NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|229462889|sp|P19823|]
View 

RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H2; Short=ITI heavy chain H2; Short=ITI-HC2; Short=Inter-alpha-inhibitor heavy chain 2; AltName: Full=Inter-alpha-trypsin inhibitor complex component II; AltName: Full=Serum-derived hyaluronan-associated protein; Short=SHAP; Flags: Precursor

Protein Classification

inter-alpha-trypsin inhibitor heavy chain H( domain architecture ID 10652060)

inter-alpha-trypsin inhibitor heavy chain H may act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes

Gene Ontology:  GO:0030212|GO:0004867

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 ...
 735-921 1.25e-95

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: 299.11  E-value: 1.25e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  735 ESGIVVNGQLVGAKKPNN--GKLSTYFGKLGFYFQSEDIKIEISTETITLSHGSSTFSLSWSDTAQVTNQRVQISVKKEK 812
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGshKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  813 VVTITLDKEMSFSVLLHRVWKKHPVNVDFLGIYIPPTNKFSPKAHGLIGQFMQEPKIHIFNERPGKDPEKPEASMEVKGQ 892
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 229462889  893 KLIITRGLQKDYRTDLVFGTDVTCWFVHN 921
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 307-488 9.43e-69

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: 226.33  E-value: 9.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 307 IPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGT 386
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 387 NINEALLRAIFILNEannlgllDPNSVSLIILVSDGDptvgELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLS 466
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 229462889 467 NENHGIAQRIYGNQDTSSQLKK 488
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
56-185 8.62e-66

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.46  E-value: 8.62e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889    56 LPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEK 135
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 229462889   136 TVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQE 185
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 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 ...
 735-921 1.25e-95

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: 299.11  E-value: 1.25e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  735 ESGIVVNGQLVGAKKPNN--GKLSTYFGKLGFYFQSEDIKIEISTETITLSHGSSTFSLSWSDTAQVTNQRVQISVKKEK 812
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGshKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  813 VVTITLDKEMSFSVLLHRVWKKHPVNVDFLGIYIPPTNKFSPKAHGLIGQFMQEPKIHIFNERPGKDPEKPEASMEVKGQ 892
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 229462889  893 KLIITRGLQKDYRTDLVFGTDVTCWFVHN 921
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 307-488 9.43e-69

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: 226.33  E-value: 9.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 307 IPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGT 386
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 387 NINEALLRAIFILNEannlgllDPNSVSLIILVSDGDptvgELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLS 466
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 229462889 467 NENHGIAQRIYGNQDTSSQLKK 488
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
56-185 8.62e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.46  E-value: 8.62e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889    56 LPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEK 135
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 229462889   136 TVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQE 185
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 308-492 4.43e-40

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 149.87  E-value: 4.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 308 PKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTwrndLISATK-TQVADAKRYIEKIQPSGGT 386
Cdd:COG2304   91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAIDRLQAGGGT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 387 NINEALLRAIFILNEAnnlglLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLS 466
Cdd:COG2304  167 ALGAGLELAYELARKH-----FIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLA 241

                        170       180
                 ....*....|....*....|....*.
gi 229462889 467 NENHGIAQRIygnqDTSSQLKKFYNQ 492
Cdd:COG2304  242 DAGGGNYYYI----DDPEEAEKVFVR 263
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 72-183 1.80e-36

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.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 132.99  E-value: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889   72 LYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEKTVGRALYAQARAKGKT 151
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 229462889  152 AGLVRSSalDMENFRTEV-NVLPGAKVQFELHY 183
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 310-471 2.54e-25

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: 103.69  E-value: 2.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889   310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDLRA---EDHFSVIDFNQNIRTWRNDLISATKtqvADAKRYIEKIQP--SG 384
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDARVLFPLNDSRSK---DALLEALASLSYklGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889   385 GTNINEALLRAIFILNEANNLGllDPNSVSLIILVSDGDPTVGElklSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKR 464
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGP---KDLLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*..
gi 229462889   465 LSNENHG 471
Cdd:smart00327 153 LASAPGG 159
VWA pfam00092
von Willebrand factor type A domain;
310-492 7.44e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 87.72  E-value: 7.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDL---RAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIeKIQPSGGT 386
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  387 NINEALLRAI-FILNEANNLGlldPNSVSLIILVSDGDPTVGElklskIQKNVKENIQDNISLFSLGMGFDVDYDfLKRL 465
Cdd:pfam00092  80 NTGKALKYALeNLFSSAAGAR---PGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 229462889  466 SNENHgiAQRIYGNQDtSSQLKKFYNQ 492
Cdd:pfam00092 151 ASEPG--EGHVFTVSD-FEALEDLQDQ 174
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 735-921 1.25e-95

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: 299.11  E-value: 1.25e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  735 ESGIVVNGQLVGAKKPNN--GKLSTYFGKLGFYFQSEDIKIEISTETITLSHGSSTFSLSWSDTAQVTNQRVQISVKKEK 812
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGshKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  813 VVTITLDKEMSFSVLLHRVWKKHPVNVDFLGIYIPPTNKFSPKAHGLIGQFMQEPKIHIFNERPGKDPEKPEASMEVKGQ 892
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 229462889  893 KLIITRGLQKDYRTDLVFGTDVTCWFVHN 921
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 307-488 9.43e-69

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: 226.33  E-value: 9.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 307 IPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGT 386
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 387 NINEALLRAIFILNEannlgllDPNSVSLIILVSDGDptvgELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLS 466
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 229462889 467 NENHGIAQRIYGNQDTSSQLKK 488
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
56-185 8.62e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.46  E-value: 8.62e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889    56 LPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEK 135
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 229462889   136 TVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQE 185
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 308-492 4.43e-40

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 149.87  E-value: 4.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 308 PKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTwrndLISATK-TQVADAKRYIEKIQPSGGT 386
Cdd:COG2304   91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAIDRLQAGGGT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 387 NINEALLRAIFILNEAnnlglLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLS 466
Cdd:COG2304  167 ALGAGLELAYELARKH-----FIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLA 241

                        170       180
                 ....*....|....*....|....*.
gi 229462889 467 NENHGIAQRIygnqDTSSQLKKFYNQ 492
Cdd:COG2304  242 DAGGGNYYYI----DDPEEAEKVFVR 263
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 72-183 1.80e-36

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.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 132.99  E-value: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889   72 LYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEKTVGRALYAQARAKGKT 151
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 229462889  152 AGLVRSSalDMENFRTEV-NVLPGAKVQFELHY 183
Cdd:pfam08487  81 AGLLEQD--TPDVFTTSVgNIPPGEKVTVELTY 111
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 306-493 3.90e-27

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: 111.57  E-value: 3.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 306 PIPKNILFVIDVSGSMWGV-KMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTwrndLISATkTQVADAKRYIEKIQPSG 384
Cdd:COG1240   90 QRGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV----LLPLT-RDREALKRALDELPPGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 385 GTNINEALLRAIFILNEAnnlgllDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENiqdNISLFSLGMGFD-VDYDFLK 463
Cdd:COG1240  165 GTPLGDALALALELLKRA------DPARRKVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGTEaVDEGLLR 235

                        170       180       190
                 ....*....|....*....|....*....|
gi 229462889 464 RLSNENHGIAQRIygnqDTSSQLKKFYNQV 493
Cdd:COG1240  236 EIAEATGGRYFRA----DDLSELAAIYREI 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 310-466 2.22e-25

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: 103.41  E-value: 2.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAE---DHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKiQPSGGT 386
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 387 NINEALLRAIFILNEANnlgllDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENiqdNISLFSLGMGFDVDYDFLKRLS 466
Cdd:cd00198   81 NIGAALRLALELLKSAK-----RPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 310-471 2.54e-25

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: 103.69  E-value: 2.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889   310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDLRA---EDHFSVIDFNQNIRTWRNDLISATKtqvADAKRYIEKIQP--SG 384
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDARVLFPLNDSRSK---DALLEALASLSYklGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889   385 GTNINEALLRAIFILNEANNLGllDPNSVSLIILVSDGDPTVGElklSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKR 464
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGP---KDLLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*..
gi 229462889   465 LSNENHG 471
Cdd:smart00327 153 LASAPGG 159
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 310-470 9.90e-23

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: 95.80  E-value: 9.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTwrndLISAT----KTQVADAkryIEKIQPSGG 385
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----VLPATpvrdKAAILAA---IDRLTAGGS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 386 TNINEALLRAIFILNEAnnlglLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRL 465
Cdd:cd01465   75 TAGGAGIQLGYQEAQKH-----FVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149


                 ....*.
gi 229462889 466 S-NENH 470
Cdd:cd01465  150 AdAGNG 155
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 265-466 7.63e-22

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 96.29  E-value: 7.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 265 RETAVDGELVVLYDVKREEKAGELEVFNGYFVHFFAPDNLDPIPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAED 344
Cdd:COG2425   75 LLLAALLAALLDALLLAVLLLALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNR 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 345 HFSVIDFNQNIRTwrnDLISATKTQVADAKRYIEKIQPSGGTNINEALLRAIFILNEannlgllDPNSVSLIILVSDGDP 424
Cdd:COG2425  155 RFGVILFDTEVVE---DLPLTADDGLEDAIEFLSGLFAGGGTDIAPALRAALELLEE-------PDYRNADIVLITDGEA 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 229462889 425 TVGElklSKIQKNVKENIQDnISLFSLGMGFDVDYDFLKRLS 466
Cdd:COG2425  225 GVSP---EELLREVRAKESG-VRLFTVAIGDAGNPGLLEALA 262
VWA pfam00092
von Willebrand factor type A domain;
310-492 7.44e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 87.72  E-value: 7.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDL---RAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIeKIQPSGGT 386
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  387 NINEALLRAI-FILNEANNLGlldPNSVSLIILVSDGDPTVGElklskIQKNVKENIQDNISLFSLGMGFDVDYDfLKRL 465
Cdd:pfam00092  80 NTGKALKYALeNLFSSAAGAR---PGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 229462889  466 SNENHgiAQRIYGNQDtSSQLKKFYNQ 492
Cdd:pfam00092 151 ASEPG--EGHVFTVSD-FEALEDLQDQ 174
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
310-495 1.48e-19

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 87.67  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAED------HFSVIDFNQNIRtWRNDLisatkTQVADAkrYIEKIQPS 383
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGEAK-VLLPL-----TDLEDF--QPPDLSAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 384 GGTNINEALLRAIFILNeaNNLGLLDPNSVS----LIILVSDGDPTVGELKlSKIQKnVKENIQDN-ISLFSLGMGFDVD 458
Cdd:COG4245   79 GGTPLGAALELLLDLIE--RRVQKYTAEGKGdwrpVVFLITDGEPTDSDWE-AALQR-LKDGEAAKkANIFAIGVGPDAD 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 229462889 459 YDFLKRLSNENHGIaqriygNQDTSSQLKKFYNQVST 495
Cdd:COG4245  155 TEVLKQLTDPVRAL------DALDGLDFREFFKWLSA 185
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 308-471 1.94e-10

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: 60.87  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 308 PKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRT----WRNDLISATKTQVADAKRYIEKIQPS 383
Cdd:cd01463   13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEAK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 384 GGTNINEALLRAIFILNEANNLGLLDPNSV--SLIILVSDGDPTvgelKLSKI--QKNVKENIQDNISLFSLGMGFDV-D 458
Cdd:cd01463   93 GIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDGVPE----NYKEIfdKYNWDKNSEIPVRVFTYLIGREVtD 168

                        170
                 ....*....|...
gi 229462889 459 YDFLKRLSNENHG 471
Cdd:cd01463  169 RREIQWMACENKG 181
VWA_3 pfam13768
von Willebrand factor type A domain;
309-474 2.29e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 60.10  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  309 KNILFVIDVSGSMWGVKMKQtVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQP-SGGTN 387
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  388 INEALLRAifilneannLGLLDPN-SVSLIILVSDGDPTVGELKLSkiqknvkENIQD---NISLFSLGMGFDVDYDFLK 463
Cdd:pfam13768  80 LLGALKEA---------VRAPASPgYIRHVLLLTDGSPMQGETRVS-------DLISRapgKIRFFAYGLGASISAPMLQ 143

                         170
                  ....*....|.
gi 229462889  464 RLSNENHGIAQ 474
Cdd:pfam13768 144 LLAEASNGTYE 154
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 314-467 6.02e-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: 58.56  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 314 VIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNqNIRTWRNDLISATKTQVADAKRYIEKIQPSGGTNINEALL 393
Cdd:cd01466    6 VLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFS-TSAKRLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVGGLK 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229462889 394 RAIFILNeannlGLLDPNSVSLIILVSDGDPTVGELKLSKiqKNVKeniqdnISLFSLGMGFDVDYD---FLKRLSN 467
Cdd:cd01466   85 KALKVLG-----DRRQKNPVASIMLLSDGQDNHGAVVLRA--DNAP------IPIHTFGLGASHDPAllaFIAEITG 148
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 310-470 8.30e-10

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: 58.46  E-value: 8.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 310 NILFVIDVSGSMWGVKMKQTVEAMKTILDDL-RAED--HFSVIDFNQNIRTWRNDLISATKTQVadaKRYIEKIQPSGG- 385
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdIGPDktRVGLVQYSDDVRVEFSLNDYKSKDDL---LKAVKNLKYLGGg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 386 -TNINEALLraiFILNEANNLGLLDPNSVSLIILVSDGDPTVGElKLSKIQKNVKENiqdNISLFSLGMGfDVDYDFLKR 464
Cdd:cd01450   79 gTNTGKALQ---YALEQLFSESNARENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDE---GIKVFVVGVG-PADEEELRE 150


                 ....*.
gi 229462889 465 LSNENH 470
Cdd:cd01450  151 IASCPS 156
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 311-427 1.15e-08

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: 55.75  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 311 ILFVIDVSGSMWG-VKM---KQTVEAMktILDDLRAEDHFSVIDFNQNIRTWrndLISATKtQVADAKRYIEKIQPSGGT 386
Cdd:cd01451    3 VIFVVDASGSMAArHRMaaaKGAVLSL--LRDAYQRRDKVALIAFRGTEAEV---LLPPTR-SVELAKRRLARLPTGGGT 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 229462889 387 NINEALLRAIFILNEAnnlgLLDPNSVSLIILVSDGDPTVG 427
Cdd:cd01451   77 PLAAGLLAAYELAAEQ----ARDPGQRPLIVVITDGRANVG 113
VWA_2 pfam13519
von Willebrand factor type A domain;
311-404 2.03e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 52.68  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889  311 ILFVIDVSGSM-WGVKMKQTVEAMKTILDDL---RAEDHFSVIDFNQNIRTwrndLISATKTQvADAKRYIEKIQP-SGG 385
Cdd:pfam13519   1 LVFVLDTSGSMrNGDYGPTRLEAAKDAVLALlksLPGDRVGLVTFGDGPEV----LIPLTKDR-AKILRALRRLEPkGGG 75

                          90
                  ....*....|....*....
gi 229462889  386 TNINEALLRAIFILNEANN 404
Cdd:pfam13519  76 TNLAAALQLARAALKHRRK 94
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 311-466 2.61e-06

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: 48.49  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 311 ILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAED------HFSVIDFNQNIRTWRnDLISATKTQVADakryiekIQPSG 384
Cdd:cd01464    6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPyalesvEISVITFDSAARVIV-PLTPLESFQPPR-------LTASG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 385 GTNINEALLRAIFILNE------ANNLGLLDPnsvsLIILVSDGDPTVGELKLSKIQKNVKENiqdNISLFSLGMGFDVD 458
Cdd:cd01464   78 GTSMGAALELALDCIDRrvqryrADQKGDWRP----WVFLLTDGEPTDDLTAAIERIKEARDS---KGRIVACAVGPKAD 150


                 ....*...
gi 229462889 459 YDFLKRLS 466
Cdd:cd01464  151 LDTLKQIT 158
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 310-484 4.38e-05

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 45.01  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 310 NILFVIDVSGSMWGVKMKQT--VEAMKTILDDL---RAEDHFSVIDFNQNIRT---WRNDLISATK----TQVADAKRyi 377
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFidrRENDRIGLVVFAGAAFTqapLTLDRESLKElledIKIGLAGQ-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 378 ekiqpsgGTNINEALLRAIFILNEANNLGlldpnsvSLIILVSDGDPTVGElkLSKIQ-KNVKENIqdNISLFSLGMG-- 454
Cdd:cd01467   82 -------GTAIGDAIGLAIKRLKNSEAKE-------RVIVLLTDGENNAGE--IDPATaAELAKNK--GVRIYTIGVGks 143

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 229462889 455 ---------FDVDYDFLKRLSNENHGiaqRIYGNQDTSS 484
Cdd:cd01467  144 gsgpkpdgsTILDEDSLVEIADKTGG---RIFRALDGFE 179
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 315-422 1.12e-04

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 43.49  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 315 IDVSGSMWGVKMKQTVEAMKTILDDLRAED-HFSVIDFNQNIRTWRNDLISatktQVADAKRYIEKIQPSGGTNINEALL 393
Cdd:cd01462    7 VDQSGSMYGAPEEVAKAVALALLRIALAENrDTYLILFDSEFQTKIVDKTD----DLEEPVEFLSGVQLGGGTDINKALR 82

                         90       100
                 ....*....|....*....|....*....
gi 229462889 394 RAIFILNEANNLGlldpnsvSLIILVSDG 422
Cdd:cd01462   83 YALELIERRDPRK-------ADIVLITDG 104
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 310-459 1.39e-03

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: 40.83  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462889 310 NILFVIDVSGSM----WGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRT-WR-NDLISATKTQVADAKRYIEKI-QP 382
Cdd:cd01471    2 DLYLLVDGSGSIgysnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKElIRlSSPNSTNKDLALNAIRALLSLyYP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229462889 383 SGGTNINEALLRAIFILNEANnlgLLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIqdNISLFSLGMGFDVDY 459
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFDTR---GNRENAPQLVIIMTDGIPDSKFRTLKEARKLRERGV--IIAVLGVGQGVNHEE 153
 
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