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Conserved domains on  [gi|1918142617|gb|QOP77360|]
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von Willebrand factor, partial [Stylodipus telum]

Protein Classification

VWA_N2 and vWFA_subfamily_ECM domain-containing protein( domain architecture ID 11069199)

VWA_N2 and vWFA_subfamily_ECM domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 25-146 8.98e-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: 85.42  E-value: 8.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSQVA 104
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1918142617 105 STSEVLKYTLFQIF-GKVDRPEASRVALLLTASQ-----EPPRMARNL 146
Cdd:cd01450    81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGRsddggDPKEAAAKL 128
VWA_N2 super family cl24671
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 4-25 9.40e-10

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


The actual alignment was detected with superfamily member pfam16164:

Pssm-ID: 465038  Cd Length: 79  Bit Score: 52.29  E-value: 9.40e-10
                          10        20
                  ....*....|....*....|..
gi 1918142617   4 TTPYVEDTPEPPLHDFHCSKLL 25
Cdd:pfam16164  58 TTPYVEDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 25-146 8.98e-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: 85.42  E-value: 8.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSQVA 104
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1918142617 105 STSEVLKYTLFQIF-GKVDRPEASRVALLLTASQ-----EPPRMARNL 146
Cdd:cd01450    81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGRsddggDPKEAAAKL 128
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 26-148 2.07e-17

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: 74.41  E-value: 2.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617   26 DLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSQVAS 105
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1918142617  106 TSEVLKYTLFQIFGKVD--RPEASRVALLLTA--SQEPPRMARNLVR 148
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILITDgeSNDGPKDLLKAAK 127
VWA pfam00092
von Willebrand factor type A domain;
26-134 2.96e-15

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.84  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  26 DLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYhdGSHAYIE--LRARKRPSELRHLAGQVKYVGSQV 103
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1918142617 104 ASTSEVLKYTLFQIFGKV--DRPEASRVALLLT 134
Cdd:pfam00092  79 TNTGKALKYALENLFSSAagARPGAPKVVVLLT 111
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 4-25 9.40e-10

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 52.29  E-value: 9.40e-10
                          10        20
                  ....*....|....*....|..
gi 1918142617   4 TTPYVEDTPEPPLHDFHCSKLL 25
Cdd:pfam16164  58 TTPYVEDTPEPPLHDFYCSKLL 79
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 25-146 8.98e-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: 85.42  E-value: 8.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSQVA 104
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1918142617 105 STSEVLKYTLFQIF-GKVDRPEASRVALLLTASQ-----EPPRMARNL 146
Cdd:cd01450    81 NTGKALQYALEQLFsESNARENVPKVIIVLTDGRsddggDPKEAAAKL 128
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 26-148 2.07e-17

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: 74.41  E-value: 2.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617   26 DLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSQVAS 105
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1918142617  106 TSEVLKYTLFQIFGKVD--RPEASRVALLLTA--SQEPPRMARNLVR 148
Cdd:smart00327  81 LGAALQYALENLFSKSAgsRRGAPKVVILITDgeSNDGPKDLLKAAK 127
VWA pfam00092
von Willebrand factor type A domain;
26-134 2.96e-15

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 68.84  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  26 DLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYhdGSHAYIE--LRARKRPSELRHLAGQVKYVGSQV 103
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQY--SSDVRTEfpLNDYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1918142617 104 ASTSEVLKYTLFQIFGKV--DRPEASRVALLLT 134
Cdd:pfam00092  79 TNTGKALKYALENLFSSAagARPGAPKVVVLLT 111
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 26-148 1.69e-13

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: 63.79  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  26 DLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEY-HDGSHAYIELRARKRPSELRHLAgQVKYVGSQVA 104
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYsDDPRTEFYLNTYRSKDDVLEAVK-NLRYIGGGTN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1918142617 105 sTSEVLKYTLFQIFGKVDRPEAS--RVALLLTASQEP---PRMARNLVR 148
Cdd:cd01472    81 -TGKALKYVRENLFTEASGSREGvpKVLVVITDGKSQddvEEPAVELKQ 128
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 26-146 1.16e-11

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: 59.22  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  26 DLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRA-RKRPSELRHLAgQVKYVGSQvA 104
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAyTSKEDVLAAIK-NLPYKGGN-T 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1918142617 105 STSEVLKYTLFQIF--GKVDRPEASRVALLLT--ASQ----EPPRMARNL 146
Cdd:cd01482    80 RTGKALTHVREKNFtpDAGARPGVPKVVILITdgKSQddveLPARVLRNL 129
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 25-153 4.16e-11

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: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSQVA 104
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1918142617 105 STSEVLKYTLfQIFGKVDRPEASRVALLLT--ASQEPPRMARNLVRYVQGL 153
Cdd:cd00198    81 NIGAALRLAL-ELLKSAKRPNARRVIILLTdgEPNDGPELLAEAARELRKL 130
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 25-134 5.45e-10

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: 55.47  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVgSQVA 104
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1918142617 105 STSEVLKYTLFQIFGKVD--RPEA---SRVALLLT 134
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEgaRPGServPRVGIVVT 116
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 26-137 5.74e-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: 54.64  E-value: 5.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  26 DLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSQVAS 105
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1918142617 106 TSEVLKYTLFQIFgkvDRPEASRVA-------LLLTASQ 137
Cdd:cd01481    82 TGSALDYVVKNLF---TKSAGSRIEegvpqflVLITGGK 117
VWA_N2 pfam16164
VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to ...
 4-25 9.40e-10

VWA N-terminal; This domain is found in von Willebrand factor proteins, where it is found to the N-terminus of the first VWA domain (pfam00092).


Pssm-ID: 465038  Cd Length: 79  Bit Score: 52.29  E-value: 9.40e-10
                          10        20
                  ....*....|....*....|..
gi 1918142617   4 TTPYVEDTPEPPLHDFHCSKLL 25
Cdd:pfam16164  58 TTPYVEDTPEPPLHDFYCSKLL 79
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 25-134 6.91e-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: 46.58  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRARKRPSELRHLAGQVKYVGSqVA 104
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1918142617 105 STSEVLKYTLFQIF--GKVDRPEASRVALLLT 134
Cdd:cd01469    80 NTATAIQYVVTELFseSNGARKDATKVLVVIT 111
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 25-134 1.59e-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: 40.06  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEAEFEVLKAFVVSAMERLHISQKR------IRVAVVEY-HDGSHAYIELRARKRPSELRHLAGQVK 97
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagsWRVGVVQYsDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1918142617  98 YVGsQVASTSEVLKYTLFQIFgKVDRPEASRVALLLT 134
Cdd:cd01480    83 YIG-GGTFTDCALKYATEQLL-EGSHQKENKFLLVIT 117
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 25-148 2.88e-04

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: 39.29  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918142617  25 LDLVFLLDGSSRLSEA-EFEVLKAFVVSAMERLHISQKRIRVAVVEYHDGSHAYIELRA--RKRPSELRHLAGQVKYVGS 101
Cdd:cd01471     1 LDLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpnSTNKDLALNAIRALLSLYY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1918142617 102 QVAST------SEVLKYtLFQifGKVDRPEASRVALLLT--ASQEPPRmARNLVR 148
Cdd:cd01471    81 PNGSTnttsalLVVEKH-LFD--TRGNRENAPQLVIIMTdgIPDSKFR-TLKEAR 131
 
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.
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