV 781
Cdd:smart00327   81 LGAALQYALENLFSkSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160


                    ....*..
gi 507116137    782 FHVENFD 788
Cdd:smart00327  161 YVFLPEL 167
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 442-609 3.00e-38

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: 142.21  E-value: 3.00e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    442 DIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIK-QLTGGTY 520
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    521 TGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTD---RVVEPAKRLRAEQITVHAVGIG-AANKIELQEIAGKEERV 596
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                           170
                    ....*....|...
gi 507116137    597 SFGQNFDALKSIK 609
Cdd:smart00327  161 YVFLPELLDLLID 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 813-969 3.56e-38

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: 141.27  E-value: 3.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNT 891
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNlKYLGGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  892 YTAKALKHANALFTEEHGSRikQNVKQMLIVITDGESHDHDQLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKN 969
Cdd:cd01450    81 NTGKALQYALEQLFSESNAR--ENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 29-195 2.43e-37

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: 138.90  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLkKNFQFIGGSL 108
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAV-KNLRYIGGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  109 QIGKALQEAHRTYFSAPinGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATSHFHFN 188
Cdd:cd01472    80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY 157


                  ....*..
gi 507116137  189 LRTIRDL 195
Cdd:cd01472   158 VFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 627-812 7.84e-37

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: 139.83  E-value: 7.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTL 706
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  707 TGKALNF-VGQYFTHSKGARLGAK---KFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEISGD--SSL 780
Cdd:cd01475    83 TGLAIQYaMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEplADH 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 507116137  781 VFHVENFDHLKALERKLIFRVCAL--------HDCKRITL 812
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKICVVpdlcatlsHVCQQVCI 202
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 814-987 1.40e-36

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: 137.20  E-value: 1.40e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNTY 892
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    893 TAKALKHA-NALFTEEHGSRIkqNVKQMLIVITDGESHDHD-QLNDTALELRNKGITIFAVGVGKA-NQKELEGMAGNKN 969
Cdd:smart00327   81 LGAALQYAlENLFSKSAGSRR--GAPKVVILITDGESNDGPkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*...
gi 507116137    970 NTiYVDNFDKLKDVFTLV 987
Cdd:smart00327  159 GV-YVFLPELLDLLIDLL 175
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 814-978 2.45e-36

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: 136.20  E-value: 2.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGGNTYT 893
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  894 AKALKHA-NALFTEEhgSRIKQNVKQMLIVITDGEShdHDQLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKNNTi 972
Cdd:cd01472    82 GKALKYVrENLFTEA--SGSREGVPKVLVVITDGKS--QDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKEL- 156


                  ....*.
gi 507116137  973 YVDNFD 978
Cdd:cd01472   157 YVFNVA 162
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2290-2467 2.97e-35

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: 132.80  E-value: 2.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2290 MDVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSPpgympnteecPVYLEFDLVTYNSIHQ 2369
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPD------KTRVGLVQYSD----------DVRVEFSLNDYKSKDD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2370 MKHHLQDSQQLNGD-VFIGHALQWTIDNVFVGTP-NLRKNKVIFVISAGetNSLDKDVLRNVSLRAKCQGYSIFVFSFGP 2447
Cdd:cd01450    65 LLKAVKNLKYLGGGgTNTGKALQYALEQLFSESNaRENVPKVIIVLTDG--RSDDGGDPKEAAAKLKDEGIKVFVVGVGP 142

                         170       180
                  ....*....|....*....|
gi 507116137 2448 kHNDKELEELASHPLDHHLV 2467
Cdd:cd01450   143 -ADEEELREIASCPSERHVF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 29-183 3.48e-35

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: 132.83  E-value: 3.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKnFQFIGGS- 107
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRR-LRLRGGSq 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507116137  108 LQIGKALQEAHRTYFSAPINGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATS 183
Cdd:cd01481    80 LNTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFD 155
VWA pfam00092
von Willebrand factor type A domain;
30-201 7.48e-35

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 132.40  E-value: 7.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    30 DVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSLQ 109
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   110 IGKALQEAHRTYFSAPINGRDRkqFPPILVVLASAESED-EVEEASKALQKDGVKIISVGVQKASEENLKAMATS----H 184
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEpgegH 158

                          170
                   ....*....|....*..
gi 507116137   185 FhFNLRTIRDLSTFSQN 201
Cdd:pfam00092  159 V-FTVSDFEALEDLQDQ 174
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 439-620 1.74e-34

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: 132.89  E-value: 1.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  439 KEADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGG 518
Cdd:cd01475     1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  519 TYTGKALDYILQI---IKNGMKDRMSKVPCYLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIAGK--E 593
Cdd:cd01475    81 TMTGLAIQYAMNNafsEAEGARPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEplA 160

                         170       180
                  ....*....|....*....|....*..
gi 507116137  594 ERVSFGQNFDALKSIKNEVVREICAEK 620
Cdd:cd01475   161 DHVFYVEDFSTIEELTKKFQGKICVVP 187
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 814-978 7.10e-32

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: 123.17  E-value: 7.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGGNTYT 893
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  894 AKALKH-ANALFTEEHGSRikQNVKQMLIVITDGEShdHDQLNDTALELRNKGITIFAVGVGKANQKELEGMAGnKNNTI 972
Cdd:cd01482    82 GKALTHvREKNFTPDAGAR--PGVPKVVILITDGKS--QDDVELPARVLRNLGVNVFAVGVKDADESELKMIAS-KPSET 156


                  ....*.
gi 507116137  973 YVDNFD 978
Cdd:cd01482   157 HVFNVA 162
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1394-1574 1.03e-31

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: 131.18  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1394 PGIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPKGGHGDDgidgldg 1473
Cdd:NF038329  161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG------- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1474 EEGCHGFPGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQNNNI-----KGQKGSKGEQGRQGRSGQKGVQGSP 1548
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVgpagkDGQNGKDGLPGKDGKDGQNGKDGLP 313

                         170       180
                  ....*....|....*....|....*....
gi 507116137 1549 SSRGSRGREGQRGLR---GVSGEPGNPGP 1574
Cdd:NF038329  314 GKDGKDGQPGKDGLPgkdGKDGQPGKPAP 342
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 29-189 5.36e-31

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: 120.85  E-value: 5.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLkKNFQFIGGSL 108
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAI-KNLPYKGGNT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  109 QIGKALQEAHRTYFSApiNGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATS----H 184
Cdd:cd01482    80 RTGKALTHVREKNFTP--DAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKpsetH 157


                  ....*
gi 507116137  185 FHFNL 189
Cdd:cd01482   158 VFNVA 162
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 627-778 2.64e-30

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 118.82  E-value: 2.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEG-T 705
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGgT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137  706 LTGKALNFVGQYFthSKGARLGAKKFLILITDGVAQDDVRDP---ARILRGKDVTIFSVGV-YNANRSQLEEISGDS 778
Cdd:cd00198    81 NIGAALRLALELL--KSAKRPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIgDDANEDELKEIADKT 155
VWA pfam00092
von Willebrand factor type A domain;
236-404 3.22e-30

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.92  E-value: 3.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   236 DLVFLVDESLG-TGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQ-VGKSN 313
Cdd:pfam00092    1 DIVFLLDGSGSiGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   314 TGAAIDQMRRDGFSESYGSRRaqGVPQIAVLVTH-RPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPEQT 392
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDgRSQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|..
gi 507116137   393 ISTLKSYADLET 404
Cdd:pfam00092  159 VFTVSDFEALED 170
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 441-598 5.04e-30

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 118.05  E-value: 5.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIK-QLTGGT 519
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  520 YTGKALDYILQIIKNGMKDRMSKVpcyLIVLTDGMSTD---RVVEPAKRLRAEQITVHAVGIG-AANKIELQEIAGKEER 595
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNARRV---IILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGdDANEDELKEIADKTTG 157


                  ...
gi 507116137  596 VSF 598
Cdd:cd00198   158 GAV 160
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1962-2137 6.46e-30

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 117.78  E-value: 6.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1962 MDVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLM 2041
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPD------KTRVGLVQYS---------DDVRVEFSLNDYKSKDDL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2042 KNHIQtSFQQLNGEAT-IGRALLWTTENLFPETPY-LRKHKVIFVVSAGENYERKEFVKmMALRAKCQGYVIFVISLGST 2119
Cdd:cd01450    66 LKAVK-NLKYLGGGGTnTGKALQYALEQLFSESNArENVPKVIIVLTDGRSDDGGDPKE-AAAKLKDEGIKVFVVGVGPA 143

                         170
                  ....*....|....*...
gi 507116137 2120 RKDDMEELASYPLDQHLI 2137
Cdd:cd01450   144 DEEELREIASCPSERHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 235-390 1.13e-29

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: 116.94  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVD--ESLGTGgNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKS 312
Cdd:cd01472     1 ADIVFLVDgsESIGLS-NFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  313 NTGAAIDQMRRDGFSESYGSRraQGVPQIAVLVTHRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPE 390
Cdd:cd01472    80 NTGKALKYVRENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKE 155
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 814-977 1.60e-29

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: 116.65  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  814 DVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGGN-TY 892
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSqLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  893 TAKALKH-ANALFTEEHGSRIKQNVKQMLIVITDGEShdHDQLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKNNT 971
Cdd:cd01481    82 TGSALDYvVKNLFTKSAGSRIEEGVPQFLVLITGGKS--QDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFV 159


                  ....*.
gi 507116137  972 IYVDNF 977
Cdd:cd01481   160 FQVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 441-590 1.67e-29

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: 116.65  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTG-GT 519
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507116137  520 YTGKALDYILQ-IIKNGMKDRMSK-VPCYLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIA 590
Cdd:cd01481    81 NTGSALDYVVKnLFTKSAGSRIEEgVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIA 153
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 628-793 2.23e-29

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: 116.69  E-value: 2.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  628 DIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTLT 707
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  708 GKALNFVGQY-FTHSKGARLGAKKFLILITDGVAQDDVRDPARILRGK--DVTIFSVGVYNA--NRSQLEEISG-----D 777
Cdd:cd01469    82 ATAIQYVVTElFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEreGIIRYAIGVGGHfqRENSREELKTiaskpP 161

                         170
                  ....*....|....*.
gi 507116137  778 SSLVFHVENFDHLKAL 793
Cdd:cd01469   162 EEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 813-974 3.36e-29

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 115.74  E-value: 3.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRK-RRDTGGNT 891
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAlKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  892 YTAKALKHANALFTEEHGSrikqNVKQMLIVITDGESHDHDQ-LNDTALELRNKGITIFAVGVG-KANQKELEGMAGNKN 969
Cdd:cd00198    81 NIGAALRLALELLKSAKRP----NARRVIILLTDGEPNDGPElLAEAARELRKLGITVYTIGIGdDANEDELKEIADKTT 156


                  ....*
gi 507116137  970 NTIYV 974
Cdd:cd00198   157 GGAVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 29-184 2.10e-28

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 113.16  E-value: 2.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLkKNFQFIGGSL 108
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAV-KNLKYLGGGG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507116137  109 Q-IGKALQEAHRTYFSApinGRDRKQFPPILVVLASAESED--EVEEASKALQKDGVKIISVGVQKASEENLKAMATSH 184
Cdd:cd01450    80 TnTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 813-983 2.86e-28

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: 113.60  E-value: 2.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGGNTY 892
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  893 TAKALKHA-NALFTEEHGSRikQNVKQMLIVITDGESHDHDQLNDTALELRNKGITIFAVGVGKANQ-----KELEGMAG 966
Cdd:cd01469    81 TATAIQYVvTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQrensrEELKTIAS 158

                         170
                  ....*....|....*....
gi 507116137  967 N--KNNTIYVDNFDKLKDV 983
Cdd:cd01469   159 KppEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 235-390 7.82e-28

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: 111.65  E-value: 7.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVDESLGTG-GNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKS- 312
Cdd:cd01481     1 KDIVFLIDGSDNVGsGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQl 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  313 NTGAAIDQMRRDGFSESYGSRRAQGVPQIAVLVTHRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIvSYPPE 390
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQI-AFDPS 157
VWA pfam00092
von Willebrand factor type A domain;
2291-2485 2.84e-27

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 110.44  E-value: 2.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSppgympnTEecpVYLEFDLVTYNSIHQM 2370
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-------SD---VRTEFPLNDYSSKEEL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  2371 KHHLQD-SQQLNGDVFIGHALQWTIDNVFVGTPNLRKN--KVIFVISAGETNSLDkdvLRNVSLRAKCQGYSIFVFSFGp 2447
Cdd:pfam00092   65 LSAVDNlRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGD---PEEVARELKSAGVTVFAVGVG- 140

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 507116137  2448 KHNDKELEELASHPLDHHLVQLgrthkPDWNYIIKFVK 2485
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTV-----SDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1005-1172 5.76e-27

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 109.67  E-value: 5.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1005 DVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVS-KSGGFPR 1083
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRyLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1084 IDFALKKVSNMFNLHAGGRRnAGVPQTLVVITSGDPRY-DVADAVKTLKDLGICVLVLGIGDVYKEHLLPI--TGNSEKI 1160
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR-PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIasEPGEGHV 159

                          170
                   ....*....|..
gi 507116137  1161 ITFQDFDKLKNV 1172
Cdd:pfam00092  160 FTVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 30-199 8.08e-27

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: 109.08  E-value: 8.08e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137     30 DVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSLQ 109
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    110 IGKALQEAHRTYFSApiNGRDRKQFPPILVVLASAESED---EVEEASKALQKDGVKIISVGV-QKASEENLKAMATSH- 184
Cdd:smart00327   81 LGAALQYALENLFSK--SAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPg 158

                           170
                    ....*....|....*..
gi 507116137    185 --FHFNLRTIRDLSTFS 199
Cdd:smart00327  159 gvYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 235-391 1.65e-26

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: 107.76  E-value: 1.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVDESLGTG-GNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGK-S 312
Cdd:cd01450     1 LDIVFLLDGSESVGpENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  313 NTGAAIDQMRRDGFSEsygSRRAQGVPQIAVLVT--HRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPE 390
Cdd:cd01450    81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTdgRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157


                  .
gi 507116137  391 Q 391
Cdd:cd01450   158 R 158
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 235-393 1.79e-26

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: 107.76  E-value: 1.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVDESLGTG-GNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKSN 313
Cdd:cd01482     1 ADIVFLVDGSWSIGrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  314 TGAAIDQMRRDGFSESYGSRRaqGVPQIAVLVTHRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPEQTI 393
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 442-608 3.66e-25

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: 104.75  E-value: 3.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  442 DIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGTYT 521
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  522 GKALDYILQ---IIKNGMKDRMSKVpcyLIVLTDGMSTD-----RVVEPAKRlraEQITVHAVGIGAANKI-----ELQE 588
Cdd:cd01469    82 ATAIQYVVTelfSESNGARKDATKV---LVVITDGESHDdpllkDVIPQAER---EGIIRYAIGVGGHFQRensreELKT 155

                         170       180
                  ....*....|....*....|..
gi 507116137  589 IAGK--EERVSFGQNFDALKSI 608
Cdd:cd01469   156 IASKppEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
1963-2135 8.64e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 103.51  E-value: 8.64e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS---------SDVRTEFPLNDYSSKEELL 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  2043 NHIQTSFQQLNGEATIGRALLWTTENLFPETPYLRKH--KVIFVVSAGENYERKefVKMMALRAKCQGYVIFVISLGSTR 2120
Cdd:pfam00092   66 SAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGD--PEEVARELKSAGVTVFAVGVGNAD 143

                          170
                   ....*....|....*
gi 507116137  2121 KDDMEELASYPLDQH 2135
Cdd:pfam00092  144 DEELRKIASEPGEGH 158
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 29-182 4.00e-24

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: 103.23  E-value: 4.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLkKNFQFIGGSL 108
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAV-RRMEYLETGT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507116137  109 QIGKALQEAHRTYFSAPINGRDRKQFPP-ILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMAT 182
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSERVPrVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIAS 156
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 441-611 5.37e-24

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: 101.69  E-value: 5.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFS------IGPDKVRVGVVQYSDDTEVEFYITDYSNDID-LRKAIFNIK 513
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTsLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  514 QLTGGTYTGKALDYILQIIkngMKDRMSKVPCYLIVLTDGMST-------DRVVEPAKRLraeQITVHAVGIGAANKIEL 586
Cdd:cd01480    83 YIGGGTFTDCALKYATEQL---LEGSHQKENKFLLVITDGHSDgspdggiEKAVNEADHL---GIKIFFVAVGSQNEEPL 156

                         170       180
                  ....*....|....*....|....*....
gi 507116137  587 QEIA--GKEE--RVSFGQnFDALKSIKNE 611
Cdd:cd01480   157 SRIAcdGKSAlyRENFAE-LLWSFFIDDE 184
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 627-782 1.48e-23

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: 99.40  E-value: 1.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNEnFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKE--EFQLNRYFTQQEISDAIDRMSLINEG 704
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  705 TLTGKALNFVGQYFTHSKGARLGAKKFLILITDGVAQDDVRDPARILR-GKDVTIFSVGVY---NANRSQLEEISGDSSL 780
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGdpgTVDTEELHSITGNEDH 159


                  ..
gi 507116137  781 VF 782
Cdd:cd01476   160 IF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2291-2459 1.55e-23

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: 99.84  E-value: 1.55e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSppgympnTEecpVYLEFDLVTYNSIHQM 2370
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPD------GDRVGLVTFS-------DD---ARVLFPLNDSRSKDAL 64

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   2371 KHHLQD-SQQLNGDVFIGHALQWTIDNVFVGTPNLRKN--KVIFVISAGETNSLDKDVLRnVSLRAKCQGYSIFVFSFGP 2447
Cdd:smart00327   65 LEALASlSYKLGGGTNLGAALQYALENLFSKSAGSRRGapKVVILITDGESNDGPKDLLK-AAKELKRSGVKVFVVGVGN 143

                           170
                    ....*....|..
gi 507116137   2448 KHNDKELEELAS 2459
Cdd:smart00327  144 DVDEEELKKLAS 155
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 813-999 2.49e-23

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: 100.92  E-value: 2.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGGNTY 892
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  893 TAKALKHA-NALFTEEHGSR-IKQNVKQMLIVITDGESHDHdqLNDTALELRNKGITIFAVGVGKANQKELEGMAGN--K 968
Cdd:cd01475    83 TGLAIQYAmNNAFSEAEGARpGSERVPRVGIVVTDGRPQDD--VSEVAAKARALGIEMFAVGVGRADEEELREIASEplA 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 507116137  969 NNTIYVDNFDKLKDVFTLVQERMCtEAPEVC 999
Cdd:cd01475   161 DHVFYVEDFSTIEELTKKFQGKIC-VVPDLC 190
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 627-787 2.90e-23

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: 99.38  E-value: 2.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIFMKNLL------TKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQ-QEISDAIDRMS 699
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAerflkdYYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNyTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  700 LINEGTLTGKALNFV-GQYFTHSkgaRLGAKKFLILITDGvaQDDVRDPARILRGKD------VTIFSVGVYNANRSQLE 772
Cdd:cd01480    83 YIGGGTFTDCALKYAtEQLLEGS---HQKENKFLLVITDG--HSDGSPDGGIEKAVNeadhlgIKIFFVAVGSQNEEPLS 157

                         170
                  ....*....|....*
gi 507116137  773 EISGDSSLVFHVENF 787
Cdd:cd01480   158 RIACDGKSALYRENF 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1005-1169 6.33e-23

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: 97.91  E-value: 6.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1005 DVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVS-KSGGFPR 1083
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1084 IDFALKKVSNMFNLHAGGRRnAGVPQTLVVITSG---DPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPI---TGNS 1157
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR-RGAPKVVILITDGesnDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKlasAPGG 159

                           170
                    ....*....|..
gi 507116137   1158 EKIITFQDFDKL 1169
Cdd:smart00327  160 VYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1004-1159 1.31e-22

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: 96.59  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFP- 1082
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGt 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507116137 1083 RIDFALKKVSNMFNLHAGGRRNagVPQTLVVITSG--DPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPITGNSEK 1159
Cdd:cd01450    81 NTGKALQYALEQLFSESNAREN--VPKVIIVLTDGrsDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 813-971 3.73e-22

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 95.54  E-value: 3.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHmINLTIHLVKKADVGRDRVQFGALKYS--DQPNILFYLNTYSNRSAIIENLRKRRDTGGN 890
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKY-KKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  891 TYTAKALKHANALFTEEHGSRikQNVKQMLIVITDGESHDHDQlnDTALELR-NKGITIFAVGVG---KANQKELEGMAG 966
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPE--KQARILRaVPNIETFAVGTGdpgTVDTEELHSITG 155


                  ....*
gi 507116137  967 NKNNT 971
Cdd:cd01476   156 NEDHI 160
VWA pfam00092
von Willebrand factor type A domain;
1758-1918 2.89e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 93.11  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1758 ELVFALDNSYDVTEESFNKTRDIITSIVNDLNIrennCPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQDt 1837
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLG- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1838 TEPRDVGNAMRFVTRNVFKRTY-AGANVRRVAVFFSNGQTASrSSIITATMEFSALDISPTVFAFDERVF--LEAFGFDN 1914
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAgARPGAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAVGVGNADDeeLRKIASEP 154


                   ....
gi 507116137  1915 TGTF 1918
Cdd:pfam00092  155 GEGH 158
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1963-2129 8.16e-21

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: 92.13  E-value: 8.16e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNiasdplISDSGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD------IGPDGDRVGLVTFS---------DDARVLFPLNDSRSKDALL 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   2043 NHIQTSFQQLNGEATIGRALLWTTENLFPETPYLRK--HKVIFVVSAGENYERKEFVKMMALRAKCQGYVIFVISLGS-T 2119
Cdd:smart00327   66 EALASLSYKLGGGTNLGAALQYALENLFSKSAGSRRgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNdV 145

                           170
                    ....*....|
gi 507116137   2120 RKDDMEELAS 2129
Cdd:smart00327  146 DEEELKKLAS 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 236-386 1.06e-20

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: 91.75  E-value: 1.06e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137    236 DLVFLVDESLGTGG-NLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQ-VGKSN 313
Cdd:smart00327    1 DVVFLLDGSGSMGGnRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137    314 TGAAIDQMRRDGFSESYGSRRaqGVPQIAVLVT-HRPSDD--EVHDAALNLRLEDVNVFALSIQGANNT-QLEEIVS 386
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRR--GAPKVVILITdGESNDGpkDLLKAAKELKRSGVKVFVVGVGNDVDEeELKKLAS 155
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 235-413 1.13e-20

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: 93.22  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVDESLGTG-GNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKSN 313
Cdd:cd01475     3 TDLVFLIDSSRSVRpENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  314 TGAAIDQMRRDGFSESYGSR-RAQGVPQIAVLVTHRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPEQT 392
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|.
gi 507116137  393 ISTLKSYADLETYSTKFLKKL 413
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKI 183
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1004-1166 1.83e-20

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: 90.75  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFPR 1083
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1084 IDFALKKVSNmFNLHAGGRRNAGVPQTLVVITSGDPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPI--TGNSEKII 1161
Cdd:cd01472    81 TGKALKYVRE-NLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIasDPKELYVF 159


                  ....*
gi 507116137 1162 TFQDF 1166
Cdd:cd01472   160 NVADF 164
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 441-599 2.42e-20

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: 90.15  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKqFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDD--TEVEFYITDYSNDIDLRKAIFNIKQLTGG 518
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRgrQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  519 TYTGKALDYILQIIKNGMKDRmSKVPCYLIVLTDGMSTDRVVEPAKRLRAE-QITVHAVGIG---AANKIELQEIAGKEE 594
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRR-EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGNED 158


                  ....*
gi 507116137  595 RVSFG 599
Cdd:cd01476   159 HIFTD 163
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1395-1732 1.18e-19

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 96.56  E-value: 1.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1395 GIPGPHGTRGLQAMKGSQGLKGSRGHR---GEDGNPGVRGDTGPQGDKGIAGCPGAW---------GQKGLKGFSGPKGG 1462
Cdd:pfam03157  227 GQQGQQPGQGQQPGQGQQGQQPGQPQQlgqGQQGYYPISPQQPRQWQQSGQGQQGYYptslqqpgqGQSGYYPTSQQQAG 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1463 HGDDGIDGLDGEEGCHGFPGIKGEKGDPGSQGS-PGSRGAPGQYGEKGFPGDPGNPGQN-------NNIKGQKGSKGEQG 1534
Cdd:pfam03157  307 QLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQqPAQGQQPGQGQPGYYPTSPQQPGQGqpgyyptSQQQPQQGQQPEQG 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1535 RQGRSGQKGVQGSPSSRGSRGREGQRGLRGVS------GEPG----NPGPTGTLGAEGlQGPQGSQGNPGRKGEKGsQGQ 1604
Cdd:pfam03157  387 QQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTSpqqsgqGQPGyyptSPQQSGQGQQPG-QGQQPGQEQPGQGQQPG-QGQ 464

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1605 KGPQGSPGLMGAKGSTGRPGLLgkKGEPGLPGDLGPVGQTGQRGrQGDSGI-------PGYGQMGRKGVKGPRgfPGDAG 1677
Cdd:pfam03157  465 QGQQPGQPEQGQQPGQGQPGYY--PTSPQQSGQGQQLGQWQQQG-QGQPGYyptsplqPGQGQPGYYPTSPQQ--PGQGQ 539

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  1678 QKGDIGNPGIPGGPGPKGFRGLALTVGLKGEEGSRGLPGP---PGQrGIKGMAGQPVY 1732
Cdd:pfam03157  540 QLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQgqqPGQ-GQQPGQGQPGY 596
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1759-1901 2.06e-19

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: 87.35  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1759 LVFALDNSYDVTEESFNKTRDIITSIVNDLNIRenncPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQDTT 1838
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507116137 1839 EPrDVGNAMRFVTRNVFKRTYAGANVRRVAVFFSNGQTASRSSIITATMEFSALDIspTVFAF 1901
Cdd:cd01450    79 GT-NTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGI--KVFVV 138
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 2291-2465 2.14e-19

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: 87.67  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPtpltstLGDRVAVLSYSppgympNTeecpVYLEFDLVTYNSIHQM 2370
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGP------DGVRVGVVQYS------DD----PRTEFYLNTYRSKDDV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2371 KHHLQDSQQLNGDVFIGHALQWTIDNVFVGTPNLRK--NKVIFVISAGEtnSLDkdvlrNVSLRAKC-QGYSIFVFSFGP 2447
Cdd:cd01472    66 LEAVKNLRYIGGGTNTGKALKYVRENLFTEASGSREgvPKVLVVITDGK--SQD-----DVEEPAVElKQAGIEVFAVGV 138

                         170
                  ....*....|....*....
gi 507116137 2448 KHNDK-ELEELASHPLDHH 2465
Cdd:cd01472   139 KNADEeELKQIASDPKELY 157
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1963-2135 3.47e-19

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: 86.90  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPD------GVRVGVVQYS---------DDPRTEFYLNTYRSKDDVL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2043 NHIQTsFQQLNGEATIGRALLWTTENLFPETPYLRKH--KVIFVVSAGENYERkefVKMMALRAKCQGYVIFVISLGSTR 2120
Cdd:cd01472    67 EAVKN-LRYIGGGTNTGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQDD---VEEPAVELKQAGIEVFAVGVKNAD 142

                         170
                  ....*....|....*
gi 507116137 2121 KDDMEELASYPLDQH 2135
Cdd:cd01472   143 EEELKQIASDPKELY 157
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1004-1166 1.21e-17

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: 82.33  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFPR 1083
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1084 IDFALKKV-SNMFNLHAGGRRnaGVPQTLVVITSGDPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPITG--NSEKI 1160
Cdd:cd01482    81 TGKALTHVrEKNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASkpSETHV 158


                  ....*.
gi 507116137 1161 ITFQDF 1166
Cdd:cd01482   159 FNVADF 164
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1004-1166 1.28e-17

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: 82.37  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFP- 1082
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1083 RIDFALKKVS-NMFNLHAGGRRNAGVPQTLVVITSGDPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPITGNSEKII 1161
Cdd:cd01481    81 NTGSALDYVVkNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 507116137 1162 TFQDF 1166
Cdd:cd01481   161 QVSDF 165
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1567-1623 1.00e-16

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: 75.99  E-value: 1.00e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137  1567 GEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRP 1623
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2291-2466 1.14e-16

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: 79.64  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSPPgymPNTeecpvylEFDLVTYNSIHQM 2370
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPD------GVQVGLVQYSDD---PRT-------EFDLNAYTSKEDV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2371 KHHLQDSQQLNGDVFIGHALQWTIDNVFVGTPNLRKN--KVIFVISAGETnsldKDVLRNVSLRAKCQGYSIFVFSFGpK 2448
Cdd:cd01482    66 LAAIKNLPYKGGNTRTGKALTHVREKNFTPDAGARPGvpKVVILITDGKS----QDDVELPARVLRNLGVNVFAVGVK-D 140

                         170
                  ....*....|....*...
gi 507116137 2449 HNDKELEELASHPLDHHL 2466
Cdd:cd01482   141 ADESELKMIASKPSETHV 158
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1398-1621 1.73e-16

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 85.44  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1398 GPHGTRGLQAMKGSQGLKGSRGHRGEDGN--PGVRGdtgpqGDKGIAGCPGAWGQKGLKG-------FSGPKGGHGDDGI 1468
Cdd:cd21118   119 NSWQGSGGHGAYGSQGGPGVQGHGIPGGTggPWASG-----GNYGTNSLGGSVGQGGNGGplnygtnSQGAVAQPGYGTV 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1469 DGLDGEEGCHGFPGIKGEKG--DPGSQGSPGSRGAPGQYGEKGFP-----GDPGNPGQNNNIKGQKGSKGEQ--GRQGRS 1539
Cdd:cd21118   194 RGNNQNSGCTNPPPSGSHESfsNSGGSSSSGSSGSQGSHGSNGQGssgssGGQGNGGNNGSSSSNSGNSGGSngGSSGNS 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1540 GQKGVQGSPSSRGSRGREGQRGLRGVSG-----EPGNPGPTGtlGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLM 1614
Cdd:cd21118   274 GSGSGGSSSGGSNGWGGSSSSGGSGGSGggnkpECNNPGNDV--RMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTL 351


                  ....*..
gi 507116137 1615 GAKGSTG 1621
Cdd:cd21118   352 NSDASTL 358
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1004-1151 2.09e-16

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: 78.76  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKS-GGFP 1082
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507116137 1083 RIDFALKKVSNMFNlhagGRRNAGVPQTLVVITSGDP---RYDVADAVKTLKDLGICVLVLGIGDVYKEHLL 1151
Cdd:cd00198    81 NIGAALRLALELLK----SAKRPNARRVIILLTDGEPndgPELLAEAARELRKLGITVYTIGIGDDANEDEL 148
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1582-1636 3.18e-16

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: 74.84  E-value: 3.18e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 507116137  1582 GLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLPG 1636
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 29-182 4.22e-16

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: 77.99  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSL 108
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  109 QIGKALQEAHRTyfsapINGRDRKQFPPILVVLASAESED---EVEEASKALQKDGVKIISVGV-QKASEENLKAMAT 182
Cdd:cd00198    81 NIGAALRLALEL-----LKSAKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIgDDANEDELKEIAD 153
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1005-1147 7.02e-16

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: 77.78  E-value: 7.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1005 DVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFPRI 1084
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507116137 1085 DFALKKV-SNMFNLHAGGRRNAgvPQTLVVITSGDPR--YDVADAVKTLKDLGICVLVLGIGDVYK 1147
Cdd:cd01469    82 ATAIQYVvTELFSESNGARKDA--TKVLVVITDGESHddPLLKDVIPQAEREGIIRYAIGVGGHFQ 145
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1759-1922 1.60e-15

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: 76.72  E-value: 1.60e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1759 LVFALDNSYDVTEESFNKTRDIITSIVNDLNIRenncPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYqDTT 1838
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIG----PDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSY-KLG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   1839 EPRDVGNAMRFVTRNVFKRTYAG-ANVRRVAVFFSNGQ-TASRSSIITATMEFSALDISPTVFAFDERV---FLEAFGFD 1913
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSrRGAPKVVILITDGEsNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeeELKKLASA 156


                    ....*....
gi 507116137   1914 NTGTFQVIP 1922
Cdd:smart00327  157 PGGVYVFLP 165
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 441-619 1.66e-15

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: 77.17  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEqIKRFMLEVTEMFsIGPDkVRVGVVQYSDDTEVEFYITDYSNDIdlRKAIFNIKQLT--GG 518
Cdd:cd01474     5 FDLYFVLDKSGSVAANWIE-IYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAI--IKGLEVLKKVTpsGQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  519 TYTGKALDYI-LQIIK-NGMKDRMSKVpcyLIVLTDGMSTDRV----VEPAKRLRAEQITVHAVGIGAANKIELQEIAGK 592
Cdd:cd01474    80 TYIHEGLENAnEQIFNrNGGGRETVSV---IIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADS 156

                         170       180
                  ....*....|....*....|....*....
gi 507116137  593 EERVsFGQN--FDALKSIKNEVVREICAE 619
Cdd:cd01474   157 KEYV-FPVTsgFQALSGIIESVVKKACIE 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1579-1635 2.69e-15

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: 72.14  E-value: 2.69e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137  1579 GAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLP 1635
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 813-985 7.38e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.83  E-value: 7.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGrDRvqFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGG-NT 891
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPG-DR--VSIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGGtAL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  892 YTA--KALKHANALFTEEHGSRIkqnvkqmlIVITDGE----SHDHDQLNDTALELRNKGITIFAVGVGKA-NQKELEGM 964
Cdd:COG2304   169 GAGleLAYELARKHFIPGRVNRV--------ILLTDGDanvgITDPEELLKLAEEAREEGITLTTLGVGSDyNEDLLERL 240

                         170       180
                  ....*....|....*....|..
gi 507116137  965 AGNKN-NTIYVDNFDKLKDVFT 985
Cdd:COG2304   241 ADAGGgNYYYIDDPEEAEKVFV 262
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 441-616 7.73e-15

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: 76.90  E-value: 7.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQ-FEQIKRFMLEVTEMFsigPDKVRVGVVQYSDDTEVefyITDYSNDID-LRKAIFNIkQLTGG 518
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEV---LLPLTRDREaLKRALDEL-PPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  519 TYTGKALDYILQIIKNGMKDRmSKVpcyLIVLTDGMSTDRVVEP---AKRLRAEQITVHAVGIGAANKIE--LQEIAgke 593
Cdd:COG1240   166 TPLGDALALALELLKRADPAR-RKV---IVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA--- 238

                         170       180
                  ....*....|....*....|....*
gi 507116137  594 eRVSFGQNFDA--LKSIKnEVVREI 616
Cdd:COG1240   239 -EATGGRYFRAddLSELA-AIYREI 261
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 2291-2466 8.36e-15

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: 75.88  E-value: 8.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTpltstlGDRVAVLSYSPpgympnteecPVYLEFDLVTYNSIHQM 2370
Cdd:cd01475     4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPD------ATRVGLVQYSS----------TVKQEFPLGRFKSKADL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2371 KHHLQDSQQLNGDVFIGHALQWTIDNVFV----GTP-NLRKNKVIFVISAGETnsldKDVLRNVSLRAKCQGYSIFVFSF 2445
Cdd:cd01475    68 KRAVRRMEYLETGTMTGLAIQYAMNNAFSeaegARPgSERVPRVGIVVTDGRP----QDDVSEVAAKARALGIEMFAVGV 143

                         170       180
                  ....*....|....*....|.
gi 507116137 2446 GpKHNDKELEELASHPLDHHL 2466
Cdd:cd01475   144 G-RADEEELREIASEPLADHV 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1004-1153 1.49e-14

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: 75.50  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFPR 1083
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507116137 1084 IDFALK-KVSNMFNLHAGGR-RNAGVPQTLVVITSGDPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPI 1153
Cdd:cd01475    83 TGLAIQyAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREI 154
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 30-189 2.36e-14

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: 73.54  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   30 DVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQfIGGSLQ 109
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQ-LLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  110 IGKALQEAHRTYFSAPINGrdRKQFPPILVVLASAESED--EVEEASKALQKDGVKIISVGVQKA-----SEENLKAMA- 181
Cdd:cd01469    81 TATAIQYVVTELFSESNGA--RKDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHfqrenSREELKTIAs 158

                         170
                  ....*....|
gi 507116137  182 --TSHFHFNL 189
Cdd:cd01469   159 kpPEEHFFNV 168
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1395-1680 3.37e-14

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 78.84  E-value: 3.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1395 GIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAG----CPGAWGQkGLKGFSGPKGGHGDDGIDG 1470
Cdd:pfam03157  365 GQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGyyptSPQQSGQ-GQPGYYPTSPQQSGQGQQP 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1471 LDGEEGCHGFPGIKGE--KGDPGSQGSPGSRGA-PGQyGEKGF-PGDPGNPGQNNNI-KGQKGSKGEQG------RQGRS 1539
Cdd:pfam03157  444 GQGQQPGQEQPGQGQQpgQGQQGQQPGQPEQGQqPGQ-GQPGYyPTSPQQSGQGQQLgQWQQQGQGQPGyyptspLQPGQ 522

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1540 GQKGVQGSPSSRGSRGREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMgakgs 1619
Cdd:pfam03157  523 GQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYY----- 597

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  1620 tgrPGLLGKKGEPGLPGDLGPVGQtGQRGRQGDSGI-PGYGQMG------RKGVKGPRgfPGDAGQKG 1680
Cdd:pfam03157  598 ---PTSPQQSGQGQQPGQWQQPGQ-GQPGYYPTSSLqLGQGQQGyyptspQQPGQGQQ--PGQWQQSG 659
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1543-1598 4.51e-14

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: 68.67  E-value: 4.51e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 507116137  1543 GVQGSPSSRGSRGREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGE 1598
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 813-989 4.72e-14

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: 72.80  E-value: 4.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVK--KADVGRD----RVQFGALKYSDQPNILF-YLNTYSNRSAIIENLRKRR 885
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAErfLKDYYRKdpagSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  886 DTGGNTYTAKALKHAnalfTEE--HGSRikQNVKQMLIVITDGESH--DHDQLNDTALELRNKGITIFAVGVGKANQKEL 961
Cdd:cd01480    83 YIGGGTFTDCALKYA----TEQllEGSH--QKENKFLLVITDGHSDgsPDGGIEKAVNEADHLGIKIFFVAVGSQNEEPL 156

                         170       180
                  ....*....|....*....|....*...
gi 507116137  962 EGMAGNKNNTIYVDNFDKLKDVFTLVQE 989
Cdd:cd01480   157 SRIACDGKSALYRENFAELLWSFFIDDE 184
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 813-966 5.66e-14

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: 72.80  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQ-YQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTY--SNRS---AIIENLRKRRD 886
Cdd:cd01471     1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDlalNAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  887 TGGNTYTAKALKHANALFTEEHGSRikQNVKQMLIVITDGESHDHDQLNDTALELRNKG--ITIFAVGVGkANQKELEGM 964
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFDTRGNR--ENAPQLVIIMTDGIPDSKFRTLKEARKLRERGviIAVLGVGQG-VNHEENRSL 157


                  ..
gi 507116137  965 AG 966
Cdd:cd01471   158 VG 159
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1490-1732 7.49e-14

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 77.68  E-value: 7.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1490 PG--SQGSPGSRGAPGQYGEKGFPGDPGNPGQnnnikGQKGSKGEQGRQGRSGQKGVQGSPSSRGSRGREGQRGLRGVSG 1567
Cdd:pfam03157  123 PGqaSPQRPGQGQQPGQGQQWYYPTSPQQPGQ-----WQQPGQGQQGYYPTSPQQSGQRQQPGQGQQLRQGQQGQQSGQG 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1568 EPG-------NPGPTGTLGaeglQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMgaKGSTGRPGLLGKKGEPGLPGDLGP 1640
Cdd:pfam03157  198 QPGyyptssqQPGQLQQTG----QGQQGQQPERGQQGQQPGQGQQPGQGQQGQQ--PGQPQQLGQGQQGYYPISPQQPRQ 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1641 VGQTGQrGRQG----DSGIPGYGQMGRkgvkgprgFPGDAGQKGDIGNPGIPGGPGPKGFRGlaltVGLKGEEGSRGLPG 1716
Cdd:pfam03157  272 WQQSGQ-GQQGyyptSLQQPGQGQSGY--------YPTSQQQAGQLQQEQQLGQEQQDQQPG----QGRQGQQPGQGQQG 338

                          250
                   ....*....|....*.
gi 507116137  1717 PPGQRGIKGMAGQPVY 1732
Cdd:pfam03157  339 QQPAQGQQPGQGQPGY 354
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1485-1576 1.15e-13

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: 67.52  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1485 GEKGDPGSQGSPGSRGAPGqygEKGFPGDPGNPGqnnnikgqkgskgeqgrqgrsgqkgvqgspssrgSRGREGQRGLRG 1564
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPG---PPGPPGPPGPPG----------------------------------EPGPPGPPGPPG 43

                           90
                   ....*....|..
gi 507116137  1565 VSGEPGNPGPTG 1576
Cdd:pfam01391   44 PPGPPGAPGAPG 55
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1963-2136 1.17e-13

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: 71.16  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITY-DNQLLM 2041
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPD------GVQVGLVQYS---------DDPRTEFDLNAYtSKEDVL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2042 KnHIQTsFQQLNGEATIGRALLWTTENLFPETPYLRKH--KVIFVVSAGENyerKEFVKMMALRAKCQGYVIFVISLGST 2119
Cdd:cd01482    67 A-AIKN-LPYKGGNTRTGKALTHVREKNFTPDAGARPGvpKVVILITDGKS---QDDVELPARVLRNLGVNVFAVGVKDA 141

                         170
                  ....*....|....*..
gi 507116137 2120 RKDDMEELASYPLDQHL 2136
Cdd:cd01482   142 DESELKMIASKPSETHV 158
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1546-1600 1.37e-13

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: 67.13  E-value: 1.37e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 507116137  1546 GSPSSRGSRGREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGEKG 1600
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1963-2137 1.74e-13

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: 70.67  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFniasdpLISDSGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSL------SASPPGDRVGLVTFG---------SNARVVLPLTTDTDKADLL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2043 NHIQTSFQQLNGEATIGRALLwTTENLFPETPYLRKHKVIFVVSAGENYERKEFVKMMALRAKCQGYVIFVISLGSTRKD 2122
Cdd:cd00198    67 EAIDALKKGLGGGTNIGAALR-LALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANE 145

                         170
                  ....*....|....*.
gi 507116137 2123 D-MEELASYPLDQHLI 2137
Cdd:cd00198   146 DeLKEIADKTTGGAVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 236-404 2.35e-13

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: 70.46  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  236 DLVFLVDESLGTG-GNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKSNT 314
Cdd:cd01469     2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  315 GAAIDQMRRDGFSESYGSRRaqGVPQIAVLVThrpsDDEVHDAALNLRL------EDVNVFALSIQGA--NNTQLEE--- 383
Cdd:cd01469    82 ATAIQYVVTELFSESNGARK--DATKVLVVIT----DGESHDDPLLKDVipqaerEGIIRYAIGVGGHfqRENSREElkt 155

                         170       180
                  ....*....|....*....|.
gi 507116137  384 IVSYPPEQTISTLKSYADLET 404
Cdd:cd01469   156 IASKPPEEHFFNVTDFAALKD 176
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 628-769 2.38e-13

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: 70.88  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  628 DIMFLVDSSWSIGNEN-FRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQ-----QEISDAIDRMSLI 701
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSLYYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507116137  702 NEGTLTGKALNFVGQYFTHSKGARLGAKKFLILITDGVAQDDVR--DPARILR--GKDVTIFSVGVY---NANRS 769
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRerGVIIAVLGVGQGvnhEENRS 156
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 29-169 2.48e-13

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: 70.12  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   29 ADVVFLVDSSDHLGPKsFPFVKTFINKMINSLPIEANKYRVALAQYSDEF--HSEFHLSTFKGRSPMLNHLkKNFQFIGG 106
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGrqRVRFNLPKHNDGEELLEKV-DNLRFIGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507116137  107 SLQIGKALQEAhrTYFSAPINGRdRKQFPPILVVLASAESEDEVEEASKALQKD-GVKIISVGV 169
Cdd:cd01476    79 TTATGAAIEVA--LQQLDPSEGR-REGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGT 139
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1963-2136 2.99e-13

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: 71.65  E-value: 2.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNiasdplISDSGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:cd01475     4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLD------VGPDATRVGLVQYS---------STVKQEFPLGRFKSKADLK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2043 NHIQTSFQQLNGEATiGRALLWTTENLFPETPYLRKH-----KVIFVVSAGENYERkefVKMMALRAKCQGYVIFVISLG 2117
Cdd:cd01475    69 RAVRRMEYLETGTMT-GLAIQYAMNNAFSEAEGARPGservpRVGIVVTDGRPQDD---VSEVAAKARALGIEMFAVGVG 144

                         170
                  ....*....|....*....
gi 507116137 2118 STRKDDMEELASYPLDQHL 2136
Cdd:cd01475   145 RADEEELREIASEPLADHV 163
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1600-1657 3.15e-13

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: 66.36  E-value: 3.15e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  1600 GSQGQKGPQGSPGLMGAKGSTGRPgllGKKGEPGLPGDLGPVGQTGQRGRQGDSGIPG 1657
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPP---GPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1394-1447 4.26e-13

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: 65.98  E-value: 4.26e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 507116137  1394 PGIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGA 1447
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 807-994 4.90e-13

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: 69.85  E-value: 4.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  807 CKRItlLDVVFVLDHSGSIKKQYqDHMINLTIHLVKKadVGRDRVQFGALKYSDQPNILFYLNTYsnRSAIIENLR--KR 884
Cdd:cd01474     1 CAGH--FDLYFVLDKSGSVAANW-IEIYDFVEQLVDR--FNSPGLRFSFITFSTRATKILPLTDD--SSAIIKGLEvlKK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  885 RDTGGNTYTAKALKHAN-ALFTEEHGSRIKQNVkqmLIVITDGESHD--HDQLNDTALELRNKGITIFAVGVGKANQKEL 961
Cdd:cd01474    74 VTPSGQTYIHEGLENANeQIFNRNGGGRETVSV---IIALTDGQLLLngHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQL 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 507116137  962 EGMAGNKNNTIYVDN-FDKLKDVFTLVQERMCTE 994
Cdd:cd01474   151 INIADSKEYVFPVTSgFQALSGIIESVVKKACIE 184
VWA_2 pfam13519
von Willebrand factor type A domain;
445-550 8.90e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 66.55  E-value: 8.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   445 FLIDGSSSI-----QEKQFEQIKRFMLEVTEMFsigpDKVRVGVVQYSDDTEVEFYITDYSNDIdlRKAIFNIKQLTGGT 519
Cdd:pfam13519    3 FVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTKDRAKI--LRALRRLEPKGGGT 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 507116137   520 YTGKALDYILQIikngMKDRMSKVPCYLIVL 550
Cdd:pfam13519   77 NLAAALQLARAA----LKHRRKNQPRRIVLI 103
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 235-393 1.55e-12

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: 67.59  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVDESLGTGG-NLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQV-GKS 312
Cdd:cd00198     1 ADIVFLLDVSGSMGGeKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLgGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  313 NTGAAIDQMRRDGFSESYGSRRaqgvpQIAVLVT---HRPSDDEVHDAALNLRLEDVNVFALSI-QGANNTQLEEIVSYP 388
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNAR-----RVIILLTdgePNDGPELLAEAARELRKLGITVYTIGIgDDANEDELKEIADKT 155


                  ....*
gi 507116137  389 PEQTI 393
Cdd:cd00198   156 TGGAV 160
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 627-797 1.65e-12

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: 70.35  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNEN-FRKMKIFMKNLLTKIQigaDKTQIGVVQFSDKTKEEFQLNRyfTQQEISDAIDRMSlINEGT 705
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP-PGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  706 LTGKALNFVGQYFthsKGARLGAKKFLILITDGVAQDDVRDP---ARILRGKDVTIFSVGVYNA--NRSQLEEISGDSS- 779
Cdd:COG1240   167 PLGDALALALELL---KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEavDEGLLREIAEATGg 243

                         170
                  ....*....|....*...
gi 507116137  780 LVFHVENFDHLKALERKL 797
Cdd:COG1240   244 RYFRADDLSELAAIYREI 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2291-2467 2.43e-12

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: 67.21  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPtpltstLGDRVAVLSYSppgympnteeCPVYLEFDLVTYNSIHQM 2370
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASP------PGDRVGLVTFG----------SNARVVLPLTTDTDKADL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2371 KHHLQDSQ-QLNGDVFIGHALQWTIDNVFVGTPNLRKnKVIFVISAGETNSLDKDVLRNVSlRAKCQGYSIFVFSFGPKH 2449
Cdd:cd00198    66 LEAIDALKkGLGGGTNIGAALRLALELLKSAKRPNAR-RVIILLTDGEPNDGPELLAEAAR-ELRKLGITVYTIGIGDDA 143

                         170
                  ....*....|....*...
gi 507116137 2450 NDKELEELASHPLDHHLV 2467
Cdd:cd00198   144 NEDELKEIADKTTGGAVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 2290-2469 2.46e-12

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: 67.77  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2290 MDVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPtplTSTLgdrVAVLSYSppgympnteECPVYlEFDLVTYNSIHQ 2369
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGP---TKTQ---FGLVQYS---------ESFRT-EFTLNEYRTKEE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2370 MKHHLQDSQQLNGDVFIGHALQWTIDNVFVGTPNLRKN--KVIFVISAGET--NSLDKDVLrNVSLRAKCQGYSIFVF-S 2444
Cdd:cd01469    65 PLSLVKHISQLLGLTNTATAIQYVVTELFSESNGARKDatKVLVVITDGEShdDPLLKDVI-PQAEREGIIRYAIGVGgH 143

                         170       180
                  ....*....|....*....|....*
gi 507116137 2445 FGPKHNDKELEELASHPLDHHLVQL 2469
Cdd:cd01469   144 FQRENSREELKTIASKPPEEHFFNV 168
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1440-1517 2.80e-12

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: 63.67  E-value: 2.80e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  1440 GIAGCPGAWGQKGLKGFSGPkgghgddgidgldgeegchgfPGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNP 1517
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGP---------------------PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 813-985 4.10e-12

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: 68.81  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSikkqyqdhMINLT-IHLVKKA-----DVGRDRVQFGALKYSDQPNILFYLnTYSNRSAI--IENLRkr 884
Cdd:COG1240    93 RDVVLVVDASGS--------MAAENrLEAAKGAlldflDDYRPRDRVGLVAFGGEAEVLLPL-TRDREALKraLDELP-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  885 rdTGGNTYTAKALKHANALFTEEHGSRIKqnvkqMLIVITDGESHD-HDQLNDTALELRNKGITIFAVGVGKA--NQKEL 961
Cdd:COG1240   162 --PGGGTPLGDALALALELLKRADPARRK-----VIVLLTDGRDNAgRIDPLEAAELAAAAGIRIYTIGVGTEavDEGLL 234

                         170       180
                  ....*....|....*....|....*
gi 507116137  962 EGMAGNKN-NTIYVDNFDKLKDVFT 985
Cdd:COG1240   235 REIAEATGgRYFRADDLSELAAIYR 259
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1005-1143 4.18e-12

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: 67.03  E-value: 4.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1005 DVIFLCDGSDRVSNSDFVT-MTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELK--NSLTKTQWKTQIQNVSK---S 1078
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVThVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSspNSTNKDLALNAIRALLSlyyP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137 1079 GGFPRIDFALKKVSNMFNLHAGGRRNAgvPQTLVVITSGDP--RYDVADAVKTLKDLGICVLVLGIG 1143
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENA--PQLVIIMTDGIPdsKFRTLKEARKLRERGVIIAVLGVG 146
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 442-591 7.77e-12

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: 66.25  E-value: 7.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  442 DIHFLIDGSSSIQE-KQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDY-SNDIDL-RKAIFNIKQL--- 515
Cdd:cd01471     2 DLYLLVDGSGSIGYsNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnSTNKDLaLNAIRALLSLyyp 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507116137  516 TGGTYTGKALDYILQIIKNGMKDRmSKVPCYLIVLTDGMSTD--RVVEPAKRLRAEQITVHAVGIGAA-NKIELQEIAG 591
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNR-ENAPQLVIIMTDGIPDSkfRTLKEARKLRERGVIIAVLGVGQGvNHEENRSLVG 159
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1525-1580 8.38e-12

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: 62.13  E-value: 8.38e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 507116137  1525 GQKGSKGEQGRQGRSGQKGVQGSPSSRGSRGREGQRGLRGVSGEPGNPGPTGTLGA 1580
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1479-1532 1.48e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 61.36  E-value: 1.48e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 507116137  1479 GFPGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPgqnnnikGQKGSKGE 1532
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP-------GAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1425-1502 1.51e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 61.36  E-value: 1.51e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137  1425 GNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPkgghgddgidgldgeegchgfPGIKGEKGDPGSQGSPGSRGAP 1502
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP---------------------PGPPGPPGPPGPPGAPGAPGPP 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1403-1668 1.57e-11

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 69.64  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1403 RGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGpkgghgddgidgldgeegchgfpg 1482
Cdd:cd21118   112 HGVDAVHNSWQGSGGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVG------------------------ 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1483 iKGEKGDPGSQGSpGSRGAPGQYGEKGFPGDPGNPGQNNniKGQKGSKGEQGRQGRSGQKGVQGSPSSRGSrgreGQRGL 1562
Cdd:cd21118   168 -QGGNGGPLNYGT-NSQGAVAQPGYGTVRGNNQNSGCTN--PPPSGSHESFSNSGGSSSSGSSGSQGSHGS----NGQGS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1563 RGVSGEPGNPGPTGtlGAEGLQGPQGSQ--GNPGRKGekGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKG-EPGLPG-DL 1638
Cdd:cd21118   240 SGSSGGQGNGGNNG--SSSSNSGNSGGSngGSSGNSG--SGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKpECNNPGnDV 315

                         250       260       270
                  ....*....|....*....|....*....|..
gi 507116137 1639 GPVGQTGQRGRQGDSGIPGY--GQMGRKGVKG 1668
Cdd:cd21118   316 RMAGGGGSQGSKESSGSHGSngGNGQAEAVGG 347
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 25-203 2.95e-11

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: 64.71  E-value: 2.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   25 GPVyaDVVFLVDSSDHLGPKSFPFVKTFINKMINSL------PIEANKYRVALAQYSDEFHSEFhlstfkGRSPMLNHLK 98
Cdd:cd01480     1 GPV--DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEA------GFLRDIRNYT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   99 ------KNFQFIGGSLQIGKALQEAHRTYFSAPINGRDRkqfppILVVLASAES--------EDEVEEASKAlqkdGVKI 164
Cdd:cd01480    73 slkeavDNLEYIGGGTFTDCALKYATEQLLEGSHQKENK-----FLLVITDGHSdgspdggiEKAVNEADHL----GIKI 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 507116137  165 ISVGVQKASEENLKAMATSHFHFNLR---TIRDLSTFSQNMT 203
Cdd:cd01480   144 FFVAVGSQNEEPLSRIACDGKSALYRenfAELLWSFFIDDET 185
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1413-1491 3.49e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.59  E-value: 3.49e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507116137  1413 GLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKgfsgpkgghgddgidgldgeegchGFPGIKGEKGDPG 1491
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP------------------------GPPGPPGAPGAPG 55
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1759-1900 5.38e-11

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: 63.40  E-value: 5.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1759 LVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENncpvGARVAMVSYnSGT----SYLirwSDYNRKKQLLQQLSQIKY 1834
Cdd:cd01472     3 IVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPD----GVRVGVVQY-SDDprteFYL---NTYRSKDDVLEAVKNLRY 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137 1835 qdTTEPRDVGNAMRFVTRNVFKRTY-AGANVRRVAVFFSNGQtaSRSSIITATMEFSALDISptVFA 1900
Cdd:cd01472    75 --IGGGTNTGKALKYVRENLFTEASgSREGVPKVLVVITDGK--SQDDVEEPAVELKQAGIE--VFA 135
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1398-1452 5.52e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.81  E-value: 5.52e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 507116137  1398 GPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKG 1452
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1410-1460 5.52e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.81  E-value: 5.52e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 507116137  1410 GSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPK 1460
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 814-961 1.27e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 64.70  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  814 DVVFVLDHSGSikkqyqdhMINLTIHLVKKA-----DVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTG 888
Cdd:COG2425   120 PVVLCVDTSGS--------MAGSKEAAAKAAalallRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGG 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507116137  889 GnTYTAKALKHANALFTEEHGSRikqnvkQMLIVITDGESH-DHDQLNDTALElRNKGITIFAVGVGKANQKEL 961
Cdd:COG2425   192 G-TDIAPALRAALELLEEPDYRN------ADIVLITDGEAGvSPEELLREVRA-KESGVRLFTVAIGDAGNPGL 257
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 440-590 1.43e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 64.32  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  440 EADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSigpDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIkQLTGGT 519
Cdd:COG2425   118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGL-FAGGGT 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507116137  520 YTGKALDYILQIIKNGmKDRMSKVpcylIVLTDGMSTDRVVEPAKRLRAEQ--ITVHAVGIGAANKIELQEIA 590
Cdd:COG2425   194 DIAPALRAALELLEEP-DYRNADI----VLITDGEAGVSPEELLREVRAKEsgVRLFTVAIGDAGNPGLLEAL 261
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 2291-2461 1.84e-10

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: 61.96  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTPLtstlgdRVAVLSYSppgympNTeecpVYLEFDLVTYNS---- 2366
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKI------RVAVVQFS------DT----PRPEFYLNTHSTkadv 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2367 ---IHQMKhhLQDSQQLNgdvfIGHALQWTIDNVFV---------GTPnlrknKVIFVISAGEtnSLDkDVLR--NVSLR 2432
Cdd:cd01481    66 lgaVRRLR--LRGGSQLN----TGSALDYVVKNLFTksagsrieeGVP-----QFLVLITGGK--SQD-DVERpaVALKR 131

                         170       180       190
                  ....*....|....*....|....*....|
gi 507116137 2433 AkcqgySIFVFSFGPKHNDK-ELEELASHP 2461
Cdd:cd01481   132 A-----GIVPFAIGARNADLaELQQIAFDP 156
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1963-2131 2.92e-10

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: 61.19  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1963 DVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDPLisdsgdRIALLSYSpwessrrkmGTVKTEFDFITYDNQLLMK 2042
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKI------RVAVVQFS---------DTPRPEFYLNTHSTKADVL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2043 NHIQTSFQQLNGEATIGRALLWTTENLFPETPYLR------KHKVIfvVSAGENYERkefVKMMALRAKCQGYVIFVISL 2116
Cdd:cd01481    67 GAVRRLRLRGGSQLNTGSALDYVVKNLFTKSAGSRieegvpQFLVL--ITGGKSQDD---VERPAVALKRAGIVPFAIGA 141

                         170
                  ....*....|....*
gi 507116137 2117 GSTRKDDMEELASYP 2131
Cdd:cd01481   142 RNADLAELQQIAFDP 156
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1410-1459 3.54e-10

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 57.50  E-value: 3.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 507116137  1410 GSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGP 1459
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1476-1717 4.24e-10

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 65.02  E-value: 4.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1476 GCHGFPGIKGEkGDPGSQGSPGSRGAP----GQYGEKGFPGDPGNPGQNNNIKGQKGSKGEQGRQGRSGQKGVQGSPSSr 1551
Cdd:cd21118   131 GSQGGPGVQGH-GIPGGTGGPWASGGNygtnSLGGSVGQGGNGGPLNYGTNSQGAVAQPGYGTVRGNNQNSGCTNPPPS- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1552 GSRGREGQRGLRGVSGEPGNPGPTGTLGAeGLQGPQGSQGNPGRKGekGSQGQKGPQGSpGLMGAKGSTGRPGllgkkge 1631
Cdd:cd21118   209 GSHESFSNSGGSSSSGSSGSQGSHGSNGQ-GSSGSSGGQGNGGNNG--SSSSNSGNSGG-SNGGSSGNSGSGS------- 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1632 pglpGDLGPVGQTGQRGRQGDSGIPGYGQMGRKGVKGPRGFPGDAGQKGDIGNPGIPGGPGPKGFRGLALTVGLKGEEGS 1711
Cdd:cd21118   278 ----GGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNS 353


                  ....*.
gi 507116137 1712 RGLPGP 1717
Cdd:cd21118   354 DASTLP 359
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1416-1514 4.94e-10

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 57.12  E-value: 4.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1416 GSRGHRGEDGNPGVRGDTGPQgdkgiagcpgawgqkglkgfsgpkgghgddgidgldgeegchGFPGIKGEKGDPGSQGS 1495
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPP------------------------------------------GPPGPPGPPGEPGPPGP 38

                           90
                   ....*....|....*....
gi 507116137  1496 PGSRGAPGQYGEKGFPGDP 1514
Cdd:pfam01391   39 PGPPGPPGPPGAPGAPGPP 57
VWA_2 pfam13519
von Willebrand factor type A domain;
815-923 9.64e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.07  E-value: 9.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   815 VVFVLDHSGSI-----KKQYQDHMINLTIHLVKKadvgRDRVQFGALKYSDQPNILFYLNtySNRSAIIENLRKRRDTGG 889
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKS----LPGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 507116137   890 NTYTAKALKHANALFteehgSRIKQNVKQMLIVI 923
Cdd:pfam13519   75 GTNLAAALQLARAAL-----KHRRKNQPRRIVLI 103
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 813-984 1.59e-09

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: 59.21  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSikkqyqdhMINLTIHLVKKA-----DVGRDRVQFGALKYSDQPNILFYLNTYSNRSAI---IENLRKR 884
Cdd:cd01465     1 LNLVFVIDRSGS--------MDGPKLPLVKSAlkllvDQLRPDDRLAIVTYDGAAETVLPATPVRDKAAIlaaIDRLTAG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  885 RDTGGNTYTAKALKHANALFTEEHGSRIkqnvkqmlIVITDGESH----DHDQLNDTALELRNKGITIFAVGVGKA-NQK 959
Cdd:cd01465    73 GSTAGGAGIQLGYQEAQKHFVPGGVNRI--------LLATDGDFNvgetDPDELARLVAQKRESGITLSTLGFGDNyNED 144

                         170       180
                  ....*....|....*....|....*.
gi 507116137  960 ELEGMAGNKN-NTIYVDNFDKLKDVF 984
Cdd:cd01465   145 LMEAIADAGNgNTAYIDNLAEARKVF 170
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1633-1718 2.06e-09

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.58  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1633 GLPGDLGPVGQTGQRGRQGDSGIPGygqmgrkgVKGPRGFPGDAGQKGdignpgipgGPgpkgfrglaltvGLKGEEGSR 1712
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG--------PPGPPGEPGPPGPPG---------PP------------GPPGPPGAP 51


                   ....*.
gi 507116137  1713 GLPGPP 1718
Cdd:pfam01391   52 GAPGPP 57
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 235-384 2.59e-09

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: 58.56  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVDESLGTGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTIS--FLKSSTTQSEFQQQIKNLSIQVGKS 312
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVrfNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507116137  313 NTGAAIdQMRRDGFSESYGSRraQGVPQIAVLVTHRPSDDEVHDAALNLR-LEDVNVFALSI---QGANNTQLEEI 384
Cdd:cd01476    81 ATGAAI-EVALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTgdpGTVDTEELHSI 153
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2291-2452 2.87e-09

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: 58.94  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2291 DVAFLIDASQRVGSDEFKEVKAFITSVLDYF----HIAPTPLTStlgdRVAVLSYSPPGympnTEECPvylefDLVTYNS 2366
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyYRKDPAGSW----RVGVVQYSDQQ----EVEAG-----FLRDIRN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2367 IHQMKHHLQDSQQLNGDVFIGHALQWTIDNVFVGTPNLRKNKVIfVISAGETNSLDKDVLRNVSLRAKCQGYSIFVFSFG 2446
Cdd:cd01480    71 YTSLKEAVDNLEYIGGGTFTDCALKYATEQLLEGSHQKENKFLL-VITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVG 149


                  ....*.
gi 507116137 2447 PKHNDK 2452
Cdd:cd01480   150 SQNEEP 155
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1759-1905 5.24e-09

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: 57.58  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1759 LVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENncpvGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQdTT 1838
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPP----GDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKG-LG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137 1839 EPRDVGNAMRFVTRNVFKRTYagANVRRVAVFFSNGQ-TASRSSIITATMEFSALDISPTVFAFDERV 1905
Cdd:cd00198    78 GGTNIGAALRLALELLKSAKR--PNARRVIILLTDGEpNDGPELLAEAARELRKLGITVYTIGIGDDA 143
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 442-617 5.83e-09

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 58.10  E-value: 5.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  442 DIHFLIDGSSSIQEKQFE-QIKRFMLEVTEMFSIGPDKVRVGVVQYSDD--TEVEFYITDYSNDIDLRKAIFNIKQLT-- 516
Cdd:cd01473     2 DLTLILDESASIGYSNWRkDVIPFTEKIINNLNISKDKVHVGILLFAEKnrDVVPFSDEERYDKNELLKKINDLKNSYrs 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  517 -GGTYTGKALDYIL-QIIKNGmkDRMSKVPCYLIVLTDGMSTDR----VVEPAKRLRAEQITVHAVGIGAANKIELQEIA 590
Cdd:cd01473    82 gGETYIVEALKYGLkNYTKHG--NRRKDAPKVTMLFTDGNDTSAskkeLQDISLLYKEENVKLLVVGVGAASENKLKLLA 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 507116137  591 GKEE------RVSFgQNFDALKSIKNEVVREIC 617
Cdd:cd01473   160 GCDInndncpNVIK-TEWNNLNGISKFLTDKIC 191
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 627-802 1.08e-08

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 57.14  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIgNENFRKMKIFMKNLLTKIQigADKTQIGVVQFSDKTKEEFQLNRYfTQQEISDAIDRMSLINEG-T 705
Cdd:cd01474     5 FDLYFVLDKSGSV-AANWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDD-SSAIIKGLEVLKKVTPSGqT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  706 LTGKALNFVGQYFTHSKGARLGAKKFLILITDGVAQDDV-RDP---ARILRGKDVTIFSVGVYNANRSQLEEISGDSSLV 781
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGhKYPeheAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                         170       180
                  ....*....|....*....|..
gi 507116137  782 FHV-ENFDHLKALERKLIFRVC 802
Cdd:cd01474   161 FPVtSGFQALSGIIESVVKKAC 182
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 628-802 1.57e-08

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 56.94  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  628 DIMFLVDSSWSIGNENFRKMKI-FMKNLLTKIQIGADKTQIGVVQFSDKTKEefqLNRyFTQQEISDAIDRMSLIN---- 702
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDVIpFTEKIINNLNISKDKVHVGILLFAEKNRD---VVP-FSDEERYDKNELLKKINdlkn 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  703 -----EGTLTGKALNFVGQYFTHSKGARLGAKKFLILITDG----VAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEE 773
Cdd:cd01473    78 syrsgGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKL 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 507116137  774 ISG----DSSLVFHVE-NFDHLKALERKLIFRVC 802
Cdd:cd01473   158 LAGcdinNDNCPNVIKtEWNNLNGISKFLTDKIC 191
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 814-992 1.81e-08

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 56.56  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  814 DVVFVLDHSGSI-KKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPN--ILFYLNTYSNRSAIIENLRKRRD---T 887
Cdd:cd01473     2 DLTLILDESASIgYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLKNsyrS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  888 GGNTYTAKALKHANALFTeeHGSRIKQNVKQMLIVITDGESHDHD--QLNDTALELRNKGITIFAVGVGKANQKELEGMA 965
Cdd:cd01473    82 GGETYIVEALKYGLKNYT--KHGNRRKDAPKVTMLFTDGNDTSASkkELQDISLLYKEENVKLLVVGVGAASENKLKLLA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 507116137  966 G-NKNNT----IYVDNFDKLKDVFTLVQERMC 992
Cdd:cd01473   160 GcDINNDncpnVIKTEWNNLNGISKFLTDKIC 191
VWA_2 pfam13519
von Willebrand factor type A domain;
629-735 2.15e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 2.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   629 IMFLVDSSWSIGNENFRKMKI-FMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRyfTQQEISDAIDRMSLINEGTLT 707
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRLeAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGTNL 78

                           90       100
                   ....*....|....*....|....*...
gi 507116137   708 GKALNFVGQYFthsKGARLGAKKFLILI 735
Cdd:pfam13519   79 AAALQLARAAL---KHRRKNQPRRIVLI 103
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1403-1651 2.49e-08

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 59.58  E-value: 2.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1403 RGLQAMKGSQGLKGSRGHRGEDGNPGVRG--DTGPQgDKGIAGCPGAW--------------------GQKGLKGFSGPK 1460
Cdd:pfam03157  456 QGQQPGQGQQGQQPGQPEQGQQPGQGQPGyyPTSPQ-QSGQGQQLGQWqqqgqgqpgyyptsplqpgqGQPGYYPTSPQQ 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1461 GGHGDDGIDGLDGEEGCHGFPGIKGEKGD-PGSQGSPGSRGAPGQ-----------YGEKGF-PGDPGNPGQnnnikGQK 1527
Cdd:pfam03157  535 PGQGQQLGQLQQPTQGQQGQQSGQGQQGQqPGQGQQGQQPGQGQQgqqpgqgqqpgQGQPGYyPTSPQQSGQ-----GQQ 609

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1528 GSKGEQGRQGRSGQ---------KGVQG-SPSSRGSRGREGQRGLRGVSGEpGNPGPTGTLGAEGLQGPQGSQGNPGRKG 1597
Cdd:pfam03157  610 PGQWQQPGQGQPGYyptsslqlgQGQQGyYPTSPQQPGQGQQPGQWQQSGQ-GQQGYYPTSPQQSGQAQQPGQGQQPGQW 688

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 507116137  1598 EKGSQGQKG-----PQgSPGLMGAKGSTGRPGLLGKKGEPGLPGDlgpvGQTGQRGRQG 1651
Cdd:pfam03157  689 LQPGQGQQGyyptsPQ-QPGQGQQLGQGQQSGQGQQGYYPTSPGQ----GQQSGQGQQG 742
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1648-1730 2.52e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 52.50  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1648 GRQGDSGIPGygQMGRKGVKGPRGFPGDAGQkgdignpgipggPgpkgfrglaltvGLKGEEGSRGLPGPPGQRGIKGMA 1727
Cdd:pfam01391    1 GPPGPPGPPG--PPGPPGPPGPPGPPGPPGP------------P------------GEPGPPGPPGPPGPPGPPGAPGAP 54


                   ...
gi 507116137  1728 GQP 1730
Cdd:pfam01391   55 GPP 57
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 442-606 3.08e-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: 56.14  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  442 DIHFLIDGSSSIQEKQFEQIKRF---MLEVTEMFSIGPdkvRVGVVQYSDDTEVEFYITD-YSNDID-----LRKAIFNI 512
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAKNAiktLIEKISSYEVSP---RYEIISYASDPKEIVSIRDfNSNDADdvikrLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  513 KQLTGGTYTGKALDYIL---QIIKNGMKDRMSKVPCYLIVLTDGMST---------DRVVE------PAKRLRAEQITVH 574
Cdd:cd01470    79 HGDKTGTNTAAALKKVYermALEKVRNKEAFNETRHVIILFTDGKSNmggsplptvDKIKNlvyknnKSDNPREDYLDVY 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 507116137  575 AVGIGA-ANKIELQEIAGKE--ERVSFG-QNFDALK 606
Cdd:cd01470   159 VFGVGDdVNKEELNDLASKKdnERHFFKlKDYEDLQ 194
PHA03169 PHA03169
hypothetical protein; Provisional
 1476-1680 1.80e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 56.13  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1476 GCHGfpgikGEKGDPGSQGSPGSRGAPGQygekgfPGDPGNPGQnnnikgQKGSKGEQGrQGRSGQKGVQGSPSSRGSRG 1555
Cdd:PHA03169   24 KRHG-----GTREQAGRRRGTAARAAKPA------PPAPTTSGP------QVRAVAEQG-HRQTESDTETAEESRHGEKE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1556 REGQrglrgvsgepgnPGPTGTlGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLP 1635
Cdd:PHA03169   86 ERGQ------------GGPSGS-GSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPP 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 507116137 1636 GDLGPVGqtgqrGRQGDSGIPGYGQMGRKGVKGPRGFPGDAGQKG 1680
Cdd:PHA03169  153 ESHNPSP-----NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGP 192
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 236-389 3.06e-07

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: 53.16  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  236 DLVFLVDES--LGTGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQ-----QQIKNLSIQ 308
Cdd:cd01471     2 DLYLLVDGSgsIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLalnaiRALLSLYYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  309 VGKSNTGAAIDQMRRDGFsESYGSRraQGVPQIAVLVTHRPSDDEVH--DAALNLRLEDVNVFALSI-QGANNTQLEEIV 385
Cdd:cd01471    82 NGSTNTTSALLVVEKHLF-DTRGNR--ENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGVgQGVNHEENRSLV 158


                  ....
gi 507116137  386 SYPP 389
Cdd:cd01471   159 GCDP 162
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 30-181 3.56e-07

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: 52.77  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   30 DVVFLVDSSDHLG-PKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSP-----MLNHLKKNFqF 103
Cdd:cd01471     2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLY-Y 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  104 IGGSLQIGKALQEAHRTYFSAPINgrdRKQFPPILVVLASAESEDEVE--EASKALQKDGVKI--ISVGVQKASEENlKA 179
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFDTRGN---RENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIavLGVGQGVNHEEN-RS 156


                  ..
gi 507116137  180 MA 181
Cdd:cd01471   157 LV 158
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1962-2139 4.09e-07

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: 52.36  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1962 MDVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASdplisdSGDRIALLSYSpwessrrkmGTVKTEFDFITY---DNQ 2038
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGP------TKTQFGLVQYS---------ESFRTEFTLNEYrtkEEP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2039 LLMKNHIqtsfQQLNGEATIGRALLWTTENLFPETPYLRKH--KVIFVVSAGE---NYERKEFVKMmalrAKCQGYVIFV 2113
Cdd:cd01469    66 LSLVKHI----SQLLGLTNTATAIQYVVTELFSESNGARKDatKVLVVITDGEshdDPLLKDVIPQ----AEREGIIRYA 137

                         170       180       190
                  ....*....|....*....|....*....|.
gi 507116137 2114 ISLGS--TRKDDMEEL---ASYPLDQHLIQL 2139
Cdd:cd01469   138 IGVGGhfQRENSREELktiASKPPEEHFFNV 168
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 628-774 5.35e-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: 53.53  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  628 DIMFLVDSSWSIGNENFRKMKIFMKNLLtkiQIGADKTQIGVVQFSDKTKEEFQLNRyftQQEISDAIDRMSLI--NEGT 705
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALL---RALRPNRRFGVILFDTEVVEDLPLTA---DDGLEDAIEFLSGLfaGGGT 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507116137  706 LTGKALNFVGQYFTHSKGARlgakKFLILITDGVAQDDVRDPARILRGK--DVTIFSVGVYNANRSQLEEI 774
Cdd:COG2425   194 DIAPALRAALELLEEPDYRN----ADIVLITDGEAGVSPEELLREVRAKesGVRLFTVAIGDAGNPGLLEA 260
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1757-1875 6.14e-07

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: 51.52  E-value: 6.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1757 TELVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENncpvGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQd 1836
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPD----GVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYK- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 507116137 1837 tTEPRDVGNAMRFVTRNVFKrTYAGA--NVRRVAVFFSNGQ 1875
Cdd:cd01482    76 -GGNTRTGKALTHVREKNFT-PDAGArpGVPKVVILITDGK 114
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1756-1885 7.89e-07

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: 52.39  E-value: 7.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1756 PTELVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENNcpvgARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQ 1835
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDA----TRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 507116137 1836 DT---TeprdvGNAMRFVTRNVFKRTyAGA-----NVRRVAVFFSNGQTASRSSIITA 1885
Cdd:cd01475    78 ETgtmT-----GLAIQYAMNNAFSEA-EGArpgseRVPRVGIVVTDGRPQDDVSEVAA 129
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1004-1154 8.32e-07

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: 51.62  E-value: 8.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1004 ADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNF------DIQSQRMKIGMAQFgSNYQSIIE--LKNSLTKTQWKTQIQNV 1075
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQY-SDQQEVEAgfLRDIRNYTSLKEAVDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1076 SKSGGFPRIDFALKKVSNMFNLHAGGRRNagvpQTLVVITSGDPRYDVA----DAVKTLKDLGICVLVLGIGDVYKEHLL 1151
Cdd:cd01480    82 EYIGGGTFTDCALKYATEQLLEGSHQKEN----KFLLVITDGHSDGSPDggieKAVNEADHLGIKIFFVAVGSQNEEPLS 157


                  ...
gi 507116137 1152 PIT 1154
Cdd:cd01480   158 RIA 160
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
628-793 2.15e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 50.69  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  628 DIMFLVDSSWSIGNENFRKMK---IFMKNLLTKIQIGADKTQIGVVQFSDK--------TKEEFQLNRYFtqqeisdaid 696
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNeglQALIDELRQDPYALETVEVSVITFDGEakvllpltDLEDFQPPDLS---------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  697 rmslINEGTLTGKALNF--------VGQYFTHSKGARlgaKKFLILITDGVAQD-DVRDPARILR----GKDVTIFSVGV 763
Cdd:COG4245    77 ----ASGGTPLGAALELlldlierrVQKYTAEGKGDW---RPVVFLITDGEPTDsDWEAALQRLKdgeaAKKANIFAIGV 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 507116137  764 -YNANRSQLEEISgDSSLVFHVENFDHLKAL 793
Cdd:COG4245   150 gPDADTEVLKQLT-DPVRALDALDGLDFREF 179
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1758-1857 5.87e-06

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: 48.86  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1758 ELVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENNCPVGarVAMVSYNSGTSYLIRwsDYNRKKQLLQQLSQIKYQDT 1837
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVA--VVQFSDTPRPEFYLN--THSTKADVLGAVRRLRLRGG 77

                          90       100
                  ....*....|....*....|
gi 507116137 1838 TePRDVGNAMRFVTRNVFKR 1857
Cdd:cd01481    78 S-QLNTGSALDYVVKNLFTK 96
PHA03169 PHA03169
hypothetical protein; Provisional
 1504-1654 8.57e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 50.74  E-value: 8.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1504 QYGEKGFPGDPGNPGQnnnikGQKGSKGEQGRQGRSGQKGVQG-SPSSRGSRGREGQRGLRGVSGEPGNPGPtGTLGAEG 1582
Cdd:PHA03169   80 RHGEKEERGQGGPSGS-----GSESVGSPTPSPSGSAEELASGlSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPE 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507116137 1583 LQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLPGDLGPVGQTGQRGRQGDSG 1654
Cdd:PHA03169  154 SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSP 225
PHA03169 PHA03169
hypothetical protein; Provisional
 1384-1624 8.64e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 50.74  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1384 RTCCCTFCKCPG----IPGPHGTRGLQAMKGSQGLKGSRGHR----GEDGNPGVRGDTGPQGDKGiAGCPGAWGQKGLKG 1455
Cdd:PHA03169   16 RSSCRGHCKRHGgtreQAGRRRGTAARAAKPAPPAPTTSGPQvravAEQGHRQTESDTETAEESR-HGEKEERGQGGPSG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1456 fSGPKGGHGDDGIDGLDGEEGCHgfpGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQNNNIKGQKGSKGEQGr 1535
Cdd:PHA03169   95 -SGSESVGSPTPSPSGSAEELAS---GLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1536 QGRSGQKGVQGSPSSRGSRGREGQRGLRGVSGEPG-----NPGPTGTLGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGS 1610
Cdd:PHA03169  170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPqsppdEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249

                         250
                  ....*....|....*...
gi 507116137 1611 PGL----MGAKGSTGRPG 1624
Cdd:PHA03169  250 HRShsytVVGWKPSTRPG 267
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 982-1143 9.46e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 51.12  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  982 DVFTLVQERMCTE---APEVCHlQEADVIFLCDGSDRVSNSDFVT-MTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSII 1057
Cdd:PTZ00441   19 SIFARGDNKIVDEvkyREEVCN-EEVDLYLLVDGSGSIGYHNWIThVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1058 ELKN--SLTKTQWKTQIQNVSKSG---GFPRIDFALKKVSNMFNLHAGgRRNAGvpQTLVVITSGDP--RYDVADAVKTL 1130
Cdd:PTZ00441   98 RLGSgaSKDKEQALIIVKSLRKTYlpyGKTNMTDALLEVRKHLNDRVN-RENAI--QLVILMTDGIPnsKYRALEESRKL 174

                         170
                  ....*....|...
gi 507116137 1131 KDLGICVLVLGIG 1143
Cdd:PTZ00441  175 KDRNVKLAVIGIG 187
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 627-763 1.14e-05

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 48.09  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  627 ADIMFLVDSSWSIGNENFRKMKIF--MKNLLTKIQIGADKTQIGVVQFSDK--TKEEFQLNRYFTQQEISDaIDRMsLIN 702
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPSRLeaAKEVLSDFIDRRENDRIGLVVFAGAafTQAPLTLDRESLKELLED-IKIG-LAG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507116137  703 EGTLTGKALNFVGQYFTHSKGArlgaKKFLILITDGVAQDDVRDP---ARILRGKDVTIFSVGV 763
Cdd:cd01467    81 QGTAIGDAIGLAIKRLKNSEAK----ERVIVLLTDGENNAGEIDPataAELAKNKGVRIYTIGV 140
PHA03169 PHA03169
hypothetical protein; Provisional
 1478-1652 1.28e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 50.35  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1478 HGFPGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQnnnikgqkGSKGEQGRQGRSGQKGVQGSPSSRGSRGRE 1557
Cdd:PHA03169   66 HRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSP--------SGSAEELASGLSPENTSGSSPESPASHSPP 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1558 GQRGLRGVSGEPGNP---------GPTGTLGAEGLQGP---QGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKgstgrpgl 1625
Cdd:PHA03169  138 PSPPSHPGPHEPAPPeshnpspnqQPSSFLQPSHEDSPeepEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-------- 209

                         170       180
                  ....*....|....*....|....*...
gi 507116137 1626 lgKKGEPGLP-GDLGPVGQTGQRGRQGD 1652
Cdd:PHA03169  210 --EPGEPQSPtPQQAPSPNTQQAVEHED 235
VWA_2 pfam13519
von Willebrand factor type A domain;
237-345 1.46e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.13  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   237 LVFLVD--ESLGTGG----NLRHLQTFLENITSSMdvKENcmRLGLMSYSNSAKTISFLKSSttQSEFQQQIKNLSIQVG 310
Cdd:pfam13519    1 LVFVLDtsGSMRNGDygptRLEAAKDAVLALLKSL--PGD--RVGLVTFGDGPEVLIPLTKD--RAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 507116137   311 KSNTGAAIDQMRrdgfseSYGSRRAQGVPQIAVLV 345
Cdd:pfam13519   75 GTNLAAALQLAR------AALKHRRKNQPRRIVLI 103
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
813-967 2.23e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 47.61  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHM---INLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSnrSAIIENLRkrrdTGG 889
Cdd:COG4245     6 LPVYLLLDTSGSMSGEPIEALnegLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLE--DFQPPDLS----ASG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  890 NTYTAKALKHANALFTEEHG---SRIKQNVKQMLIVITDGESHDHDQLNDTAL---ELRNKGITIFAVGVG-KANQKELE 962
Cdd:COG4245    80 GTPLGAALELLLDLIERRVQkytAEGKGDWRPVVFLITDGEPTDSDWEAALQRlkdGEAAKKANIFAIGVGpDADTEVLK 159


                  ....*
gi 507116137  963 GMAGN 967
Cdd:COG4245   160 QLTDP 164
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1946-2128 3.20e-05

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: 48.01  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1946 FPNACIREAFLPEDSYMDVVFLIDNSRN-IAKDEFKAVKALVSSVIDNFniasdplisDSGDRIALLSYSpwessrrkmG 2024
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---------RPRDRVGLVAFG---------G 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2025 TVKTEFDFiTYDNQLLMK--NHIQTsfqqlnGEAT-IGRALLwTTENLFPETPYlRKHKVIFVVSAGENYERKEFVKMMA 2101
Cdd:COG1240   139 EAEVLLPL-TRDREALKRalDELPP------GGGTpLGDALA-LALELLKRADP-ARRKVIVLLTDGRDNAGRIDPLEAA 209

                         170       180
                  ....*....|....*....|....*....
gi 507116137 2102 LRAKCQGYVIFVISLGSTRKDD--MEELA 2128
Cdd:COG1240   210 ELAAAAGIRIYTIGVGTEAVDEglLREIA 238
VWA_2 pfam13519
von Willebrand factor type A domain;
1964-2084 1.32e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 43.43  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1964 VVFLIDNS-----RNIAKDEFKAVKALVSSVIDNFNiasdplisdsGDRIALLSYSpwessrrkmGTVKTEFDFITYDNQ 2038
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLP----------GDRVGLVTFG---------DGPEVLIPLTKDRAK 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 507116137  2039 LLMKNHiqtSFQQLNGEATIGRALLwTTENLFPETPYLRKHKVIFV 2084
Cdd:pfam13519   62 ILRALR---RLEPKGGGTNLAAALQ-LARAALKHRRKNQPRRIVLI 103
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1525-1729 1.88e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 46.53  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1525 GQKGSKGEQGRQGRSGQKGVQGSPSSRGSRGREGQRGLRGVSGEPGNPGPTgTLGAEGlqgpQGSQGNPGRKGEKGSQGQ 1604
Cdd:cd21118   125 GGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGPL-NYGTNS----QGAVAQPGYGTVRGNNQN 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1605 KGPQGSPGlMGAKGSTGRPGLLGKKGEPGLPGDLGPVGQtGQRGRQGDSGIPGYGQmGRKGVKGPRGfPGDAGQKGDIGN 1684
Cdd:cd21118   200 SGCTNPPP-SGSHESFSNSGGSSSSGSSGSQGSHGSNGQ-GSSGSSGGQGNGGNNG-SSSSNSGNSG-GSNGGSSGNSGS 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 507116137 1685 PGIPGGPGPKGFRGLALTVGLKGEEGSRGLPGPPGQRGIKGMAGQ 1729
Cdd:cd21118   276 GSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGG 320
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 441-611 2.22e-04

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 44.63  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  441 ADIHFLIDGSSSIQEKQFEQIKRFML--EVTEMFSIGPDKVRVGVVQYSDDTEVEFYIT-DYsndIDLRKAIFNIKQ-LT 516
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPSRLEAakEVLSDFIDRRENDRIGLVVFAGAAFTQAPLTlDR---ESLKELLEDIKIgLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  517 G-GTYTGKALDYILQIIKNgmKDRMSKVpcyLIVLTDGMSTDRVVEP--AKRL-RAEQITVHAVGIGAankielqEIAGK 592
Cdd:cd01467    80 GqGTAIGDAIGLAIKRLKN--SEAKERV---IVLLTDGENNAGEIDPatAAELaKNKGVRIYTIGVGK-------SGSGP 147

                         170
                  ....*....|....*....
gi 507116137  593 EERVSFGQNFDALKSIKNE 611
Cdd:cd01467   148 KPDGSTILDEDSLVEIADK 166
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1488-1659 3.34e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 45.76  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1488 GDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQnnnikGQKGSKGEQGRQGRSGQKgVQGSPSSRGSRGREGQRGLRGVSG 1567
Cdd:cd21118    38 GDAISHGIGEAVGQGAKEAASSGIQNALGQGH-----GEEGGSTLGSRGDVFEHR-LGEAARSLGNAGNEIGRQAEDIIR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1568 EPGNP--GPTGTLGAeglQGPQGSQGNPgrkgekGSQGQKGPQGspglmgakgsTGRPGLLGkkGEPGLPGDLGPVGQTG 1645
Cdd:cd21118   112 HGVDAvhNSWQGSGG---HGAYGSQGGP------GVQGHGIPGG----------TGGPWASG--GNYGTNSLGGSVGQGG 170

                         170       180
                  ....*....|....*....|.
gi 507116137 1646 QRG-------RQGDSGIPGYG 1659
Cdd:cd21118   171 NGGplnygtnSQGAVAQPGYG 191
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
847-980 3.49e-04

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 45.86  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  847 GRDRVQFGALKYSDQPnilfylntYSNRS-AIIENLRkrrdTGGNTYTAKALKHANALFtEEHGSRIKqnvkqMLIVITD 925
Cdd:COG4548   302 GRHRVRYYRIKDFDEP--------YDDAVrARIAGLE----PGYYTRMGAAIRHATALL-AAQPARRR-----LLLVLTD 363

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507116137  926 GESHDHDQ------LNDTA---LELRNKGITIFAVGVGKANQKELEGMAGNKNNTIyVDNFDKL 980
Cdd:COG4548   364 GKPNDIDVyegrygIEDTRqavREARRAGIHPFCITIDPEADDYLPRIFGRGGYTV-IDDVERL 426
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 445-593 3.71e-04

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: 43.42  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  445 FLIDGSSSIQEKQFEQIKRFMLEVTEMfsIGPDKvRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQlTGGTYTGKA 524
Cdd:cd01465     5 FVIDRSGSMDGPKLPLVKSALKLLVDQ--LRPDD-RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTA-GGSTAGGAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507116137  525 LDY-ILQIIKNGMKDRMSKVpcylIVLTDG---MSTDRVVEPAKRLRAEQ---ITVHAVGIGAA-NKIELQEIAGKE 593
Cdd:cd01465    81 IQLgYQEAQKHFVPGGVNRI----LLATDGdfnVGETDPDELARLVAQKResgITLSTLGFGDNyNEDLMEAIADAG 153
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 235-402 3.88e-04

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: 43.91  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  235 ADLVFLVDESLGTGGN-----LRHLQTFLENITSSMDVK--ENCMRLGLMSYSNSAKTIS-FLKSSTTQSEFQQQIKNLS 306
Cdd:cd01480     3 VDITFVLDSSESVGLQnfditKNFVKRVAERFLKDYYRKdpAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  307 IQVGKSNTGAAI----DQMRRDgfsesygsrRAQGVPQIAVLVT---HRPSDDEVHDAALNL-RLEDVNVFALSIQGANN 378
Cdd:cd01480    83 YIGGGTFTDCALkyatEQLLEG---------SHQKENKFLLVITdghSDGSPDGGIEKAVNEaDHLGIKIFFVAVGSQNE 153

                         170       180
                  ....*....|....*....|....
gi 507116137  379 TQLEEIVSYPPEQTISTlkSYADL 402
Cdd:cd01480   154 EPLSRIACDGKSALYRE--NFAEL 175
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 442-580 4.98e-04

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 42.72  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  442 DIHFLIDGSSSIQEKQFEQIKRFMLEVteMFSIGPDKVRVGVVQYSDdtevEFYITDYSNDIDLRKAIFNIK--QLTGGT 519
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAKAVALAL--LRIALAENRDTYLILFDS----EFQTKIVDKTDDLEEPVEFLSgvQLGGGT 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507116137  520 YTGKALDYILQIIKNGMKDRmskvpCYLIVLTDGM---STDRVVEPAKRLRAEQITVHAVGIGA 580
Cdd:cd01462    76 DINKALRYALELIERRDPRK-----ADIVLITDGYeggVSDELLREVELKRSRVARFVALALGD 134
VWA_2 pfam13519
von Willebrand factor type A domain;
1759-1871 5.30e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 41.51  E-value: 5.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  1759 LVFALDNSYDVTEESFNKTR-DIITSIVNDLnIRENNcpvGARVAMVSYNSGTSYLIRW-SDYNRKKQLLQQLsQIKYQD 1836
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLAL-LKSLP---GDRVGLVTFGDGPEVLIPLtKDRAKILRALRRL-EPKGGG 75

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 507116137  1837 TteprDVGNAMRFVTRNVFKRTyagANVRRVAVFF 1871
Cdd:pfam13519   76 T----NLAAALQLARAALKHRR---KNQPRRIVLI 103
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 813-984 5.44e-04

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: 43.43  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  813 LDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPN-ILFYLNTYSN-RSAIIENLR----KRRD 886
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKeIVSIRDFNSNdADDVIKRLEdfnyDDHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  887 TGGNTYTAKALK---HANALFTEEHGSRIKQnVKQMLIVITDGESH---------DHDQL----NDTALELRNKGITIFA 950
Cdd:cd01470    81 DKTGTNTAAALKkvyERMALEKVRNKEAFNE-TRHVIILFTDGKSNmggsplptvDKIKNlvykNNKSDNPREDYLDVYV 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 507116137  951 VGVGK-ANQKELEGMAGNKNN---TIYVDNFDKLKDVF 984
Cdd:cd01470   160 FGVGDdVNKEELNDLASKKDNerhFFKLKDYEDLQEVF 197
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 52-181 9.58e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 42.69  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   52 FINKMINSLPIEANKYRVALAQYSDE------FHSEfhLSTFKGR-SPMLNHLKKNFqFIGGSLQIGKALQEAHRTYFSa 124
Cdd:cd01473    25 FTEKIINNLNISKDKVHVGILLFAEKnrdvvpFSDE--ERYDKNElLKKINDLKNSY-RSGGETYIVEALKYGLKNYTK- 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507116137  125 piNGRDRKQFPPILVVLA----SAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMA 181
Cdd:cd01473   101 --HGNRRKDAPKVTMLFTdgndTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLA 159
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 443-590 1.67e-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: 41.94  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  443 IHFLIDGSSSIQEKQFEQ----IKRFMLEVTEMfSIGPDKVRVGVVQYSDDTEVEFYITDYSNdidlrkaiFNIKQLT-- 516
Cdd:cd01464     6 IYLLLDTSGSMAGEPIEAlnqgLQMLQSELRQD-PYALESVEISVITFDSAARVIVPLTPLES--------FQPPRLTas 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137  517 GGTYTGKALDYILQIIKNGMKD-RMSKVPCY---LIVLTDGMSTDRVVEPAKRLRAE---QITVHAVGIG-AANKIELQE 588
Cdd:cd01464    77 GGTSMGAALELALDCIDRRVQRyRADQKGDWrpwVFLLTDGEPTDDLTAAIERIKEArdsKGRIVACAVGpKADLDTLKQ 156


                  ..
gi 507116137  589 IA 590
Cdd:cd01464   157 IT 158
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 16-205 1.94e-03

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: 42.62  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   16 TLADQSPGPGPVYADVVFLVDSSDH-LGPKSFPFVKTFINKMINSLPIEAnkyRVALAQYSDEfhSE------FHLSTFK 88
Cdd:COG1240    80 ALAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGE--AEvllpltRDREALK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137   89 GRspmLNHLKknfqfIGGSLQIGKALQEAHRTYFSAPINGRdrkqfpPILVVL---ASAESEDEVEEASKALQKDGVKI- 164
Cdd:COG1240   155 RA---LDELP-----PGGGTPLGDALALALELLKRADPARR------KVIVLLtdgRDNAGRIDPLEAAELAAAAGIRIy 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 507116137  165 -ISVGVQKASEENLKAMAT----SHFHfnlrtIRDLSTFSQNMTQI 205
Cdd:COG1240   221 tIGVGTEAVDEGLLREIAEatggRYFR-----ADDLSELAAIYREI 261
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1756-1874 1.94e-03

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: 41.60  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1756 PTELVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENNCPV--GARVAMVSY-NSGTSYLIRWSDYNRKKQLLQQLSQI 1832
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPagSWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 507116137 1833 KYqdTTEPRDVGNAMRFVTRNVFKRTYAGANvrRVAVFFSNG 1874
Cdd:cd01480    82 EY--IGGGTFTDCALKYATEQLLEGSHQKEN--KFLLVITDG 119
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 2291-2467 2.55e-03

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: 40.85  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2291 DVAFLIDASQRVGsDEFKEVKAFITSVLDYFHIAPTPltstlgDRVAVLSYSPPGYMpnteecpvYLEFDLVTYNSIHQM 2370
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTA------TRVALITYSGRGRQ--------RVRFNLPKHNDGEEL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 2371 KHHLQDSQQLNGDVFIGHALQWTIDNVFVGTPnLRKN--KVIFVISAGETNSLDKDVLRnvSLRAKcQGYSIFVFSFG-- 2446
Cdd:cd01476    67 LEKVDNLRFIGGTTATGAAIEVALQQLDPSEG-RREGipKVVVVLTDGRSHDDPEKQAR--ILRAV-PNIETFAVGTGdp 142

                         170       180
                  ....*....|....*....|.
gi 507116137 2447 PKHNDKELEELASHPldHHLV 2467
Cdd:cd01476   143 GTVDTEELHSITGNE--DHIF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1758-1877 2.70e-03

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: 40.85  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1758 ELVFALDNSyDVTEESFNKTRDIITSIVNDLNIRenncPVGARVAMVSYNSGTSYLIRW--SDYNRKKQLLQQLSQIKY- 1834
Cdd:cd01476     2 DLLFVLDSS-GSVRGKFEKYKKYIERIVEGLEIG----PTATRVALITYSGRGRQRVRFnlPKHNDGEELLEKVDNLRFi 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 507116137 1835 QDTTEprdVGNAMRFVTRNVFKRTYAGANVRRVAVFFSNGQTA 1877
Cdd:cd01476    77 GGTTA---TGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSH 116
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1395-1574 7.12e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1395 GIPGPHGtRGLQAMKGSQGLKGSRGHRGedgnpGVRGDTGPQGDkgiagcpgawGQKGLKGFSGpkgghgddgidgldGE 1474
Cdd:cd21118   227 GSQGSHG-SNGQGSSGSSGGQGNGGNNG-----SSSSNSGNSGG----------SNGGSSGNSG--------------SG 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507116137 1475 EGCHGFPGIKGEKGDPGSQGSPGSRGAPGQygekgfpgDPGNPGQNNnikGQKGSKGEQGRQGRSGQKGVQGspssrGSR 1554
Cdd:cd21118   277 SGGSSSGGSNGWGGSSSSGGSGGSGGGNKP--------ECNNPGNDV---RMAGGGGSQGSKESSGSHGSNG-----GNG 340

                         170       180
                  ....*....|....*....|
gi 507116137 1555 GREGQRGLrGVSGEPGNPGP 1574
Cdd:cd21118   341 QAEAVGGL-NTLNSDASTLP 359
 
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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