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Conserved domains on  [gi|40068485|ref|NP_073745|]
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von Willebrand factor A domain-containing protein 1 isoform 1 precursor [Homo sapiens]

Protein Classification

fibronectin type III domain-containing protein; VWA domain-containing protein( domain architecture ID 10208343)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain; VWA (von Willebrand factor type A) domain-containing protein with a Flp pilus assembly protein TadE/TadG-like domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 34-194 8.55e-40

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 cd01482:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 164  Bit Score: 140.50  E-value: 8.55e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHT 113
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 114 GLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLHFV 193
Cdd:cd01482  82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                .
gi 40068485 194 D 194
Cdd:cd01482 162 A 162
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 335-416 1.22e-10

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.89  E-value: 1.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 335 PERIVISHARPRSLRVSW-APALGSAAALGYHVQFGPLRGGEAQRVEVPAGRNCT-TLQGLAPGTAYLVTVTaAFRSGRE 412
Cdd:cd00063   4 PTNLRVTDVTSTSVTLSWtPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVR-AVNGGGE 82


                ....
gi 40068485 413 SALS 416
Cdd:cd00063  83 SPPS 86
fn3 pfam00041
Fibronectin type III domain;
215-311 1.05e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485   215 PQQLHATEITSSGFRLAWPPLLTADSGY--YVLELVPSAQPGAARRQQLPGNATDWIWAGLDPDTDYDValvpesnvrll 292
Cdd:pfam00041   3 PSNLTVTDVTSTSLTVSWTPPPDGNGPItgYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEV----------- 71

                          90
                  ....*....|....*....
gi 40068485   293 rpqilRVRTRPGEAGPGAS 311
Cdd:pfam00041  72 -----RVQAVNGGGEGPPS 85
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 34-194 8.55e-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: 140.50  E-value: 8.55e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHT 113
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 114 GLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLHFV 193
Cdd:cd01482  82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                .
gi 40068485 194 D 194
Cdd:cd01482 162 A 162
VWA pfam00092
von Willebrand factor type A domain;
34-204 7.38e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 138.18  E-value: 7.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485    34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRA-SAQRMGDTH 112
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485   113 TGLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDP-VGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLH 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 40068485   192 FV-DVDDLHIIVQE 204
Cdd:pfam00092 161 TVsDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-205 5.49e-33

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: 122.56  E-value: 5.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485     34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRA-SAQRMGDTH 112
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485    113 TGLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGP---PMQELKDLGVTVFIVSTGRG-NFLELSAAASAPAEk 188
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDllkAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGG- 159

                          170
                   ....*....|....*..
gi 40068485    189 hLHFVDVDDLHIIVQEL 205
Cdd:smart00327 160 -VYVFLPELLDLLIDLL 175
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 335-416 1.22e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.89  E-value: 1.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 335 PERIVISHARPRSLRVSW-APALGSAAALGYHVQFGPLRGGEAQRVEVPAGRNCT-TLQGLAPGTAYLVTVTaAFRSGRE 412
Cdd:cd00063   4 PTNLRVTDVTSTSVTLSWtPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVR-AVNGGGE 82


                ....
gi 40068485 413 SALS 416
Cdd:cd00063  83 SPPS 86
fn3 pfam00041
Fibronectin type III domain;
335-405 6.39e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 6.39e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40068485   335 PERIVISHARPRSLRVSW-APALGSAAALGYHVQFGPLRGGEA-QRVEVPAGRNCTTLQGLAPGTAYLVTVTA 405
Cdd:pfam00041   3 PSNLTVTDVTSTSLTVSWtPPPDGNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 335-411 3.67e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 50.69  E-value: 3.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485    335 PERIVISHARPRSLRVSWAPALGSAAA---LGYHVQFGPlRGGEAQRVEVPAGRNCTTLQGLAPGTAYLVTVTAAFRSGR 411
Cdd:smart00060   4 PSNLRVTDVTSTSVTLSWEPPPDDGITgyiVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 22-206 2.00e-07

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: 52.25  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  22 AERGPPASAPRGDLMFLLDSSASVSHYE-FSRVREFVGQLVAPLPLGTgalRASLVHVGSRPYTEFPFGqhSSGEAAQDA 100
Cdd:COG1240  82 APLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLT--RDREALKRA 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 101 VRaSAQRMGDTHTGLALVYAKEQLfaeaSGARPGVPKVLVWVTDGGSSDPVGPPMQ---ELKDLGVTVFIVSTG-----R 172
Cdd:COG1240 157 LD-ELPPGGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEaaeLAAAAGIRIYTIGVGteavdE 231

                       170       180       190
                ....*....|....*....|....*....|....
gi 40068485 173 GNFLELSAAASApaeKHLHFVDVDDLHIIVQELR 206
Cdd:COG1240 232 GLLREIAEATGG---RYFRADDLSELAAIYREID 262
fn3 pfam00041
Fibronectin type III domain;
215-311 1.05e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485   215 PQQLHATEITSSGFRLAWPPLLTADSGY--YVLELVPSAQPGAARRQQLPGNATDWIWAGLDPDTDYDValvpesnvrll 292
Cdd:pfam00041   3 PSNLTVTDVTSTSLTVSWTPPPDGNGPItgYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEV----------- 71

                          90
                  ....*....|....*....
gi 40068485   293 rpqilRVRTRPGEAGPGAS 311
Cdd:pfam00041  72 -----RVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 215-289 6.77e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.36  E-value: 6.77e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40068485    215 PQQLHATEITSSGFRLAWPPLLTADSGYYVLELVPSAQPGAARRQQLPGNATD---WIWaGLDPDTDYDVALVPESNV 289
Cdd:smart00060   4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSStsyTLT-GLKPGTEYEFRVRAVNGA 80
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 34-194 8.55e-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: 140.50  E-value: 8.55e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHT 113
Cdd:cd01482   2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 114 GLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLHFV 193
Cdd:cd01482  82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                .
gi 40068485 194 D 194
Cdd:cd01482 162 A 162
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 34-194 9.68e-40

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: 140.06  E-value: 9.68e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHT 113
Cdd:cd01472   2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 114 GLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLHFV 193
Cdd:cd01472  82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFNV 161


                .
gi 40068485 194 D 194
Cdd:cd01472 162 A 162
VWA pfam00092
von Willebrand factor type A domain;
34-204 7.38e-39

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 138.18  E-value: 7.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485    34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRA-SAQRMGDTH 112
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485   113 TGLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDP-VGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHLH 191
Cdd:pfam00092  81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                         170
                  ....*....|....
gi 40068485   192 FV-DVDDLHIIVQE 204
Cdd:pfam00092 161 TVsDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 34-190 1.15e-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: 129.33  E-value: 1.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGD-TH 112
Cdd:cd01450   2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgTN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 113 TGLALVYAKEQLFAEaSGARPGVPKVLVWVTDGGSSDPVGP--PMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHL 190
Cdd:cd01450  82 TGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDGGDPkeAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERHV 160
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 34-193 4.39e-35

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: 129.81  E-value: 4.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHT 113
Cdd:cd01475   4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 114 GLALVYAKEQLFAEASGARPG---VPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAPAEKHL 190
Cdd:cd01475  84 GLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADHV 163


                ...
gi 40068485 191 HFV 193
Cdd:cd01475 164 FYV 166
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-205 5.49e-33

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: 122.56  E-value: 5.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485     34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRA-SAQRMGDTH 112
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485    113 TGLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSDPVGP---PMQELKDLGVTVFIVSTGRG-NFLELSAAASAPAEk 188
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDllkAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGG- 159

                          170
                   ....*....|....*..
gi 40068485    189 hLHFVDVDDLHIIVQEL 205
Cdd:smart00327 160 -VYVFLPELLDLLIDLL 175
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 34-197 1.15e-27

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: 108.21  E-value: 1.15e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMGDTHT 113
Cdd:cd01469   2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 114 GLALVYAKEQLFAEASGARPGVPKVLVWVTDGGSSD-PVGPP-MQELKDLGVTVFIVSTG----RGNFL-ELSAAASAPA 186
Cdd:cd01469  82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdPLLKDvIPQAEREGIIRYAIGVGghfqRENSReELKTIASKPP 161

                       170
                ....*....|.
gi 40068485 187 EKhlHFVDVDD 197
Cdd:cd01469 162 EE--HFFNVTD 170
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 34-185 5.33e-23

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: 95.08  E-value: 5.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRMG-DTH 112
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQLN 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40068485 113 TGLALVYAKEQLFAEASGAR--PGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTVFIVSTGRGNFLELSAAASAP 185
Cdd:cd01481  82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP 156
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 34-189 8.55e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 91.47  E-value: 8.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRA-SAQRMGDTH 112
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAlKKGLGGGTN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 113 TGLALVYAKEQLFAEasgARPGVPKVLVWVTDGGSSDPVGPPM---QELKDLGVTVFIVSTG-RGNFLELSAAASAPAEK 188
Cdd:cd00198  82 IGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGPELLAeaaRELRKLGITVYTIGIGdDANEDELKEIADKTTGG 158


                .
gi 40068485 189 H 189
Cdd:cd00198 159 A 159
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 34-189 2.07e-17

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: 79.37  E-value: 2.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHyEFSRVREFVGQLVAPLPLGTGALRASLVHVGS--RPYTEFPFGQHSSGEAAQDAVRASAQRMGDT 111
Cdd:cd01476   2 DLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEIGPTATRVALITYSGrgRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 112 HTGLALVYAKEQLfAEASGARPGVPKVLVWVTDGGSSDPVGPPMQELKDL-GVTVFIVSTG-RGNFLELSAAASAPAEKH 189
Cdd:cd01476  81 ATGAAIEVALQQL-DPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdPGTVDTEELHSITGNEDH 159
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 34-174 2.17e-13

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 68.18  E-value: 2.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHYEFSRVREFVGQLV------APLPLGTGALRASLVHVGSRPYTEFPFGQHSSGeaaQDAVRASAQR 107
Cdd:cd01480   4 DITFVLDSSESVGLQNFDITKNFVKRVAerflkdYYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRN---YTSLKEAVDN 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40068485 108 M----GDTHTGLALVYAKEQLFaEASGArpGVPKVLVWVTDGGS--SDPVGPPM--QELKDLGVTVFIVSTGRGN 174
Cdd:cd01480  81 LeyigGGTFTDCALKYATEQLL-EGSHQ--KENKFLLVITDGHSdgSPDGGIEKavNEADHLGIKIFFVAVGSQN 152
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 34-173 3.79e-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: 64.71  E-value: 3.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSHY-EFSRVREFVGQLVAPLPLGTGALRASLVHVGSRPYTEFPFGQHSS--GEAAQDAVRAsAQRM-- 108
Cdd:cd01471   2 DLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRA-LLSLyy 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40068485 109 --GDTHTGLALVYAKEQLFaEASGARPGVPKVLVWVTDGGSSDPVGP--PMQELKDLGVTVFIVSTGRG 173
Cdd:cd01471  81 pnGSTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGVIIAVLGVGQG 148
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 335-416 1.22e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 57.89  E-value: 1.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 335 PERIVISHARPRSLRVSW-APALGSAAALGYHVQFGPLRGGEAQRVEVPAGRNCT-TLQGLAPGTAYLVTVTaAFRSGRE 412
Cdd:cd00063   4 PTNLRVTDVTSTSVTLSWtPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVR-AVNGGGE 82


                ....
gi 40068485 413 SALS 416
Cdd:cd00063  83 SPPS 86
fn3 pfam00041
Fibronectin type III domain;
335-405 6.39e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 6.39e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40068485   335 PERIVISHARPRSLRVSW-APALGSAAALGYHVQFGPLRGGEA-QRVEVPAGRNCTTLQGLAPGTAYLVTVTA 405
Cdd:pfam00041   3 PSNLTVTDVTSTSLTVSWtPPPDGNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
VWA_2 pfam13519
von Willebrand factor type A domain;
35-142 2.16e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.61  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485    35 LMFLLDSSASVSHY-----EFSRVREFVGQLVAPLPLGtgalRASLVHVGSRPYTEFPFGqhSSGEAAQDAVRASAQRMG 109
Cdd:pfam13519   1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 40068485   110 DTHTGLALVYAKEQLFAEasgaRPGVPKVLVWV 142
Cdd:pfam13519  75 GTNLAAALQLARAALKHR----RKNQPRRIVLI 103
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 335-411 3.67e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 50.69  E-value: 3.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485    335 PERIVISHARPRSLRVSWAPALGSAAA---LGYHVQFGPlRGGEAQRVEVPAGRNCTTLQGLAPGTAYLVTVTAAFRSGR 411
Cdd:smart00060   4 PSNLRVTDVTSTSVTLSWEPPPDDGITgyiVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 22-206 2.00e-07

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: 52.25  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  22 AERGPPASAPRGDLMFLLDSSASVSHYE-FSRVREFVGQLVAPLPLGTgalRASLVHVGSRPYTEFPFGqhSSGEAAQDA 100
Cdd:COG1240  82 APLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLT--RDREALKRA 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 101 VRaSAQRMGDTHTGLALVYAKEQLfaeaSGARPGVPKVLVWVTDGGSSDPVGPPMQ---ELKDLGVTVFIVSTG-----R 172
Cdd:COG1240 157 LD-ELPPGGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEaaeLAAAAGIRIYTIGVGteavdE 231

                       170       180       190
                ....*....|....*....|....*....|....
gi 40068485 173 GNFLELSAAASApaeKHLHFVDVDDLHIIVQELR 206
Cdd:COG1240 232 GLLREIAEATGG---RYFRADDLSELAAIYREID 262
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 34-194 2.29e-07

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: 50.97  E-value: 2.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  34 DLMFLLDSSASVSH-----YEFsrVREFVGQLVAPlplgtgALRASLVHVGSRPYTEFPFGQHSSGEAAQDAVRASAQRM 108
Cdd:cd01474   6 DLYFVLDKSGSVAAnwieiYDF--VEQLVDRFNSP------GLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 109 GDTHTGLALVYAKEQLFAEASGARPgVPKVLVWVTDGG-SSDPVGPPMQE---LKDLGVTVFIVstGRGNFLELSAAASA 184
Cdd:cd01474  78 GQTYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQlLLNGHKYPEHEaklSRKLGAIVYCV--GVTDFLKSQLINIA 154

                       170
                ....*....|
gi 40068485 185 PAEKHLHFVD 194
Cdd:cd01474 155 DSKEYVFPVT 164
fn3 pfam00041
Fibronectin type III domain;
215-311 1.05e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485   215 PQQLHATEITSSGFRLAWPPLLTADSGY--YVLELVPSAQPGAARRQQLPGNATDWIWAGLDPDTDYDValvpesnvrll 292
Cdd:pfam00041   3 PSNLTVTDVTSTSLTVSWTPPPDGNGPItgYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEV----------- 71

                          90
                  ....*....|....*....
gi 40068485   293 rpqilRVRTRPGEAGPGAS 311
Cdd:pfam00041  72 -----RVQAVNGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
215-419 4.69e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 42.68  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 215 PQQLHATEITSSGFRLAWPPLLTADSGYYVLELVPSAQPGAARRQQLPGNA-TDwiwAGLDPDTDYDValvpesnvrllr 293
Cdd:COG3401 236 PTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSyTD---TGLTNGTTYYY------------ 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 294 pqilRVRTRpgeagpGASGPESGAGPAPTQLAALPAPeeAGPERIVISHARPRSLRVSWAPALGSAAAlGYHVQFGPLRG 373
Cdd:COG3401 301 ----RVTAV------DAAGNESAPSNVVSVTTDLTPP--AAPSGLTATAVGSSSITLSWTASSDADVT-GYNVYRSTSGG 367

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 40068485 374 GEAQRV-EVPAGRNCTTLqGLAPGTAYLVTVTAAFRSGRESALSAKA 419
Cdd:COG3401 368 GTYTKIaETVTTTSYTDT-GLTPGTTYYYKVTAVDAAGNESAPSEEV 413
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 215-289 6.77e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 38.36  E-value: 6.77e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40068485    215 PQQLHATEITSSGFRLAWPPLLTADSGYYVLELVPSAQPGAARRQQLPGNATD---WIWaGLDPDTDYDVALVPESNV 289
Cdd:smart00060   4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSStsyTLT-GLKPGTEYEFRVRAVNGA 80
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 22-183 3.34e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 39.28  E-value: 3.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485  22 AERGPPASAPRGDLMFLLDSSASVSHYEFSRVREFVGQLVAplpLGTGALRASLVHVGSRPYTEFPFGQHSSGEAAQDAV 101
Cdd:COG2425 108 APASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLR---ALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFL 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485 102 RASaQRMGDTHTGLALVYAKEQLfaEASGARpgvPKVLVWVTDGGSSDPVGPPMQEL--KDLGVTVFIVSTGRGNFLELS 179
Cdd:COG2425 185 SGL-FAGGGTDIAPALRAALELL--EEPDYR---NADIVLITDGEAGVSPEELLREVraKESGVRLFTVAIGDAGNPGLL 258


                ....
gi 40068485 180 AAAS 183
Cdd:COG2425 259 EALA 262
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 335-406 5.19e-03

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 36.23  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40068485   335 PERIVIS-HARPRSLRVSWAPAlgsAAALGYHVQFGPLRGGEAQRVE-----------VPAGRNCTTLQGLAPGTAYLVT 402
Cdd:pfam16656   1 PEQVHLSlTGDSTSMTVSWVTP---SAVTSPVVQYGTSSSALTSTATatsstyttgdgGTGYIHRATLTGLEPGTTYYYR 77


                  ....
gi 40068485   403 VTAA 406
Cdd:pfam16656  78 VGDD 81
 
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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