NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568986780|ref|XP_006518647|]
View 

inter-alpha-trypsin inhibitor heavy chain H1 isoform X1 [Mus musculus]

Protein Classification

VWA domain-containing protein( domain architecture ID 10106957)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 562-748 8.65e-88

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


:

Pssm-ID: 461981  Cd Length: 189  Bit Score: 274.85  E-value: 8.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  562 DTGFTVNGQLIGNKASSPG-QHESTYFGRLGISSPTSDFQLEVTPQNITLNPSSSGSMFSWRDQAVLQKDGVVVTINKKR 640
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGShKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  641 NLVVSVDDGATFEIVLHRTWKGSAVHQDFLGFYVLDSFRMSARTKGLLGQFFSPLDFEVFDLHPGSDPTKTDATMVVKNR 720
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*...
gi 568986780  721 QLTVTRGLQKDYSKDPRHGAEVPCWFVH 748
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVH 188
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-328 2.89e-71

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


:

Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 230.56  E-value: 2.89e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 147 MSKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSLAGAT 226
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 227 NLNGGLLRGIEILNKAQGShpelsspASILIMLTDGEptegETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 306
Cdd:cd01461   81 NMNDALEAALELLNSSPGS-------VPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 568986780 307 TENNGWAQRIYEDHDATQQLQG 328
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT_2 super family cl02699
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 1-24 8.06e-06

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


The actual alignment was detected with superfamily member smart00609:

Pssm-ID: 470654 [Multi-domain]  Cd Length: 130  Bit Score: 45.81  E-value: 8.06e-06
                           10        20
                   ....*....|....*....|....
gi 568986780     1 MEQFTIHITVGAQSKATFRLTYEE 24
Cdd:smart00609 107 MEQFTVSVNVAPGSKVTFELTYEE 130
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 562-748 8.65e-88

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 274.85  E-value: 8.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  562 DTGFTVNGQLIGNKASSPG-QHESTYFGRLGISSPTSDFQLEVTPQNITLNPSSSGSMFSWRDQAVLQKDGVVVTINKKR 640
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGShKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  641 NLVVSVDDGATFEIVLHRTWKGSAVHQDFLGFYVLDSFRMSARTKGLLGQFFSPLDFEVFDLHPGSDPTKTDATMVVKNR 720
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*...
gi 568986780  721 QLTVTRGLQKDYSKDPRHGAEVPCWFVH 748
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVH 188
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-328 2.89e-71

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 230.56  E-value: 2.89e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 147 MSKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSLAGAT 226
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 227 NLNGGLLRGIEILNKAQGShpelsspASILIMLTDGEptegETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 306
Cdd:cd01461   81 NMNDALEAALELLNSSPGS-------VPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 568986780 307 TENNGWAQRIYEDHDATQQLQG 328
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 149-349 4.40e-36

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 137.93  E-value: 4.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 149 KNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQswkgSLVPA-SNANLQAAQDFVRRFSLAGATN 227
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR----VLLPPtPATDRAKILAAIDRLQAGGGTA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 228 LNGGLLRGIEILNKAQGSHpelssPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMST 307
Cdd:COG2304  168 LGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAD 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568986780 308 ENNGWAQRIYEDHDATQQLQGFYNQVANPLLTDVELQYPQDA 349
Cdd:COG2304  243 AGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-311 1.24e-24

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: 101.38  E-value: 1.24e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780   150 NLVFVIDISGSMEGQKVRQTKEALLKILEDMR---PVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFsLAGAT 226
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK-LGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780   227 NLNGGLLRGIEILNKAQGSHPElsSPASILIMLTDGEPTEGETDrsqILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 306
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRR--GAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154


                   ....*
gi 568986780   307 TENNG 311
Cdd:smart00327 155 SAPGG 159
VWA pfam00092
von Willebrand factor type A domain;
150-332 2.09e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 89.26  E-value: 2.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  150 NLVFVIDISGSMEGQKVRQTKEALLKILEDM---RPVDNFDLVLFGSKVQSWKgSLvpASNANLQAAQDFVRRFSLA--G 224
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEF-PL--NDYSSKEELLSAVDNLRYLggG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  225 ATNLNGGLLRGIEILNKAQGSHPELSSpaSILIMLTDGEPTEGEtdrsqILKNVRNAIRGRFPLYNLGFGHDlDFSFLEV 304
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGARPGAP--KVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNA-DDEELRK 149

                         170       180
                  ....*....|....*....|....*...
gi 568986780  305 MSTENNgwAQRIYEDHDATqQLQGFYNQ 332
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-24 8.06e-06

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 45.81  E-value: 8.06e-06
                           10        20
                   ....*....|....*....|....
gi 568986780     1 MEQFTIHITVGAQSKATFRLTYEE 24
Cdd:smart00609 107 MEQFTVSVNVAPGSKVTFELTYEE 130
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 562-748 8.65e-88

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 274.85  E-value: 8.65e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  562 DTGFTVNGQLIGNKASSPG-QHESTYFGRLGISSPTSDFQLEVTPQNITLNPSSSGSMFSWRDQAVLQKDGVVVTINKKR 640
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGShKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  641 NLVVSVDDGATFEIVLHRTWKGSAVHQDFLGFYVLDSFRMSARTKGLLGQFFSPLDFEVFDLHPGSDPTKTDATMVVKNR 720
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*...
gi 568986780  721 QLTVTRGLQKDYSKDPRHGAEVPCWFVH 748
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVH 188
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-328 2.89e-71

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 230.56  E-value: 2.89e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 147 MSKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSLAGAT 226
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 227 NLNGGLLRGIEILNKAQGShpelsspASILIMLTDGEptegETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 306
Cdd:cd01461   81 NMNDALEAALELLNSSPGS-------VPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 568986780 307 TENNGWAQRIYEDHDATQQLQG 328
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 149-349 4.40e-36

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 137.93  E-value: 4.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 149 KNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQswkgSLVPA-SNANLQAAQDFVRRFSLAGATN 227
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR----VLLPPtPATDRAKILAAIDRLQAGGGTA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 228 LNGGLLRGIEILNKAQGSHpelssPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMST 307
Cdd:COG2304  168 LGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAD 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568986780 308 ENNGWAQRIYEDHDATQQLQGFYNQVANPLLTDVELQYPQDA 349
Cdd:COG2304  243 AGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-311 1.24e-24

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: 101.38  E-value: 1.24e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780   150 NLVFVIDISGSMEGQKVRQTKEALLKILEDMR---PVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFsLAGAT 226
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYK-LGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780   227 NLNGGLLRGIEILNKAQGSHPElsSPASILIMLTDGEPTEGETDrsqILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 306
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRR--GAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154


                   ....*
gi 568986780   307 TENNG 311
Cdd:smart00327 155 SAPGG 159
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 140-306 2.19e-23

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 100.52  E-value: 2.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 140 APKNLTNMSKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQSwkgSLVPASNANLQAAQDFVRR 219
Cdd:COG2425  110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 220 FSLAGATNLNGGLLRGIEILNKAQGshpelssPASILIMLTDGEPTEGETDrsqILKNVRNAiRGRFPLYNLGFGHDLDF 299
Cdd:COG2425  187 LFAGGGTDIAPALRAALELLEEPDY-------RNADIVLITDGEAGVSPEE---LLREVRAK-ESGVRLFTVAIGDAGNP 255


                 ....*..
gi 568986780 300 SFLEVMS 306
Cdd:COG2425  256 GLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-311 1.79e-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: 94.55  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 150 NLVFVIDISGSMEGQKVRQTKEALLKILEDMRPV---DNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVrRFSLAGAT 226
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAL-KKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 227 NLNGGLLRGIEILNKAQGSHPElsspaSILIMLTDGEPTEGETDRSQILKNVRNAirgRFPLYNLGFGHDLDFSFLEVMS 306
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNAR-----RVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                 ....*
gi 568986780 307 TENNG 311
Cdd:cd00198  153 DKTTG 157
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 150-334 1.52e-21

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: 95.01  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 150 NLVFVIDISGSMEGQ-KVRQTKEALLKILEDMRPVDNFDLVLFGSKVQswkgSLVPASNaNLQAAQDFVRRFSLAGATNL 228
Cdd:COG1240   94 DVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE----VLLPLTR-DREALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 229 NGGLLRGIEILNKAQgshpelSSPASILIMLTDGEPTEGETDRSQILKNVRNAirgRFPLYNLGFGHD-LDFSFLEVMST 307
Cdd:COG1240  169 GDALALALELLKRAD------PARRKVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGTEaVDEGLLREIAE 239

                        170       180
                 ....*....|....*....|....*..
gi 568986780 308 ENNGWAQRIyedhDATQQLQGFYNQVA 334
Cdd:COG1240  240 ATGGRYFRA----DDLSELAAIYREID 262
VWA pfam00092
von Willebrand factor type A domain;
150-332 2.09e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 89.26  E-value: 2.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  150 NLVFVIDISGSMEGQKVRQTKEALLKILEDM---RPVDNFDLVLFGSKVQSWKgSLvpASNANLQAAQDFVRRFSLA--G 224
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEF-PL--NDYSSKEELLSAVDNLRYLggG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  225 ATNLNGGLLRGIEILNKAQGSHPELSSpaSILIMLTDGEPTEGEtdrsqILKNVRNAIRGRFPLYNLGFGHDlDFSFLEV 304
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGARPGAP--KVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNA-DDEELRK 149

                         170       180
                  ....*....|....*....|....*...
gi 568986780  305 MSTENNgwAQRIYEDHDATqQLQGFYNQ 332
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 150-311 5.45e-20

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: 87.71  E-value: 5.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 150 NLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVqswkGSLVPASNANLQAA-QDFVRRFSLAGATNL 228
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATPVRDKAAiLAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 229 NGGLLRGIEILNKAQGshpelSSPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMSTE 308
Cdd:cd01465   78 GAGIQLGYQEAQKHFV-----PGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADA 152


                 ...
gi 568986780 309 NNG 311
Cdd:cd01465  153 GNG 155
VWA_3 pfam13768
von Willebrand factor type A domain;
149-314 8.63e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 69.35  E-value: 8.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  149 KNLVFVIDISGSMEGQKVRQtKEALLKILEDMRPVDNFDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSLA-GATN 227
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  228 LNGGLLRGIeilnkAQGSHPElsSPASILIMlTDGEPTEGETDrsqILKNVRNAiRGRFPLYNLGFGHDLDFSFLEVMST 307
Cdd:pfam13768  80 LLGALKEAV-----RAPASPG--YIRHVLLL-TDGSPMQGETR---VSDLISRA-PGKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 568986780  308 ENNGWAQ 314
Cdd:pfam13768 148 ASNGTYE 154
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
150-303 1.05e-13

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 70.34  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 150 NLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDN------FDLVLFGSKVQswkgSLVPasnanLQAAQDF-VRRFSL 222
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletveVSVITFDGEAK----VLLP-----LTDLEDFqPPDLSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 223 AGATNLNGGLLRGIEILNKAQGSHPELSSPA--SILIMLTDGEPTEGETdrSQILKNVRNAIRGRFP-LYNLGFGHDLDF 299
Cdd:COG4245   78 SGGTPLGAALELLLDLIERRVQKYTAEGKGDwrPVVFLITDGEPTDSDW--EAALQRLKDGEAAKKAnIFAIGVGPDADT 155


                 ....
gi 568986780 300 SFLE 303
Cdd:COG4245  156 EVLK 159
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 151-311 2.30e-10

VWA C3HC4-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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 59.71  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 151 LVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSkvQSWKGS-LVPASNANLQAAQDFVRRFSLAGATNLN 229
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFST--SAKRLSpLRRMTAKGKRSAKRVVDGLQAGGGTNVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 230 GGLLRGIEILNKAQGshpelSSPASILIMLTDGEPTEGETdrsqilknVRNAIRGRFPLYNLGFGHDLDFSFLEVMSTEN 309
Cdd:cd01466   81 GGLKKALKVLGDRRQ-----KNPVASIMLLSDGQDNHGAV--------VLRADNAPIPIHTFGLGASHDPALLAFIAEIT 147


                 ..
gi 568986780 310 NG 311
Cdd:cd01466  148 GG 149
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 148-264 6.98e-08

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 53.17  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 148 SKNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQS----WKGSLVPASNANLQAAQDFVRRFSLA 223
Cdd:cd01463   13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEAK 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568986780 224 GATNLNGGLLRGIEILNK-AQGSHPELSSPASILIML-TDGEP 264
Cdd:cd01463   93 GIANYTKALEFAFSLLLKnLQSNHSGSRSQCNQAIMLiTDGVP 135
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 150-267 2.73e-07

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 51.12  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 150 NLV-FVIDISGSMEG-QKVRQTKEALLKILED---MRpvDNFDLVLF-GSKVQswkgSLVPASNaNLQAAQDFVRRFSLA 223
Cdd:cd01451    1 NLViFVVDASGSMAArHRMAAAKGAVLSLLRDayqRR--DKVALIAFrGTEAE----VLLPPTR-SVELAKRRLARLPTG 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568986780 224 GATNLNGGLLRGIEILNKAQGSHPElsspASILIMLTDGEPTEG 267
Cdd:cd01451   74 GGTPLAAGLLAAYELAAEQARDPGQ----RPLIVVITDGRANVG 113
VWA_2 pfam13519
von Willebrand factor type A domain;
151-247 1.66e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.29  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780  151 LVFVIDISGSMEGQKVRQT-----KEALLKILEDMrPVDNFDLVLFGSKVQ---SWKGslvpasnaNLQAAQDFVRRF-S 221
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTrleaaKDAVLALLKSL-PGDRVGLVTFGDGPEvliPLTK--------DRAKILRALRRLeP 71

                          90       100
                  ....*....|....*....|....*.
gi 568986780  222 LAGATNLNGGLLRGIEILNKAQGSHP 247
Cdd:pfam13519  72 KGGGTNLAAALQLARAALKHRRKNQP 97
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
1-24 8.06e-06

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 45.81  E-value: 8.06e-06
                           10        20
                   ....*....|....*....|....
gi 568986780     1 MEQFTIHITVGAQSKATFRLTYEE 24
Cdd:smart00609 107 MEQFTVSVNVAPGSKVTFELTYEE 130
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 150-285 9.27e-06

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: 46.99  E-value: 9.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 150 NLVFVIDISGSM-EGQKVRQTKEALLKILEDMrPVDNFD----LVLFGSKVQS-WKGSLVPASNAN--LQAAQDFVRRFS 221
Cdd:cd01471    2 DLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNL-NISPDEinlyLVTFSTNAKElIRLSSPNSTNKDlaLNAIRALLSLYY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568986780 222 LAGATNLNGGLLRGIEILNKAQGSHPelSSPASILIMlTDGEPtegeTDRSQILKNVRnAIRGR 285
Cdd:cd01471   81 PNGSTNTTSALLVVEKHLFDTRGNRE--NAPQLVIIM-TDGIP----DSKFRTLKEAR-KLRER 136
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-277 1.20e-05

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: 46.13  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 150 NLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVDN---FDLVLFGSKVQSWKGSLVPASNANLQAAQDFVRRFSlAGAT 226
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDktrVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLG-GGGT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568986780 227 NLNGGLLRGIEILNKAQGSHPELSspaSILIMLTDGEPTEGET--DRSQILKN 277
Cdd:cd01450   81 NTGKALQYALEQLFSESNARENVP---KVIIVLTDGRSDDGGDpkEAAAKLKD 130
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 152-298 5.58e-04

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: 41.56  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 152 VFVIDISGSMEGQKVRQTKEALLKILEDMRPvDNFDL-------VLFGSKVQSwKGSLVPASNANLQaaqdfvrRFSLAG 224
Cdd:cd01464    7 YLLLDTSGSMAGEPIEALNQGLQMLQSELRQ-DPYALesveisvITFDSAARV-IVPLTPLESFQPP-------RLTASG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568986780 225 ATNLNGGLLRGIEILN----KAQGSHPELSSPasILIMLTDGEPTEGETDRSQILKNVRNAiRGRFPLYNLGFGHDLD 298
Cdd:cd01464   78 GTSMGAALELALDCIDrrvqRYRADQKGDWRP--WVFLLTDGEPTDDLTAAIERIKEARDS-KGRIVACAVGPKADLD 152
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 149-281 2.02e-03

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: 39.25  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 149 KNLVFVIDISGSMEGQKVRQTKEALLKILEDMRPVD-NFDLVLFGSKVQSWKGSLVpasnANLQAAQDFVRRFSLAGATN 227
Cdd:cd01462    1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENrDTYLILFDSEFQTKIVDKT----DDLEEPVEFLSGVQLGGGTD 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568986780 228 LNGGLLRGIEILnkaqgshpELSSPA-SILIMLTDG---EPTEgETDRSQILKNVRNA 281
Cdd:cd01462   77 INKALRYALELI--------ERRDPRkADIVLITDGyegGVSD-ELLREVELKRSRVA 125
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 151-274 8.75e-03

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: 38.11  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568986780 151 LVFVIDISGSM---EGQKVRQTKEALLKILEDMRPVDNFDLVLFGSKVQS-WKGSLVPASNANLQAAQDFVRRfslAGAT 226
Cdd:cd01469    3 IVFVLDGSGSIypdDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTeFTLNEYRTKEEPLSLVKHISQL---LGLT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568986780 227 NLNGGLLRGI-EILNKAQGSHPelsSPASILIMLTDGEPTEGETDRSQI 274
Cdd:cd01469   80 NTATAIQYVVtELFSESNGARK---DATKVLVVITDGESHDDPLLKDVI 125
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH