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Conserved domains on  [gi|2169419194|ref|NP_034712|]
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inter-alpha-trypsin inhibitor heavy chain H2 precursor [Mus musculus]

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

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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 1.00e-85

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: 272.92  E-value: 1.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 735 ESGIVVNGQLIGAKR--AENGKLSTYFGKLGFYFQKEGMKIEISTETITLSSGSSTSRLSWSDTAHLGNSRVLISVKKEK 812
Cdd:pfam06668   1 GSGVTVNGQLIGAKKppGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 813 SVTLTLNKELFFSVLLHRVWRKHPVNVDFLGIYAPPIDKFSPRVHGLLGQFMQEPAIHIFNERPGKEPGKPEASMEVKGH 892
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 2169419194 893 KLTVTRGLQKDYRTDIVFGTDVPCWFVHN 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 8.26e-73

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: 237.11  E-value: 8.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 307 IPKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIEKIQPSGGT 386
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAIFILNEasnmgllNPDSVSLIILVSDGDptvgELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRLS 466
Cdd:cd01461    81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 2169419194 467 NENRGIAQRIYGNQDTSSQLKK 488
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
56-185 1.10e-65

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.07  E-value: 1.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194   56 LPEESGEETDTVDPVTLYSYKVQSTITSRVATTTIQSKLVNNSPLPQSVVFDVQIPKGAFISNFTMTVNGMTFTSSIKEK 135
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2169419194  136 TVGRALYSQARAKGKTAGWVRSRTLDMENFNTEVNIPPGAKVQFELHYQE 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 1.00e-85

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: 272.92  E-value: 1.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 735 ESGIVVNGQLIGAKR--AENGKLSTYFGKLGFYFQKEGMKIEISTETITLSSGSSTSRLSWSDTAHLGNSRVLISVKKEK 812
Cdd:pfam06668   1 GSGVTVNGQLIGAKKppGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 813 SVTLTLNKELFFSVLLHRVWRKHPVNVDFLGIYAPPIDKFSPRVHGLLGQFMQEPAIHIFNERPGKEPGKPEASMEVKGH 892
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 2169419194 893 KLTVTRGLQKDYRTDIVFGTDVPCWFVHN 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 8.26e-73

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: 237.11  E-value: 8.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 307 IPKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIEKIQPSGGT 386
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAIFILNEasnmgllNPDSVSLIILVSDGDptvgELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRLS 466
Cdd:cd01461    81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 2169419194 467 NENRGIAQRIYGNQDTSSQLKK 488
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
56-185 1.10e-65

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.07  E-value: 1.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194   56 LPEESGEETDTVDPVTLYSYKVQSTITSRVATTTIQSKLVNNSPLPQSVVFDVQIPKGAFISNFTMTVNGMTFTSSIKEK 135
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2169419194  136 TVGRALYSQARAKGKTAGWVRSRTLDMENFNTEVNIPPGAKVQFELHYQE 185
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 308-511 6.60e-42

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 155.26  E-value: 6.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 308 PKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTwrndLVSATK-TQIADAKRYIEKIQPSGGT 386
Cdd:COG2304    91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAIDRLQAGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAIFILNEAsnmglLNPDSVSLIILVSDGDPTVGELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRLS 466
Cdd:COG2304   167 ALGAGLELAYELARKH-----FIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLA 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2169419194 467 NENRGIAQRIYGNQDTSSQLKKFYNQVSTP--LLRNVQFNYPQASVT 511
Cdd:COG2304   242 DAGGGNYYYIDDPEEAEKVFVREFSRIGYEnrALATEDFPLPYGTLK 288
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 72-183 1.66e-35

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: 130.30  E-value: 1.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194  72 LYSYKVQSTITSRVATTTIQSKLVNNSPLPQSVVFDVQIPKGAFISNFTMTVNGMTFTSSIKEKTVGRALYSQARAKGKT 151
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2169419194 152 AGWVrsRTLDMENFNTEV-NIPPGAKVQFELHY 183
Cdd:pfam08487  81 AGLL--EQDTPDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 310-471 3.79e-28

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: 111.78  E-value: 3.79e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194  310 NILFVIDVSGSMWGIKMKQTVEAMKTILDDLR---TDDQFSVVDFNHNVRTWRNDLVSATKtqiADAKRYIEKIQP--SG 384
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSK---DALLEALASLSYklGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194  385 GTNINEALLRAIFILNEASNMGllNPDSVSLIILVSDGDPTVGElklSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKR 464
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGP---KDLLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*..
gi 2169419194  465 LSNENRG 471
Cdd:smart00327 153 LASAPGG 159
VWA pfam00092
von Willebrand factor type A domain;
310-492 1.89e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 95.42  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSMWGIKMKQTVEAMKTILDDL---RTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIeKIQPSGGT 386
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAI-FILNEASNMGllnPDSVSLIILVSDGDPTVGElklskIQKNVKQSIQDNISLFSLGIGFDVDYDfLKRL 465
Cdd:pfam00092  80 NTGKALKYALeNLFSSAAGAR---PGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 2169419194 466 SNENRgiAQRIYGNQDtSSQLKKFYNQ 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 1.00e-85

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: 272.92  E-value: 1.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 735 ESGIVVNGQLIGAKR--AENGKLSTYFGKLGFYFQKEGMKIEISTETITLSSGSSTSRLSWSDTAHLGNSRVLISVKKEK 812
Cdd:pfam06668   1 GSGVTVNGQLIGAKKppGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 813 SVTLTLNKELFFSVLLHRVWRKHPVNVDFLGIYAPPIDKFSPRVHGLLGQFMQEPAIHIFNERPGKEPGKPEASMEVKGH 892
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 2169419194 893 KLTVTRGLQKDYRTDIVFGTDVPCWFVHN 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 8.26e-73

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: 237.11  E-value: 8.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 307 IPKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIEKIQPSGGT 386
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAIFILNEasnmgllNPDSVSLIILVSDGDptvgELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRLS 466
Cdd:cd01461    81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 2169419194 467 NENRGIAQRIYGNQDTSSQLKK 488
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
56-185 1.10e-65

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.07  E-value: 1.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194   56 LPEESGEETDTVDPVTLYSYKVQSTITSRVATTTIQSKLVNNSPLPQSVVFDVQIPKGAFISNFTMTVNGMTFTSSIKEK 135
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2169419194  136 TVGRALYSQARAKGKTAGWVRSRTLDMENFNTEVNIPPGAKVQFELHYQE 185
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 308-511 6.60e-42

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 155.26  E-value: 6.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 308 PKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTwrndLVSATK-TQIADAKRYIEKIQPSGGT 386
Cdd:COG2304    91 PLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAIDRLQAGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAIFILNEAsnmglLNPDSVSLIILVSDGDPTVGELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRLS 466
Cdd:COG2304   167 ALGAGLELAYELARKH-----FIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLA 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2169419194 467 NENRGIAQRIYGNQDTSSQLKKFYNQVSTP--LLRNVQFNYPQASVT 511
Cdd:COG2304   242 DAGGGNYYYIDDPEEAEKVFVREFSRIGYEnrALATEDFPLPYGTLK 288
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 72-183 1.66e-35

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: 130.30  E-value: 1.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194  72 LYSYKVQSTITSRVATTTIQSKLVNNSPLPQSVVFDVQIPKGAFISNFTMTVNGMTFTSSIKEKTVGRALYSQARAKGKT 151
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2169419194 152 AGWVrsRTLDMENFNTEV-NIPPGAKVQFELHY 183
Cdd:pfam08487  81 AGLL--EQDTPDVFTTSVgNIPPGEKVTVELTY 111
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 306-493 1.61e-28

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: 115.81  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 306 PIPKNILFVIDVSGSMWGI-KMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTwrndLVSATkTQIADAKRYIEKIQPSG 384
Cdd:COG1240    90 QRGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV----LLPLT-RDREALKRALDELPPGG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 385 GTNINEALLRAIFILNEASnmgllnPDSVSLIILVSDGDPTVGELKLSKIQKNVKQSiqdNISLFSLGIGFD-VDYDFLK 463
Cdd:COG1240   165 GTPLGDALALALELLKRAD------PARRKVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGTEaVDEGLLR 235

                         170       180       190
                  ....*....|....*....|....*....|
gi 2169419194 464 RLSNENRGIAQRIygnqDTSSQLKKFYNQV 493
Cdd:COG1240   236 EIAEATGGRYFRA----DDLSELAAIYREI 261
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 310-471 3.79e-28

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: 111.78  E-value: 3.79e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194  310 NILFVIDVSGSMWGIKMKQTVEAMKTILDDLR---TDDQFSVVDFNHNVRTWRNDLVSATKtqiADAKRYIEKIQP--SG 384
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSK---DALLEALASLSYklGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194  385 GTNINEALLRAIFILNEASNMGllNPDSVSLIILVSDGDPTVGElklSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKR 464
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGP---KDLLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*..
gi 2169419194  465 LSNENRG 471
Cdd:smart00327 153 LASAPGG 159
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 310-465 1.67e-27

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: 109.67  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTwrndLVSAT----KTQIADAkryIEKIQPSGG 385
Cdd:cd01465     2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----VLPATpvrdKAAILAA---IDRLTAGGS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 386 TNINEALLRAIfilNEASNMglLNPDSVSLIILVSDGDPTVGELKLSKIQKNVKQSIQDNISLFSLGIGFDVDYDFLKRL 465
Cdd:cd01465    75 TAGGAGIQLGY---QEAQKH--FVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 310-466 3.93e-26

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 105.34  E-value: 3.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSMWGIKMKQTVEAMKTILDDL---RTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIEKiQPSGGT 386
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAIFILNEASnmgllNPDSVSLIILVSDGDPTVGELKLSKIQKNVKQSiqdNISLFSLGIGFDVDYDFLKRLS 466
Cdd:cd00198    81 NIGAALRLALELLKSAK-----RPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 300-466 8.94e-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: 98.98  E-value: 8.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 300 APENLDPIPKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTwrnDLVSATKTQIADAKRYIEK 379
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 380 IQPSGGTNINEALLRAIFILNEAsnmgllnPDSVSLIILVSDGDPTVGElklSKIQKNVKQSIQDnISLFSLGIGFDVDY 459
Cdd:COG2425   187 LFAGGGTDIAPALRAALELLEEP-------DYRNADIVLITDGEAGVSP---EELLREVRAKESG-VRLFTVAIGDAGNP 255


                  ....*..
gi 2169419194 460 DFLKRLS 466
Cdd:COG2425   256 GLLEALA 262
VWA pfam00092
von Willebrand factor type A domain;
310-492 1.89e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 95.42  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSMWGIKMKQTVEAMKTILDDL---RTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIeKIQPSGGT 386
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 387 NINEALLRAI-FILNEASNMGllnPDSVSLIILVSDGDPTVGElklskIQKNVKQSIQDNISLFSLGIGFDVDYDfLKRL 465
Cdd:pfam00092  80 NTGKALKYALeNLFSSAAGAR---PGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 2169419194 466 SNENRgiAQRIYGNQDtSSQLKKFYNQ 492
Cdd:pfam00092 151 ASEPG--EGHVFTVSD-FEALEDLQDQ 174
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
310-495 3.08e-22

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 95.38  E-value: 3.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQ------FSVVDFNHNVRtWRNDLVSATKTQIADakryiekIQPS 383
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletveVSVITFDGEAK-VLLPLTDLEDFQPPD-------LSAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 384 GGTNINEALLRAIFILNEASNMGLLNPDSV--SLIILVSDGDPTVGELKlSKIQKnVKQSIQDN-ISLFSLGIGFDVDYD 460
Cdd:COG4245    79 GGTPLGAALELLLDLIERRVQKYTAEGKGDwrPVVFLITDGEPTDSDWE-AALQR-LKDGEAAKkANIFAIGVGPDADTE 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2169419194 461 FLKRLSNENRGIaqriygNQDTSSQLKKFYNQVST 495
Cdd:COG4245   157 VLKQLTDPVRAL------DALDGLDFREFFKWLSA 185
VWA_3 pfam13768
von Willebrand factor type A domain;
309-474 2.88e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 65.50  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 309 KNILFVIDVSGSMWGIKMKQtVEAMKTILDDLRTDDQFSVVDFNHNVRTWRNDLVSATKTQIADAKRYIEKIQP-SGGTN 387
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 388 ineaLLRAifiLNEASNMgLLNPDSVSLIILVSDGDPTVGELKLSkiqKNVKQSiQDNISLFSLGIGFDVDYDFLKRLSN 467
Cdd:pfam13768  80 ----LLGA---LKEAVRA-PASPGYIRHVLLLTDGSPMQGETRVS---DLISRA-PGKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 2169419194 468 ENRGIAQ 474
Cdd:pfam13768 148 ASNGTYE 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 310-468 3.84e-12

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 65.39  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSM---WGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTWRNDLVSATKtqiADAKRYIEKIQPSGG- 385
Cdd:cd01450     2 DIVFLLDGSESVgpeNFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSK---DDLLKAVKNLKYLGGg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 386 -TNINEALLRAIFILNEASNMgllNPDSVSLIILVSDGDPTVGElKLSKIQKNVKQSiqdNISLFSLGIGfDVDYDFLKR 464
Cdd:cd01450    79 gTNTGKALQYALEQLFSESNA---RENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDE---GIKVFVVGVG-PADEEELRE 150


                  ....
gi 2169419194 465 LSNE 468
Cdd:cd01450   151 IASC 154
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 308-471 5.07e-12

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: 65.49  E-value: 5.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 308 PKNILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRT----WRNDLVSATKTQIADAKRYIEKIQPS 383
Cdd:cd01463    13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEAK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 384 GGTNINEALLRAIFILNEASNMGLLNPDSV--SLIILVSDGDPtvgelklSKIQKNVKQSIQDN-----ISLFSLGIGFD 456
Cdd:cd01463    93 GIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDGVP-------ENYKEIFDKYNWDKnseipVRVFTYLIGRE 165

                         170
                  ....*....|....*.
gi 2169419194 457 V-DYDFLKRLSNENRG 471
Cdd:cd01463   166 VtDRREIQWMACENKG 181
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 314-467 7.48e-11

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: 61.25  E-value: 7.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 314 VIDVSGSMWGIKMKQTVEAMKTILDDLRTDDQFSVVDFNhNVRTWRNDLVSATKTQIADAKRYIEKIQPSGGTNINEALL 393
Cdd:cd01466     6 VLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFS-TSAKRLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVGGLK 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2169419194 394 RAIFILneasnMGLLNPDSVSLIILVSDGDPTVGELKLskiqknvkQSIQDNISLFSLGIGFDVDYD---FLKRLSN 467
Cdd:cd01466    85 KALKVL-----GDRRQKNPVASIMLLSDGQDNHGAVVL--------RADNAPIPIHTFGLGASHDPAllaFIAEITG 148
VWA_2 pfam13519
von Willebrand factor type A domain;
311-404 7.67e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 7.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 311 ILFVIDVSGSM----WGIKMKQTV-EAMKTILDDLRTdDQFSVVDFNHNVRTwrndLVSATKTQiADAKRYIEKIQP-SG 384
Cdd:pfam13519   1 LVFVLDTSGSMrngdYGPTRLEAAkDAVLALLKSLPG-DRVGLVTFGDGPEV----LIPLTKDR-AKILRALRRLEPkGG 74

                          90       100
                  ....*....|....*....|
gi 2169419194 385 GTNINEALLRAIFILNEASN 404
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRK 94
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 311-427 2.24e-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: 51.89  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 311 ILFVIDVSGSMwgiKMKQTVEAMKTILDDLRTD-----DQFSVVDFNHNvrtwRNDLVSATKTQIADAKRYIEKIQPSGG 385
Cdd:cd01451     3 VIFVVDASGSM---AARHRMAAAKGAVLSLLRDayqrrDKVALIAFRGT----EAEVLLPPTRSVELAKRRLARLPTGGG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2169419194 386 TNINEALLRAIFILNEAsnmgLLNPDSVSLIILVSDGDPTVG 427
Cdd:cd01451    76 TPLAAGLLAAYELAAEQ----ARDPGQRPLIVVITDGRANVG 113
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 309-468 4.50e-06

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 47.61  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 309 KNILFVIDVSGSMwGIKMKQTVEA-MKTILDDL--RTDD-QFSVVDFNHNVRTWRNDLVSATKTQIADAkryIEKIQP-S 383
Cdd:cd01472     1 ADIVFLVDGSESI-GLSNFNLVKDfVKRVVERLdiGPDGvRVGVVQYSDDPRTEFYLNTYRSKDDVLEA---VKNLRYiG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 384 GGTNINEALLRAI-FILNEASNMGLLNPdsvSLIILVSDGDPTvgelklSKIQKNVKQSIQDNISLFSLGIGfDVDYDFL 462
Cdd:cd01472    77 GGTNTGKALKYVReNLFTEASGSREGVP---KVLVVITDGKSQ------DDVEEPAVELKQAGIEVFAVGVK-NADEEEL 146


                  ....*.
gi 2169419194 463 KRLSNE 468
Cdd:cd01472   147 KQIASD 152
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 311-466 4.79e-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: 47.72  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 311 ILFVIDVSGSMWGIKMKQTVEAMKTILDDLRTDD------QFSVVDFNHNVRTWRnDLVSatktqiadakryIEKIQP-- 382
Cdd:cd01464     6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPyalesvEISVITFDSAARVIV-PLTP------------LESFQPpr 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 383 ---SGGTNINEALLRAIFILNE------ASNMGLLNPdsvsLIILVSDGDPTVGELKLSKIQKNVKQSiqdNISLFSLGI 453
Cdd:cd01464    73 ltaSGGTSMGAALELALDCIDRrvqryrADQKGDWRP----WVFLLTDGEPTDDLTAAIERIKEARDS---KGRIVACAV 145

                         170
                  ....*....|...
gi 2169419194 454 GFDVDYDFLKRLS 466
Cdd:cd01464   146 GPKADLDTLKQIT 158
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 299-458 6.33e-05

VWA ywmD 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. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif.


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 45.11  E-value: 6.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 299 FAPENLDPIPK---NILFVIDVSGSM------WGIKMKQTVEAMKTILDDLRTDDQFSVVDFNH---NVRTWRNDLVS-- 364
Cdd:cd01456     8 FALEPVETEPQlppNVAIVLDNSGSMrevdggGETRLDNAKAALDETANALPDGTRLGLWTFSGdgdNPLDVRVLVPKgc 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 365 ---------ATKTQIADAKryIEKIQ-PSGGTNINEALLRAifilneASNmglLNPDSVSLIILVSDG---DPTVGELKL 431
Cdd:cd01456    88 ltapvngfpSAQRSALDAA--LNSLQtPTGWTPLAAALAEA------AAY---VDPGRVNVVVLITDGedtCGPDPCEVA 156

                         170       180
                  ....*....|....*....|....*..
gi 2169419194 432 SKIQKnvKQSIQDNISLFSLGIGFDVD 458
Cdd:cd01456   157 RELAK--RRTPAPPIKVNVIDFGGDAD 181
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 310-473 6.01e-04

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 41.99  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSM----WGIKMKQTVEAMKTIL----DDLRTddqfSVVDFNHNVRT-WR-NDLVSATKTQIADAKRYIEK 379
Cdd:cd01471     2 DLYLLVDGSGSIgysnWVTHVVPFLHTFVQNLnispDEINL----YLVTFSTNAKElIRlSSPNSTNKDLALNAIRALLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 380 I-QPSGGTNINEALLRAIFILNEaSNMGllNPDSVSLIILVSDGDP-----TVGELKLSKiQKNVKQSIqdnislfsLGI 453
Cdd:cd01471    78 LyYPNGSTNTTSALLVVEKHLFD-TRGN--RENAPQLVIIMTDGIPdskfrTLKEARKLR-ERGVIIAV--------LGV 145

                         170       180
                  ....*....|....*....|
gi 2169419194 454 GFDVDydflkrlSNENRGIA 473
Cdd:cd01471   146 GQGVN-------HEENRSLV 158
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 310-484 6.62e-04

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 41.55  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 310 NILFVIDVSGSMWGIKMKQT--VEAMKTILDDL---RTDDQFSVVDFNHNVRT---WRNDLVSATK----TQIADAKRyi 377
Cdd:cd01467     4 DIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFidrRENDRIGLVVFAGAAFTqapLTLDRESLKElledIKIGLAGQ-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 378 ekiqpsgGTNINEALLRAIFILNEASNMGllnpdsvSLIILVSDGDPTVGElkLSKIQ-KNVKQSIqdNISLFSLGIG-- 454
Cdd:cd01467    82 -------GTAIGDAIGLAIKRLKNSEAKE-------RVIVLLTDGENNAGE--IDPATaAELAKNK--GVRIYTIGVGks 143

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2169419194 455 ---------FDVDYDFLKRLSNENRGiaqRIYGNQDTSS 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 9.66e-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: 40.79  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 315 IDVSGSMWGIKMKQTVEAMKTILDDLRTDDQ-FSVVDFNHNVRTWRNDLVSatktQIADAKRYIEKIQPSGGTNINEALL 393
Cdd:cd01462     7 VDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSEFQTKIVDKTD----DLEEPVEFLSGVQLGGGTDINKALR 82

                          90       100
                  ....*....|....*....|....*....
gi 2169419194 394 RAIFILneaSNMGLLNPDsvslIILVSDG 422
Cdd:cd01462    83 YALELI---ERRDPRKAD----IVLITDG 104
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 311-454 6.69e-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: 38.49  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169419194 311 ILFVIDVSGSM----WGiKMKQTVEAMKTILDDLRTDDQFSVVDFNHNVRTW--------RNDLVSATKtQIAdakryie 378
Cdd:cd01469     3 IVFVLDGSGSIypddFQ-KVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEftlneyrtKEEPLSLVK-HIS------- 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169419194 379 kiQPSGGTNINEALLRAIFILNEASNMGllNPDSVSLIILVSDGDPTVGELklskIQKNVKQSIQDNISLFSLGIG 454
Cdd:cd01469    74 --QLLGLTNTATAIQYVVTELFSESNGA--RKDATKVLVVITDGESHDDPL----LKDVIPQAEREGIIRYAIGVG 141
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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