NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|313151177|ref|NP_001100761|]
View 

inter-alpha-trypsin inhibitor heavy chain H1 precursor [Rattus norvegicus]

Protein Classification

vWA_interalpha_trypsin_inhibitor and ITI_HC_C domain-containing protein( domain architecture ID 10652060)

protein containing domains VIT, vWA_interalpha_trypsin_inhibitor, and ITI_HC_C

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 698-884 1.10e-84

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: 269.07  E-value: 1.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  698 DTGFSVNGQLIGIKAGSPG-QHESTYFGRLGVSSPTSDFQLEVTPQNITLNPSSGGPVFSWRDQAVLQKDGVVVTINKKR 776
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGShKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  777 NLVVSVDDGATFEIVLHRTWRGSSIHQDFLGFYVLDSFRMSARTQGLLGQFFSPLDFEVFDLRPGSDPTKTDATMVVKNR 856
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*...
gi 313151177  857 QLTVTRGLQKDYSKDPRHGTEVSCWFVH 884
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVH 188
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 283-464 2.62e-69

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


:

Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 227.10  E-value: 2.62e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 283 MSKNLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSQVQSWKGSLVPASHANLQAAQDFVRRFSLAGAT 362
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 363 NLNGGLLRGIEILNRAQGShpelsspASILIMLTDGEptegETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 442
Cdd:cd01461   81 NMNDALEAALELLNSSPGS-------VPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 313151177 443 IENNGWAQRIYEDHDATQQLQG 464
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
33-160 6.93e-67

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 219.15  E-value: 6.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177    33 EKRQAVDTTVNGVSIRSLKVNCKVTSRFAHYVITSQVVNSANKAREVAFDVEIPKTAFISDFAITADGNAFIGDIKDKVT 112
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 313151177   113 AWKQYRKAAISGENAGLVRASGRNMEQFTIHITVGAQSKATFQLTYEE 160
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 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 ...
 698-884 1.10e-84

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: 269.07  E-value: 1.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  698 DTGFSVNGQLIGIKAGSPG-QHESTYFGRLGVSSPTSDFQLEVTPQNITLNPSSGGPVFSWRDQAVLQKDGVVVTINKKR 776
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGShKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  777 NLVVSVDDGATFEIVLHRTWRGSSIHQDFLGFYVLDSFRMSARTQGLLGQFFSPLDFEVFDLRPGSDPTKTDATMVVKNR 856
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*...
gi 313151177  857 QLTVTRGLQKDYSKDPRHGTEVSCWFVH 884
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVH 188
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 283-464 2.62e-69

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 227.10  E-value: 2.62e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 283 MSKNLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSQVQSWKGSLVPASHANLQAAQDFVRRFSLAGAT 362
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 363 NLNGGLLRGIEILNRAQGShpelsspASILIMLTDGEptegETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 442
Cdd:cd01461   81 NMNDALEAALELLNSSPGS-------VPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 313151177 443 IENNGWAQRIYEDHDATQQLQG 464
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
33-160 6.93e-67

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 219.15  E-value: 6.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177    33 EKRQAVDTTVNGVSIRSLKVNCKVTSRFAHYVITSQVVNSANKAREVAFDVEIPKTAFISDFAITADGNAFIGDIKDKVT 112
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 313151177   113 AWKQYRKAAISGENAGLVRASGRNMEQFTIHITVGAQSKATFQLTYEE 160
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 285-485 1.05e-33

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 131.38  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 285 KNLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSQVQswkgSLVPASHA-NLQAAQDFVRRFSLAGATN 363
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR----VLLPPTPAtDRAKILAAIDRLQAGGGTA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 364 LNGGLLRGIEILNRAQGSHpelssPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMSI 443
Cdd:COG2304  168 LGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAD 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313151177 444 ENNGWAQRIYEDHDATQQLQGFYNQVAHPLLTDVELQYPQDA 485
Cdd:COG2304  243 AGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 47-158 2.62e-30

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: 115.27  E-value: 2.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177   47 IRSLKVNCKVTSRFAHYVITSQVVNSANKAREVAFDVEIPKTAFISDFAITADGNAFIGDIKDKVTAWKQYRKAAISGEN 126
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 313151177  127 AGLVRASGrnMEQFTIHI-TVGAQSKATFQLTY 158
Cdd:pfam08487  81 AGLLEQDT--PDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 286-447 1.10e-23

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: 98.68  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177   286 NLVFVIDISGSMEGQKVKQTKEALLKILGDM---KPVDNFDLVLFGSQVQSWKGslvPASHANLQAAQDFVRRFS--LAG 360
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFP---LNDSRSKDALLEALASLSykLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177   361 ATNLNGGLLRGIEILNRAQGSHPElsSPASILIMLTDGEPTEGETDrsqILKNVRNAIRGRFPLYNLGFGHDLDFSFLEV 440
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRR--GAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*..
gi 313151177   441 MSIENNG 447
Cdd:smart00327 153 LASAPGG 159
VWA pfam00092
von Willebrand factor type A domain;
286-468 3.46e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 88.87  E-value: 3.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  286 NLVFVIDISGSMEGQKVKQTKEALLKILGDM---KPVDNFDLVLFGSQVQSWKgSLvpASHANLQAAQDFVRRFSLA--G 360
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEF-PL--NDYSSKEELLSAVDNLRYLggG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  361 ATNLNGGLLRGIE-ILNRAQGSHPELSspaSILIMLTDGEPTEGEtdrsqILKNVRNAIRGRFPLYNLGFGHDlDFSFLE 439
Cdd:pfam00092  78 TTNTGKALKYALEnLFSSAAGARPGAP---KVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNA-DDEELR 148

                         170       180
                  ....*....|....*....|....*....
gi 313151177  440 VMSIENNgwAQRIYEDHDATqQLQGFYNQ 468
Cdd:pfam00092 149 KIASEPG--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 ...
 698-884 1.10e-84

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: 269.07  E-value: 1.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  698 DTGFSVNGQLIGIKAGSPG-QHESTYFGRLGVSSPTSDFQLEVTPQNITLNPSSGGPVFSWRDQAVLQKDGVVVTINKKR 776
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGShKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  777 NLVVSVDDGATFEIVLHRTWRGSSIHQDFLGFYVLDSFRMSARTQGLLGQFFSPLDFEVFDLRPGSDPTKTDATMVVKNR 856
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*...
gi 313151177  857 QLTVTRGLQKDYSKDPRHGTEVSCWFVH 884
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVH 188
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 283-464 2.62e-69

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 227.10  E-value: 2.62e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 283 MSKNLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSQVQSWKGSLVPASHANLQAAQDFVRRFSLAGAT 362
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 363 NLNGGLLRGIEILNRAQGShpelsspASILIMLTDGEptegETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMS 442
Cdd:cd01461   81 NMNDALEAALELLNSSPGS-------VPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 313151177 443 IENNGWAQRIYEDHDATQQLQG 464
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
33-160 6.93e-67

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 219.15  E-value: 6.93e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177    33 EKRQAVDTTVNGVSIRSLKVNCKVTSRFAHYVITSQVVNSANKAREVAFDVEIPKTAFISDFAITADGNAFIGDIKDKVT 112
Cdd:smart00609   3 GKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 313151177   113 AWKQYRKAAISGENAGLVRASGRNMEQFTIHITVGAQSKATFQLTYEE 160
Cdd:smart00609  83 AQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 285-485 1.05e-33

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 131.38  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 285 KNLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSQVQswkgSLVPASHA-NLQAAQDFVRRFSLAGATN 363
Cdd:COG2304   92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDAR----VLLPPTPAtDRAKILAAIDRLQAGGGTA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 364 LNGGLLRGIEILNRAQGSHpelssPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMSI 443
Cdd:COG2304  168 LGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLERLAD 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313151177 444 ENNGWAQRIYEDHDATQQLQGFYNQVAHPLLTDVELQYPQDA 485
Cdd:COG2304  243 AGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPLPY 284
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 47-158 2.62e-30

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: 115.27  E-value: 2.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177   47 IRSLKVNCKVTSRFAHYVITSQVVNSANKAREVAFDVEIPKTAFISDFAITADGNAFIGDIKDKVTAWKQYRKAAISGEN 126
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 313151177  127 AGLVRASGrnMEQFTIHI-TVGAQSKATFQLTY 158
Cdd:pfam08487  81 AGLLEQDT--PDVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 286-447 1.10e-23

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: 98.68  E-value: 1.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177   286 NLVFVIDISGSMEGQKVKQTKEALLKILGDM---KPVDNFDLVLFGSQVQSWKGslvPASHANLQAAQDFVRRFS--LAG 360
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFP---LNDSRSKDALLEALASLSykLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177   361 ATNLNGGLLRGIEILNRAQGSHPElsSPASILIMLTDGEPTEGETDrsqILKNVRNAIRGRFPLYNLGFGHDLDFSFLEV 440
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRR--GAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152


                   ....*..
gi 313151177   441 MSIENNG 447
Cdd:smart00327 153 LASAPGG 159
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 276-442 1.75e-22

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 98.21  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 276 APQNLTNMSKNLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSQVQSwkgSLVPASHANLQAAQDFVRR 355
Cdd:COG2425  110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 356 FSLAGATNLNGGLLRGIEILNRAQGshpelssPASILIMLTDGEPTEGETDrsqILKNVRNAiRGRFPLYNLGFGHDLDF 435
Cdd:COG2425  187 LFAGGGTDIAPALRAALELLEEPDY-------RNADIVLITDGEAGVSPEE---LLREVRAK-ESGVRLFTVAIGDAGNP 255


                 ....*..
gi 313151177 436 SFLEVMS 442
Cdd:COG2425  256 GLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 286-447 1.93e-21

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: 91.86  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 286 NLVFVIDISGSMEGQKVKQTKEALLKILGDMKPV---DNFDLVLFGSQVQSWKGSLVPASHANLQAAQDFVrRFSLAGAT 362
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAL-KKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 363 NLNGGLLRGIEILNRAQGSHPElsspaSILIMLTDGEPTEGETDRSQILKNVRNAirgRFPLYNLGFGHDLDFSFLEVMS 442
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNAR-----RVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                 ....*
gi 313151177 443 IENNG 447
Cdd:cd00198  153 DKTTG 157
VWA pfam00092
von Willebrand factor type A domain;
286-468 3.46e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 88.87  E-value: 3.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  286 NLVFVIDISGSMEGQKVKQTKEALLKILGDM---KPVDNFDLVLFGSQVQSWKgSLvpASHANLQAAQDFVRRFSLA--G 360
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEF-PL--NDYSSKEELLSAVDNLRYLggG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  361 ATNLNGGLLRGIE-ILNRAQGSHPELSspaSILIMLTDGEPTEGEtdrsqILKNVRNAIRGRFPLYNLGFGHDlDFSFLE 439
Cdd:pfam00092  78 TTNTGKALKYALEnLFSSAAGARPGAP---KVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNA-DDEELR 148

                         170       180
                  ....*....|....*....|....*....
gi 313151177  440 VMSIENNgwAQRIYEDHDATqQLQGFYNQ 468
Cdd:pfam00092 149 KIASEPG--EGHVFTVSDFE-ALEDLQDQ 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 286-470 1.19e-19

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: 89.61  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 286 NLVFVIDISGSMEGQ-KVKQTKEALLKILGDMKPVDNFDLVLFGSQVQswkgSLVPASHaNLQAAQDFVRRFSLAGATNL 364
Cdd:COG1240   94 DVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE----VLLPLTR-DREALKRALDELPPGGGTPL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 365 NGGLLRGIEILNRAQgshpelSSPASILIMLTDGEPTEGETDRSQILKNVRNAirgRFPLYNLGFGHD-LDFSFLEVMSI 443
Cdd:COG1240  169 GDALALALELLKRAD------PARRKVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGTEaVDEGLLREIAE 239

                        170       180
                 ....*....|....*....|....*..
gi 313151177 444 ENNGWAQRIyedhDATQQLQGFYNQVA 470
Cdd:COG1240  240 ATGGRYFRA----DDLSELAAIYREID 262
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 286-447 1.64e-18

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: 83.86  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 286 NLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSQVqswkGSLVPASHANLQAA-QDFVRRFSLAGATNL 364
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATPVRDKAAiLAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 365 NGGLLRGIEILNRAQGshpelSSPASILIMLTDGEPTEGETDRSQILKNVRNAIRGRFPLYNLGFGHDLDFSFLEVMSIE 444
Cdd:cd01465   78 GAGIQLGYQEAQKHFV-----PGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADA 152


                 ...
gi 313151177 445 NNG 447
Cdd:cd01465  153 GNG 155
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
288-439 7.53e-13

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 68.03  E-value: 7.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 288 VFVIDISGSMEGQKVKQTKEALLKILGDMKPVDN------FDLVLFGSQVQswkgSLVPashanLQAAQDF-VRRFSLAG 360
Cdd:COG4245    9 YLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletveVSVITFDGEAK----VLLP-----LTDLEDFqPPDLSASG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 361 ATNLNGGLLRGIEILNRAQGSHPELSSPA--SILIMLTDGEPTEGETdrSQILKNVRNAIRGRFP-LYNLGFGHDLDFSF 437
Cdd:COG4245   80 GTPLGAALELLLDLIERRVQKYTAEGKGDwrPVVFLITDGEPTDSDW--EAALQRLKDGEAAKKAnIFAIGVGPDADTEV 157


                 ..
gi 313151177 438 LE 439
Cdd:COG4245  158 LK 159
VWA_3 pfam13768
von Willebrand factor type A domain;
285-450 1.33e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 66.27  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  285 KNLVFVIDISGSMEGQKVKQtKEALLKILGDMKPVDNFDLVLFGSQVQSWKGSLVPASHANLQAAQDFVRRFSLA-GATN 363
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  364 LNGGLLRGIeilnrAQGSHPElsSPASILIMlTDGEPTEGETDrsqILKNVRNAiRGRFPLYNLGFGHDLDFSFLEVMSI 443
Cdd:pfam13768  80 LLGALKEAV-----RAPASPG--YIRHVLLL-TDGSPMQGETR---VSDLISRA-PGKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 313151177  444 ENNGWAQ 450
Cdd:pfam13768 148 ASNGTYE 154
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 287-434 1.18e-08

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: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 287 LVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDNFDLVLFGSqvQSWKGS-LVPASHANLQAAQDFVRRFSLAGATNLN 365
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFST--SAKRLSpLRRMTAKGKRSAKRVVDGLQAGGGTNVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313151177 366 GGLLRGIEILNRAQGshpelSSPASILIMLTDGEPTEGETdrsqilknVRNAIRGRFPLYNLGFGHDLD 434
Cdd:cd01466   81 GGLKKALKVLGDRRQ-----KNPVASIMLLSDGQDNHGAV--------VLRADNAPIPIHTFGLGASHD 136
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 284-400 2.17e-07

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: 52.01  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 284 SKNLVFVIDISGSMEGQK---VKQTKEALLKILGDMkpvDNFDLVLFGSQVQS----WKGSLVPASHANLQAAQDFVRRF 356
Cdd:cd01463   13 PKDIVILLDVSGSMTGQRlhlAKQTVSSILDTLSDN---DFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDML 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 313151177 357 SLAGATNLNGGLLRGIEIL-NRAQGSHPELSSPASILIML-TDGEP 400
Cdd:cd01463   90 EAKGIANYTKALEFAFSLLlKNLQSNHSGSRSQCNQAIMLiTDGVP 135
VWA_2 pfam13519
von Willebrand factor type A domain;
287-383 3.14e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.52  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177  287 LVFVIDISGSMEGQKVKQT-----KEALLKILGDMkPVDNFDLVLFGSQVQ---SWKGslvpashaNLQAAQDFVRRF-S 357
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTrleaaKDAVLALLKSL-PGDRVGLVTFGDGPEvliPLTK--------DRAKILRALRRLeP 71

                          90       100
                  ....*....|....*....|....*.
gi 313151177  358 LAGATNLNGGLLRGIEILNRAQGSHP 383
Cdd:pfam13519  72 KGGGTNLAAALQLARAALKHRRKNQP 97
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 286-403 1.36e-05

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: 46.50  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 286 NLV-FVIDISGSMEG-QKVKQTKEALLKILGD---MKpvDNFDLVLF-GSQVQswkgSLVPASHaNLQAAQDFVRRFSLA 359
Cdd:cd01451    1 NLViFVVDASGSMAArHRMAAAKGAVLSLLRDayqRR--DKVALIAFrGTEAE----VLLPPTR-SVELAKRRLARLPTG 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 313151177 360 GATNLNGGLLRGIEILNRAQGSHPElsspASILIMLTDGEPTEG 403
Cdd:cd01451   74 GGTPLAAGLLAAYELAAEQARDPGQ----RPLIVVITDGRANVG 113
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 286-413 2.11e-05

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 45.75  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 286 NLVFVIDISGSMEGQKVKQTKEALLKILGDMKPVDN---FDLVLFGSQVQSWKGSLVPASHANLQAAQDFVRRFSlAGAT 362
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDktrVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLG-GGGT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 313151177 363 NLNGGLLRGIEILnrAQGSHPELSSPaSILIMLTDGEPTEGET--DRSQILKN 413
Cdd:cd01450   81 NTGKALQYALEQL--FSESNARENVP-KVIIVLTDGRSDDGGDpkEAAAKLKD 130
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 286-421 1.23e-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: 43.91  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 286 NLVFVIDISGSMEGQ----KVKQTKEALLKILGDMKPVDNFDLVLFGSQVQS-WKGSLVPASHAN--LQAAQDFVRRFSL 358
Cdd:cd01471    2 DLYLLVDGSGSIGYSnwvtHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKElIRLSSPNSTNKDlaLNAIRALLSLYYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313151177 359 AGATNLNGGLLRGIEILNRAQGSHPelSSPASILIMlTDGEPtegeTDRSQILKNVRnAIRGR 421
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFDTRGNRE--NAPQLVIIM-TDGIP----DSKFRTLKEAR-KLRER 136
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 288-434 1.35e-03

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: 40.79  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151177 288 VFVIDISGSMEGQKVKQTKEALLKILGDMKPvDNFDL-------VLFGSQVQSwKGSLVPAShanlqaaQDFVRRFSLAG 360
Cdd:cd01464    7 YLLLDTSGSMAGEPIEALNQGLQMLQSELRQ-DPYALesveisvITFDSAARV-IVPLTPLE-------SFQPPRLTASG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313151177 361 ATNLNGGLLRGIEILNR----AQGSHPELSSPasILIMLTDGEPTEGETDRSQILKNVRNAiRGRFPLYNLGFGHDLD 434
Cdd:cd01464   78 GTSMGAALELALDCIDRrvqrYRADQKGDWRP--WVFLLTDGEPTDDLTAAIERIKEARDS-KGRIVACAVGPKADLD 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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