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Conserved domains on  [gi|261878618|ref|NP_001159908|]
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inter-alpha-trypsin inhibitor heavy chain H1 isoform c [Homo sapiens]

Protein Classification

inter-alpha-trypsin inhibitor heavy chain H; vWA domain-containing protein( domain architecture ID 10106957)

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| vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

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 ...
 417-604 4.40e-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: 289.87  E-value: 4.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  417 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 494
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  495 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 574
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 261878618  575 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 604
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 1-182 5.80e-68

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: 218.62  E-value: 5.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   1 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 80
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  81 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 160
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 261878618 161 MENNGRAQRIYEDHDATQQLQG 182
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 417-604 4.40e-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: 289.87  E-value: 4.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  417 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 494
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  495 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 574
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 261878618  575 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 604
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 1-182 5.80e-68

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: 218.62  E-value: 5.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   1 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 80
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  81 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 160
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 261878618 161 MENNGRAQRIYEDHDATQQLQG 182
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1-203 3.48e-34

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 131.76  E-value: 3.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   1 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASE--ANLQAAQDFVRGFSLDE 78
Cdd:COG2304   90 PPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR-----VLLPPTpaTDRAKILAAIDRLQAGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  79 ATNLNGGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 158
Cdd:COG2304  165 GTALGAGLELAYELARKHFI-----PGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLER 239

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 261878618 159 MSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDA 203
Cdd:COG2304  240 LADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-181 1.59e-24

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 100.61  E-value: 1.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618     4 NVVFVIDISGSMRGQKVKQTKEALLKILGDM---QPGDYFDLVLFGTRVQSWKGSLvqaSEANLQAAQDFVRGFSLD--E 78
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618    79 ATNLNGGLLRGIEILNqvQESLPELSNHASILIMLTDGDPTEGVTDrsqILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 158
Cdd:smart00327  78 GTNLGAALQYALENLF--SKSAGSRRGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 261878618   159 MSMENNGRAQRIYEDHDATQQLQ 181
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
4-186 2.27e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.57  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618    4 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQ-SWKGSLVQASEANLQAAQDFVrgFSLDEA 79
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRtEFPLNDYSSKEELLSAVDNLR--YLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   80 TNLNGGLLRGIEILNQVQESLPElsNHASILIMLTDGDPTEGvtdrsQILKNVRNAIRGRFPLYNLGFGhNVDFNFLEVM 159
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDEELRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 261878618  160 SMENNgrAQRIYEDHDATqQLQGFYSQ 186
Cdd:pfam00092 151 ASEPG--EGHVFTVSDFE-ALEDLQDQ 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 ...
 417-604 4.40e-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: 289.87  E-value: 4.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  417 NTGFSVNGQLIGNKARsPGQHD--GTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKK 494
Cdd:pfam06668   1 GSGVTVNGQLIGAKKP-PGSHKklRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  495 RNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRN 574
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 261878618  575 RRLTVTRGLQKDYSKDPWHGAEVSCWFIHN 604
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 1-182 5.80e-68

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: 218.62  E-value: 5.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   1 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEAT 80
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  81 NLNGGLLRGIEILNqvqeslpELSNHASILIMLTDGDptegVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMS 160
Cdd:cd01461   81 NMNDALEAALELLN-------SSPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 261878618 161 MENNGRAQRIYEDHDATQQLQG 182
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1-203 3.48e-34

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 131.76  E-value: 3.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   1 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASE--ANLQAAQDFVRGFSLDE 78
Cdd:COG2304   90 PPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR-----VLLPPTpaTDRAKILAAIDRLQAGG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  79 ATNLNGGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 158
Cdd:COG2304  165 GTALGAGLELAYELARKHFI-----PGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLER 239

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 261878618 159 MSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDA 203
Cdd:COG2304  240 LADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-181 1.59e-24

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 100.61  E-value: 1.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618     4 NVVFVIDISGSMRGQKVKQTKEALLKILGDM---QPGDYFDLVLFGTRVQSWKGSLvqaSEANLQAAQDFVRGFSLD--E 78
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618    79 ATNLNGGLLRGIEILNqvQESLPELSNHASILIMLTDGDPTEGVTDrsqILKNVRNAIRGRFPLYNLGFGHNVDFNFLEV 158
Cdd:smart00327  78 GTNLGAALQYALENLF--SKSAGSRRGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 261878618   159 MSMENNGRAQRIYEDHDATQQLQ 181
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-188 4.88e-22

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: 96.16  E-value: 4.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   4 NVVFVIDISGSMRGQ-KVKQTKEALLKILGDMQPGDYFDLVLFGTRVQswkgsLVQASEANLQAAQDFVRGFSLDEATNL 82
Cdd:COG1240   94 DVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE-----VLLPLTRDREALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  83 NGGLLRGIEILNQVQESLPelsnhaSILIMLTDGDPTEGVTDRSQILKNVRNAirgRFPLYNLGFGHN-VDFNFLEVMSM 161
Cdd:COG1240  169 GDALALALELLKRADPARR------KVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGTEaVDEGLLREIAE 239

                        170       180
                 ....*....|....*....|....*..
gi 261878618 162 ENNGRAQRIyedhDATQQLQGFYSQVA 188
Cdd:COG1240  240 ATGGRYFRA----DDLSELAAIYREID 262
VWA pfam00092
von Willebrand factor type A domain;
4-186 2.27e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 91.57  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618    4 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQ-SWKGSLVQASEANLQAAQDFVrgFSLDEA 79
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRtEFPLNDYSSKEELLSAVDNLR--YLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   80 TNLNGGLLRGIEILNQVQESLPElsNHASILIMLTDGDPTEGvtdrsQILKNVRNAIRGRFPLYNLGFGhNVDFNFLEVM 159
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDEELRKI 150

                         170       180
                  ....*....|....*....|....*..
gi 261878618  160 SMENNgrAQRIYEDHDATqQLQGFYSQ 186
Cdd:pfam00092 151 ASEPG--EGHVFTVSDFE-ALEDLQDQ 174
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1-160 2.54e-21

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 93.98  E-value: 2.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   1 MNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSwkgSLVQASEANLQAAQDFVRGFSLDEAT 80
Cdd:COG2425  117 LEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSGLFAGGGT 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  81 NLNGGLLRGIEILNQVQeslpelsNHASILIMLTDGDPTEgvtDRSQILKNVRNAiRGRFPLYNLGFGHNVDFNFLEVMS 160
Cdd:COG2425  194 DIAPALRAALELLEEPD-------YRNADIVLITDGEAGV---SPEELLREVRAK-ESGVRLFTVAIGDAGNPGLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-165 1.03e-20

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: 89.16  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   4 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQ---PGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRgFSLDEAT 80
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALK-KGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  81 NLNGGLLRGIEILNQvqeslPELSNHASILIMLTDGDPTEGVTDRSQILKNVRNAirgRFPLYNLGFGHNVDFNFLEVMS 160
Cdd:cd00198   81 NIGAALRLALELLKS-----AKRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                 ....*
gi 261878618 161 MENNG 165
Cdd:cd00198  153 DKTTG 157
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 4-170 2.19e-16

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: 76.93  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   4 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVqswkGSLVQASEANLQAA-QDFVRGFSLDEATNL 82
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATPVRDKAAiLAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  83 NGGLLRGIEILnqVQESLPELSNHasiLIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMSME 162
Cdd:cd01465   78 GAGIQLGYQEA--QKHFVPGGVNR---ILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADA 152


                 ....*...
gi 261878618 163 NNGRAQRI 170
Cdd:cd01465  153 GNGNTAYI 160
VWA_3 pfam13768
von Willebrand factor type A domain;
3-168 1.22e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.96  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618    3 KNVVFVIDISGSMRGQKVKQtKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDE-ATN 81
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPLgGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   82 LNGGLLRGIEilnqvQESLPELSNHasiLIMLTDGDPTEGVTDrsqILKNVRNAiRGRFPLYNLGFGHNVDFNFLEVMSM 161
Cdd:pfam13768  80 LLGALKEAVR-----APASPGYIRH---VLLLTDGSPMQGETR---VSDLISRA-PGKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 261878618  162 ENNGRAQ 168
Cdd:pfam13768 148 ASNGTYE 154
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
4-157 3.26e-11

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 62.63  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   4 NVVFVIDISGSMRGQKVKQTKEALLKILGDMQP------GDYFDLVLFGTRVQsWKGSLVQASEanLQAAQDFVRGfsld 77
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQdpyaleTVEVSVITFDGEAK-VLLPLTDLED--FQPPDLSASG---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  78 eATNLNGGLLRGIEIL-NQVQESLPE-LSNHASILIMLTDGDPTEgvTDRSQILKNVRNAIRGRFP-LYNLGFGHNVDFN 154
Cdd:COG4245   80 -GTPLGAALELLLDLIeRRVQKYTAEgKGDWRPVVFLITDGEPTD--SDWEAALQRLKDGEAAKKAnIFAIGVGPDADTE 156


                 ...
gi 261878618 155 FLE 157
Cdd:COG4245  157 VLK 159
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 5-165 7.63e-09

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: 55.09  E-value: 7.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   5 VVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTrvQSWKGS-LVQASEANLQAAQDFVRGFSLDEATNLN 83
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFST--SAKRLSpLRRMTAKGKRSAKRVVDGLQAGGGTNVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  84 GGLLRGIEILNQVQEslpelSNHASILIMLTDGDPTEGVTdrsqilknVRNAIRGRFPLYNLGFGHNVDFNFLEVMSMEN 163
Cdd:cd01466   81 GGLKKALKVLGDRRQ-----KNPVASIMLLSDGQDNHGAV--------VLRADNAPIPIHTFGLGASHDPALLAFIAEIT 147


                 ..
gi 261878618 164 NG 165
Cdd:cd01466  148 GG 149
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 3-188 3.29e-08

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


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 53.94  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   3 KNVVFVIDISGSMRGQK---VKQTKEALLKILGDmqpGDYFDLVLFGTRVQS----WKGSLVQASEANLQAAQDFVRGFS 75
Cdd:cd01463   14 KDIVILLDVSGSMTGQRlhlAKQTVSSILDTLSD---NDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618  76 LDEATNLNGGLLRGIEILNQVQESLpeLSNHASI---LIMLTdgdpTEGVTDR-SQILK--NVRNAIRGRFPLYNLGFG- 148
Cdd:cd01463   91 AKGIANYTKALEFAFSLLLKNLQSN--HSGSRSQcnqAIMLI----TDGVPENyKEIFDkyNWDKNSEIPVRVFTYLIGr 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 261878618 149 HNVDFNFLEVMSMENngraqriyedhdatqqlQGFYSQVA 188
Cdd:cd01463  165 EVTDRREIQWMACEN-----------------KGYYSHIQ 187
VWA_2 pfam13519
von Willebrand factor type A domain;
5-113 7.56e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.98  E-value: 7.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618    5 VVFVIDISGSMRGQKVKQT-----KEALLKILGDMqPGDYFDLVLFGTRVQ---SWKGSLVQASEAnLQAAQDFVRGfsl 76
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTrleaaKDAVLALLKSL-PGDRVGLVTFGDGPEvliPLTKDRAKILRA-LRRLEPKGGG--- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 261878618   77 deaTNLNGGLLRGIEILNQVQeslpelSNHASILIML 113
Cdd:pfam13519  76 ---TNLAAALQLARAALKHRR------KNQPRRIVLI 103
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-131 1.26e-04

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: 42.66  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   4 NVVFVIDISGSMRGQKVKQTKEALLKILgdmqpgDYFDLVLFGTRVqswkgSLVQAS-----EANLQAAQDF------VR 72
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLV------EKLDIGPDKTRV-----GLVQYSddvrvEFSLNDYKSKddllkaVK 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261878618  73 GFSLD--EATNLNGGLLRGIEILNQVQESlpeLSNHASILIMLTDGDPTEG--VTDRSQILKN 131
Cdd:cd01450   71 NLKYLggGGTNTGKALQYALEQLFSESNA---RENVPKVIIVLTDGRSDDGgdPKEAAAKLKD 130
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 5-123 1.05e-03

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: 40.34  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   5 VVFVIDISGSMRG-QKVKQTKEALLKILGD---------MQP--GDYFDLVLFGTRvqswkgSLVQASeanlQAAQDFVR 72
Cdd:cd01451    3 VIFVVDASGSMAArHRMAAAKGAVLSLLRDayqrrdkvaLIAfrGTEAEVLLPPTR------SVELAK----RRLARLPT 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 261878618  73 GfsldEATNLNGGLLRGIEILNQVQESLPElsnhASILIMLTDG------DPTEGVT 123
Cdd:cd01451   73 G----GGTPLAAGLLAAYELAAEQARDPGQ----RPLIVVITDGranvgpDPTADRA 121
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 3-134 7.89e-03

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 37.76  E-value: 7.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878618   3 KNVVFVIDISGSMRGQKVKQTK--EALLKILGDMQPGDYFDLVLFGTRVQswkgslvQASEANLQAAQD---FVRGFSLD 77
Cdd:cd01476    1 LDLLFVLDSSGSVRGKFEKYKKyiERIVEGLEIGPTATRVALITYSGRGR-------QRVRFNLPKHNDgeeLLEKVDNL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261878618  78 EA----TNLNGGLLRGieiLNQVQESLPELSNHASILIMLTDGDPTEGVTDRSQILKNVRN 134
Cdd:cd01476   74 RFiggtTATGAAIEVA---LQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPN 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • 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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