NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|312434033|ref|NP_116206|]
View 

inter-alpha-trypsin inhibitor heavy chain H5 isoform 2 [Homo sapiens]

Protein Classification

vWA_interalpha_trypsin_inhibitor and ITI_HC_C domain-containing protein( domain architecture ID 10106957)

protein containing domains VIT_2, 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 ...
 501-695 1.52e-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: 267.91  E-value: 1.52e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  501 DSGVTVNGELIGAPAPPNGHKKQRTYLRTITILiNKPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSWGLEVSVSAN 579
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  580 ANVTVTIQGSIAFVILIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQ-DARLTEDPAGpsqnlthplllQVG 658
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPG-----------SDP 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 312434033  659 EGPEAVLTVKGHQVPVVWKQRKIYNGE----EQIDCWFARN 695
Cdd:pfam06668 149 EKPDATMKVKGHKLPVTRGWQKDYRGDrkhgTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 78-259 3.42e-74

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: 237.50  E-value: 3.42e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  78 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPTGGT 157
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 158 DINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLS 237
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 312434033 238 LENCGLTRRVHEEEDAGSQLIG 259
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 ...
 501-695 1.52e-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: 267.91  E-value: 1.52e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  501 DSGVTVNGELIGAPAPPNGHKKQRTYLRTITILiNKPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSWGLEVSVSAN 579
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  580 ANVTVTIQGSIAFVILIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQ-DARLTEDPAGpsqnlthplllQVG 658
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPG-----------SDP 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 312434033  659 EGPEAVLTVKGHQVPVVWKQRKIYNGE----EQIDCWFARN 695
Cdd:pfam06668 149 EKPDATMKVKGHKLPVTRGWQKDYRGDrkhgTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 78-259 3.42e-74

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: 237.50  E-value: 3.42e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  78 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPTGGT 157
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 158 DINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLS 237
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 312434033 238 LENCGLTRRVHEEEDAGSQLIG 259
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 63-278 5.85e-38

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 142.93  E-value: 5.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  63 NGYFVHYFAPKDLPP---LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTP- 138
Cdd:COG2304   72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPa 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 139 DSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYvahsGIGDRsVSLIVFLTDGKPTVGETHTLKILNNTREAARGQVC 218
Cdd:COG2304  148 TDRAKILAAIDRLQAGGGTALGAGLELAYELARKH----FIPGR-VNRVILLTDGDANVGITDPEELLKLAEEAREEGIT 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 219 IFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIRIDYPP 278
Cdd:COG2304  223 LTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPL 282
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 81-253 1.36e-27

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: 109.85  E-value: 1.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033    81 NVVFVLDSSASMVGTKLRQTKDALFTILHDLR---PQDRFSIIGFSNRIKVWKDHLISVTPDSIRDgkvYIHHMSPT--G 155
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLE---ALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   156 GTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGNDVDFRLLEK 235
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---KELKRSGVKVFVVGVGNDVDEEELKK 152

                          170
                   ....*....|....*...
gi 312434033   236 LSLENCGltRRVHEEEDA 253
Cdd:smart00327 153 LASAPGG--VYVFLPELL 168
VWA pfam00092
von Willebrand factor type A domain;
81-240 1.65e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 89.26  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   81 NVVFVLDSSASMVGTKLRQTKDALFTILHDL---RPQDRFSIIGFSNRIKVW--------KDHLISvtpdSIRDGKVyih 149
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEfplndyssKEELLS----AVDNLRY--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  150 hmSPTGGTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGEthtlkILNNTREAARGQVCIFTIGIGNDVD 229
Cdd:pfam00092  74 --LGGGTTNTGKALKYALENLFSSAAGARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADD 144

                         170
                  ....*....|.
gi 312434033  230 fRLLEKLSLEN 240
Cdd:pfam00092 145 -EELRKIASEP 154
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 78-232 1.11e-05

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 48.07  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   78 LPKNVVFVLDSSASMVGtKLRQTKDALFTIL-HDLRPQDRFSIIGFSNR----------IKVWKDHLISVTPDSIRDGKV 146
Cdd:TIGR03436  52 LPLTVGLVIDTSGSMRN-DLDRARAAAIRFLkTVLRPNDRVFVVTFNTRlrllqdftsdPRLLEAALNRLKPPLRTDYNS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  147 YIHHMSPTGGTdingALQRAIRL--LNKYVAH-SGIGDRSVsLIVFlTDGkptVGETHTLKILNNTREAARGQVCIFTIG 223
Cdd:TIGR03436 131 SGAFVRDGGGT----ALYDAITLaaLEQLANAlAGIPGRKA-LIVI-SDG---GDNRSRDTLERAIDAAQRADVAIYSID 201


                  ....*....
gi 312434033  224 IGNDVDFRL 232
Cdd:TIGR03436 202 ARGLRAPDL 210
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 501-695 1.52e-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: 267.91  E-value: 1.52e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  501 DSGVTVNGELIGAPAPPNGHKKQRTYLRTITILiNKPERSYLEITPSRVIL-DGGDRLVLPCNQSVVVGSWGLEVSVSAN 579
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLkDGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  580 ANVTVTIQGSIAFVILIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQ-DARLTEDPAGpsqnlthplllQVG 658
Cdd:pfam06668  80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPG-----------SDP 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 312434033  659 EGPEAVLTVKGHQVPVVWKQRKIYNGE----EQIDCWFARN 695
Cdd:pfam06668 149 EKPDATMKVKGHKLPVTRGWQKDYRGDrkhgTNVPCWFVHN 189
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 78-259 3.42e-74

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: 237.50  E-value: 3.42e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  78 LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPTGGT 157
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 158 DINGALQRAIRLLNKyvahsgiGDRSVSLIVFLTDGKptvgETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLS 237
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 312434033 238 LENCGLTRRVHEEEDAGSQLIG 259
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 63-278 5.85e-38

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 142.93  E-value: 5.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  63 NGYFVHYFAPKDLPP---LPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTP- 138
Cdd:COG2304   72 TRLLLVGLQPPKAAAeerPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPa 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 139 DSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYvahsGIGDRsVSLIVFLTDGKPTVGETHTLKILNNTREAARGQVC 218
Cdd:COG2304  148 TDRAKILAAIDRLQAGGGTALGAGLELAYELARKH----FIPGR-VNRVILLTDGDANVGITDPEELLKLAEEAREEGIT 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 219 IFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIRIDYPP 278
Cdd:COG2304  223 LTTLGVGSDYNEDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFPL 282
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 76-237 9.45e-28

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 112.85  E-value: 9.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  76 PPLPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdHLISVTPDSIRDGKVYIHHMSPTG 155
Cdd:COG2425  115 PLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE---DLPLTADDGLEDAIEFLSGLFAGG 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 156 GTDINGALQRAIRLLNKYVAHSGIgdrsvslIVFLTDGKPTVGETHTLKILNntreAARGQVCIFTIGIGNDVDFRLLEK 235
Cdd:COG2425  192 GTDIAPALRAALELLEEPDYRNAD-------IVLITDGEAGVSPEELLREVR----AKESGVRLFTVAIGDAGNPGLLEA 260


                 ..
gi 312434033 236 LS 237
Cdd:COG2425  261 LA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 81-253 1.36e-27

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: 109.85  E-value: 1.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033    81 NVVFVLDSSASMVGTKLRQTKDALFTILHDLR---PQDRFSIIGFSNRIKVWKDHLISVTPDSIRDgkvYIHHMSPT--G 155
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLE---ALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   156 GTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGNDVDFRLLEK 235
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKDLLKAA---KELKRSGVKVFVVGVGNDVDEEELKK 152

                          170
                   ....*....|....*...
gi 312434033   236 LSLENCGltRRVHEEEDA 253
Cdd:smart00327 153 LASAPGG--VYVFLPELL 168
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 76-237 6.00e-26

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: 107.72  E-value: 6.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  76 PPLPKNVVFVLDSSASMVG-TKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTPDsIRDGKVYIHHMSPT 154
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV----LLPLTRD-REALKRALDELPPG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 155 GGTDINGALQRAIRLLNKYvahsgiGDRSVSLIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGND-VDFRLL 233
Cdd:COG1240  164 GGTPLGDALALALELLKRA------DPARRKVIVLLTDGRDNAGRIDPLEAA---ELAAAAGIRIYTIGVGTEaVDEGLL 234


                 ....
gi 312434033 234 EKLS 237
Cdd:COG1240  235 REIA 238
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 81-237 1.20e-23

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: 98.02  E-value: 1.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  81 NVVFVLDSSASMVGTKLRQTKDALFTILHDL---RPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHmSPTGGT 157
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 158 DINGALQRAIRLLNKYvahsgIGDRSVSLIVFLTDGKPTVGETHTLKILNNTREAargQVCIFTIGIGNDVDFRLLEKLS 237
Cdd:cd00198   81 NIGAALRLALELLKSA-----KRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
76-237 4.78e-22

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 94.61  E-value: 4.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  76 PPLPknVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQD------RFSIIGFSNRIKVwkdhlisVTPDSIRDgKVYIH 149
Cdd:COG4245    4 RRLP--VYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGEAKV-------LLPLTDLE-DFQPP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 150 HMSPTGGTDINGALQRAIRLLNKYVAHS---GIGDRSVsLIVFLTDGKPTVGETHT-LKILNNTREAARGQvcIFTIGIG 225
Cdd:COG4245   74 DLSASGGTPLGAALELLLDLIERRVQKYtaeGKGDWRP-VVFLITDGEPTDSDWEAaLQRLKDGEAAKKAN--IFAIGVG 150

                        170
                 ....*....|..
gi 312434033 226 NDVDFRLLEKLS 237
Cdd:COG4245  151 PDADTEVLKQLT 162
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 81-236 4.85e-22

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: 93.49  E-value: 4.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  81 NVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVwkdhLISVTP----DSIRDGkvyIHHMSPTGG 156
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----VLPATPvrdkAAILAA---IDRLTAGGS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 157 TDINGALQRAIRLLNKyvahsGIGDRSVSLIVFLTDGKPTVGETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKL 236
Cdd:cd01465   75 TAGGAGIQLGYQEAQK-----HFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149
VWA pfam00092
von Willebrand factor type A domain;
81-240 1.65e-20

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 89.26  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   81 NVVFVLDSSASMVGTKLRQTKDALFTILHDL---RPQDRFSIIGFSNRIKVW--------KDHLISvtpdSIRDGKVyih 149
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEfplndyssKEELLS----AVDNLRY--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  150 hmSPTGGTDINGALQRAIRLLNKYVAHSGIGDRSVslIVFLTDGKPTVGEthtlkILNNTREAARGQVCIFTIGIGNDVD 229
Cdd:pfam00092  74 --LGGGTTNTGKALKYALENLFSSAAGARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADD 144

                         170
                  ....*....|.
gi 312434033  230 fRLLEKLSLEN 240
Cdd:pfam00092 145 -EELRKIASEP 154
VWA_3 pfam13768
von Willebrand factor type A domain;
80-237 1.08e-16

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 77.82  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   80 KNVVFVLDSSASMVGTKLRQtKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPT-GGTD 158
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312434033  159 INGALQRAIRLLnkyvAHSGIgdrsVSLIVFLTDGKPTVGETHTLKILnntrEAARGQVCIFTIGIGNDVDFRLLEKLS 237
Cdd:pfam13768  80 LLGALKEAVRAP----ASPGY----IRHVLLLTDGSPMQGETRVSDLI----SRAPGKIRFFAYGLGASISAPMLQLLA 146
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 79-242 2.13e-13

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: 69.35  E-value: 2.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  79 PKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIK----VWKDHLISVTPDSIRDGKVYIHHMSPT 154
Cdd:cd01463   13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNpvvpCFNDTLVQATTSNKKVLKEALDMLEAK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 155 GGTDINGALQRAIRLLNKYVAHSGIGDRSV--SLIVFLTDGKPtvgETHTlKILN--NTREAARGQVCIFTIGIGNDV-D 229
Cdd:cd01463   93 GIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDGVP---ENYK-EIFDkyNWDKNSEIPVRVFTYLIGREVtD 168

                        170
                 ....*....|...
gi 312434033 230 FRLLEKLSLENCG 242
Cdd:cd01463  169 RREIQWMACENKG 181
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 82-237 2.67e-13

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: 68.19  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  82 VVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDhLISVTPDSIRDGKVYIHHMSPTGGTDING 161
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312434033 162 ALQRAIRLLNKyvahSGIGDRSVSLIVfLTDGKPTVGETHTlkilnntrEAARGQVCIFTIGIGNDVDFRLLEKLS 237
Cdd:cd01466   82 GLKKALKVLGD----RRQKNPVASIML-LSDGQDNHGAVVL--------RADNAPIPIHTFGLGASHDPALLAFIA 144
VWA_2 pfam13519
von Willebrand factor type A domain;
82-172 8.75e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 59.23  E-value: 8.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   82 VVFVLDSSASM-----VGTKLRQTKDALFTILHDLrPQDRFSIIGFSNRIKVwkdhLISVTpDSIRDGKVYIHHMSPT-G 155
Cdd:pfam13519   1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPEV----LIPLT-KDRAKILRALRRLEPKgG 74

                          90
                  ....*....|....*..
gi 312434033  156 GTDINGALQRAIRLLNK 172
Cdd:pfam13519  75 GTNLAAALQLARAALKH 91
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 81-237 4.13e-10

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 58.84  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  81 NVVFVLDSSASMVGTKLRQTKDALFTILHDLRP---QDRFSIIGFSNRIKVW--------KDHLISvtpdSIRDgkvyIH 149
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpdKTRVGLVQYSDDVRVEfslndyksKDDLLK----AVKN----LK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 150 HMSPtGGTDINGALQRAIRLLNKyvaHSGIGDRSVSLIVFLTDGKPTVGEthtlKILNNTREAARGQVCIFTIGIGnDVD 229
Cdd:cd01450   74 YLGG-GGTNTGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGG----DPKEAAAKLKDEGIKVFVVGVG-PAD 144


                 ....*...
gi 312434033 230 FRLLEKLS 237
Cdd:cd01450  145 EEELREIA 152
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 78-237 7.88e-10

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: 58.51  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  78 LPknVVFVLDSSASMVGTKLRQTKDALFTILHDLRpQDRF-------SIIGFSNRIKVWKDhLISVTpdsirdgKVYIHH 150
Cdd:cd01464    4 LP--IYLLLDTSGSMAGEPIEALNQGLQMLQSELR-QDPYalesveiSVITFDSAARVIVP-LTPLE-------SFQPPR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 151 MSPTGGTDINGALQRAIRLLN----KYVAhSGIGDRSvSLIVFLTDGKPTVGETHTLKILnntREAARGQVCIFTIGIGN 226
Cdd:cd01464   73 LTASGGTSMGAALELALDCIDrrvqRYRA-DQKGDWR-PWVFLLTDGEPTDDLTAAIERI---KEARDSKGRIVACAVGP 147

                        170
                 ....*....|.
gi 312434033 227 DVDFRLLEKLS 237
Cdd:cd01464  148 KADLDTLKQIT 158
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 82-198 2.88e-06

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: 48.04  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  82 VVFVLDSSASM-VGTKLRQTKDALFTILHD-LRPQDRFSIIGFSNRIkvwKDHLISVTpDSIRDGKVYIHHMSPTGGTDI 159
Cdd:cd01451    3 VIFVVDASGSMaARHRMAAAKGAVLSLLRDaYQRRDKVALIAFRGTE---AEVLLPPT-RSVELAKRRLARLPTGGGTPL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 312434033 160 NGALQRAIRLLNKYVAHSGIgdrsVSLIVFLTDGKPTVG 198
Cdd:cd01451   79 AAGLLAAYELAAEQARDPGQ----RPLIVVITDGRANVG 113
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 82-228 6.49e-06

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 46.94  E-value: 6.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  82 VVFVLDSSASMVGT-KLRQTKDALFtILHD--LRPQDRFSIIGFSNRIKV--WKDHLISVTPDSIRDGKVY--IHHMSPT 154
Cdd:cd01454    3 VTLLLDLSGSMRSDrRIDVAKKAAV-LLAEalEACGVPHAILGFTTDAGGreRVRWIKIKDFDESLHERARkrLAALSPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 155 GGTDINGALQRAIRLLNKYVAHSGIgdrsvsLIVFlTDGKPTVGETHTLKI------LNNTREAARGQVCIFTIGIGNDV 228
Cdd:cd01454   82 GNTRDGAAIRHAAERLLARPEKRKI------LLVI-SDGEPNDLDYYEGNVfatedaLRAVIEARKLGIEVFGITIDRDA 154
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 78-232 1.11e-05

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 48.07  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033   78 LPKNVVFVLDSSASMVGtKLRQTKDALFTIL-HDLRPQDRFSIIGFSNR----------IKVWKDHLISVTPDSIRDGKV 146
Cdd:TIGR03436  52 LPLTVGLVIDTSGSMRN-DLDRARAAAIRFLkTVLRPNDRVFVVTFNTRlrllqdftsdPRLLEAALNRLKPPLRTDYNS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  147 YIHHMSPTGGTdingALQRAIRL--LNKYVAH-SGIGDRSVsLIVFlTDGkptVGETHTLKILNNTREAARGQVCIFTIG 223
Cdd:TIGR03436 131 SGAFVRDGGGT----ALYDAITLaaLEQLANAlAGIPGRKA-LIVI-SDG---GDNRSRDTLERAIDAAQRADVAIYSID 201


                  ....*....
gi 312434033  224 IGNDVDFRL 232
Cdd:TIGR03436 202 ARGLRAPDL 210
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 80-228 7.65e-05

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: 43.76  E-value: 7.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  80 KNVVFVLDSSASMVGTKLRQTKDALFTILHDL--RPQD-RFSIIGFSNRIKVWKDHLISVTPDSIRDGkvyIHHMSPTGG 156
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGvRVGVVQYSDDPRTEFYLNTYRSKDDVLEA---VKNLRYIGG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312434033 157 -TDINGALQRAIRLLnkYVAHSGIGDRSVSLIVFLTDGKPTVGethtlkILNNTREAARGQVCIFTIGIGNDV 228
Cdd:cd01472   78 gTNTGKALKYVRENL--FTEASGSREGVPKVLVVITDGKSQDD------VEEPAVELKQAGIEVFAVGVKNAD 142
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 76-229 1.08e-04

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: 43.96  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  76 PPLPKNVVFVLDSSASMV------GTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDhlISVT-PDSIRDGKVYI 148
Cdd:cd01456   17 PQLPPNVAIVLDNSGSMRevdgggETRLDNAKAALDETANALPDGTRLGLWTFSGDGDNPLD--VRVLvPKGCLTAPVNG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 149 HHM--------------SPTGGTDINGALQRAirllnkyvAHSgIGDRSVSLIVFLTDGKPTVGETH--TLKILNNTREA 212
Cdd:cd01456   95 FPSaqrsaldaalnslqTPTGWTPLAAALAEA--------AAY-VDPGRVNVVVLITDGEDTCGPDPceVARELAKRRTP 165

                        170
                 ....*....|....*..
gi 312434033 213 ARGqVCIFTIGIGNDVD 229
Cdd:cd01456  166 APP-IKVNVIDFGGDAD 181
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 84-224 1.32e-04

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 43.27  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  84 FVLDSSASmVGTKLRQTKDALFTILHDL-RPQDRFSIIGFSNRIKVwkdhLISVTPDS--IRDGKVYIHHMSPTGGTDIN 160
Cdd:cd01474    9 FVLDKSGS-VAANWIEIYDFVEQLVDRFnSPGLRFSFITFSTRATK----ILPLTDDSsaIIKGLEVLKKVTPSGQTYIH 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312434033 161 GALQRAirllNKYVAHSGIGDR-SVSLIVFLTDgkptvGETHTLKILNNTREAARGQ---VCIFTIGI 224
Cdd:cd01474   84 EGLENA----NEQIFNRNGGGReTVSVIIALTD-----GQLLLNGHKYPEHEAKLSRklgAIVYCVGV 142
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
81-192 1.23e-03

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 41.35  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  81 NVVFVLDSSASM-----VGTKLRQTKDALFTILHD-LRPQDRFSIIGFSNRIKVWkdhlisVTPDSirdGKVYIHHM--- 151
Cdd:COG1721  149 TVVLLLDTSASMrfgsgGPSKLDLAVEAAASLAYLaLRQGDRVGLLTFGDRVRRY------LPPRR---GRRHLLRLlea 219

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 312434033 152 ----SPTGGTDINGALQRAIRLLnkyvahsgigdRSVSLIVFLTD 192
Cdd:COG1721  220 larlEPAGETDLAAALRRLARRL-----------PRRSLVVLISD 253
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 80-227 4.67e-03

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 38.48  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033  80 KNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDR-FSIIGFSNRIKVWkdhlISVTPDSIRDGKVYIHHMSPTGGTD 158
Cdd:cd01462    1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSEFQTK----IVDKTDDLEEPVEFLSGVQLGGGTD 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312434033 159 INGALQRAIRLLNKYvahsgigDRSVSLIVFLTDG-KPTVGEthtlKILNNTREAARGQVCIFTIGIGND 227
Cdd:cd01462   77 INKALRYALELIERR-------DPRKADIVLITDGyEGGVSD----ELLREVELKRSRVARFVALALGDH 135
 
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