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Conserved domains on  [gi|38348336|ref|NP_940912|]
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inter-alpha-trypsin inhibitor heavy chain H6 precursor [Homo sapiens]

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

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List of domain hits

 Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 280-464 5.39e-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: 243.28  E-value: 5.39e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  280 MEKNVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVWKaGGSIQATIQNVHSAKDYLHCMEADGW 359
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFS-PSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  360 TDVNSALLAAASVLNHSNqepgrgpsvGRIPLIIFLTDGEptagVTTPSVILSNVRQALGHRVSLFSLAFGDDADFTLLR 439
Cdd:cd01461   80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146

                        170       180
                 ....*....|....*....|....*
gi 38348336  440 RLSLENRGIARRIYEDTDAALQLKG 464
Cdd:cd01461  147 RLAREGRGIARRIYETDDIESQLLR 171
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 1116-1297 1.78e-55

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: 190.87  E-value: 1.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   1116 KAGLHVSGKLLGAPPRPGHKDQTRTYFQIITVTtDKPRAYTITISRSSISLR-GEGTLRLSWDQPALLKRPQLELYVAAA 1194
Cdd:pfam06668    1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLKdGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   1195 ARLTLRLGPYLEFLVLRHRYRHPSTLQLPHLGFYVANGSGLSPSARGLIGQFQHA-DIRLVTGPMGPCLRRHH------G 1267
Cdd:pfam06668   80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPGSDPEKPDatmkvkG 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 38348336   1268 PDVPVILGKRLLKDSPRLLPRWASCWLVKR 1297
Cdd:pfam06668  160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
39-150 2.11e-50

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 174.08  E-value: 2.11e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336      39 SYSMRSTVVSRYAHTLVTSVLFNPHAEAHEAIFDLDLPHLAFISNFTMTINNKVYIAEVKEKHQAKKIYEEAHQQGKTAA 118
Cdd:smart00609   19 SLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAG 98

                            90       100       110
                    ....*....|....*....|....*....|..
gi 38348336     119 HVGIRDRESEKFRISTSLAAGTEVTFSLAYEE 150
Cdd:smart00609   99 LVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 740-985 7.94e-06

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.46  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   740 KPGSLSHQNPDILPTNSRTQVPPVKPGIPASPKadtvkcvTPLHSK-PGAPSHPqlgaLTSQAPKgLPQSrpgvstLQVP 818
Cdd:PTZ00449  560 KPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPE-------EPKKPKrPRSAQRP----TRPKSPK-LPEL------LDIP 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   819 KYPLH----TRPRVPAPKTRNNMPHLGPGILLSKTPKILLSLKPSAPPH-------QISTSISLSKpETPNPHMPQTPLP 887
Cdd:PTZ00449  622 KSPKRpespKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKfkekfydDYLDAAAKSK-ETKTTVVLDESFE 700

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   888 PRPDRPRPPLPESLSTFPNTISSSTGPSSTTTTSVLGEP-LPMP-----FTPTLPPGRFWHQ---YDLLPG--------P 950
Cdd:PTZ00449  701 SILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdAEQPddiefFTPPEEERTFFHEtpaDTPLPDilaeefkeE 780

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 38348336   951 QRTRQVLGP----SRPGVPTmsllnSSRPTPEGSPPNLP 985
Cdd:PTZ00449  781 DIHAETGEPdeamKRPDSPS-----EHEDKPPGDHPSLP 814
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 280-464 5.39e-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: 243.28  E-value: 5.39e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  280 MEKNVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVWKaGGSIQATIQNVHSAKDYLHCMEADGW 359
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFS-PSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  360 TDVNSALLAAASVLNHSNqepgrgpsvGRIPLIIFLTDGEptagVTTPSVILSNVRQALGHRVSLFSLAFGDDADFTLLR 439
Cdd:cd01461   80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146

                        170       180
                 ....*....|....*....|....*
gi 38348336  440 RLSLENRGIARRIYEDTDAALQLKG 464
Cdd:cd01461  147 RLAREGRGIARRIYETDDIESQLLR 171
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 1116-1297 1.78e-55

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: 190.87  E-value: 1.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   1116 KAGLHVSGKLLGAPPRPGHKDQTRTYFQIITVTtDKPRAYTITISRSSISLR-GEGTLRLSWDQPALLKRPQLELYVAAA 1194
Cdd:pfam06668    1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLKdGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   1195 ARLTLRLGPYLEFLVLRHRYRHPSTLQLPHLGFYVANGSGLSPSARGLIGQFQHA-DIRLVTGPMGPCLRRHH------G 1267
Cdd:pfam06668   80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPGSDPEKPDatmkvkG 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 38348336   1268 PDVPVILGKRLLKDSPRLLPRWASCWLVKR 1297
Cdd:pfam06668  160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
39-150 2.11e-50

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 174.08  E-value: 2.11e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336      39 SYSMRSTVVSRYAHTLVTSVLFNPHAEAHEAIFDLDLPHLAFISNFTMTINNKVYIAEVKEKHQAKKIYEEAHQQGKTAA 118
Cdd:smart00609   19 SLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAG 98

                            90       100       110
                    ....*....|....*....|....*....|..
gi 38348336     119 HVGIRDRESEKFRISTSLAAGTEVTFSLAYEE 150
Cdd:smart00609   99 LVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-478 6.03e-36

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 138.31  E-value: 6.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  277 LPPMekNVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVWKAGgsiqATIQNVHSAKDYLHCMEA 356
Cdd:COG2304   89 RPPL--NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPP----TPATDRAKILAAIDRLQA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  357 DGWTDVNSALLAAAsvlnhsnQEPGRGPSVGRIPLIIFLTDGEPTAGVTTPSVILSNVRQALGHRVSLFSLAFGDDADFT 436
Cdd:COG2304  163 GGGTALGAGLELAY-------ELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNED 235

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 38348336  437 LLRRLSLENRGIARRIYEDTDAALQLKGLYEEISMPLLADVR 478
Cdd:COG2304  236 LLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALAT 277
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 37-148 2.93e-35

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 129.91  E-value: 2.93e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336     37 MTSYSMRSTVVSRYAHTLVTSVLFNPHAEAHEAIFDLDLPHLAFISNFTMTINNKVYIAEVKEKHQAKKIYEEAHQQGKT 116
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 38348336    117 AAHVgiRDRESEKFRIS-TSLAAGTEVTFSLAY 148
Cdd:pfam08487   81 AGLL--EQDTPDVFTTSvGNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 283-463 1.87e-24

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 101.38  E-value: 1.87e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336     283 NVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQA---NDYFNIISFSDTVNVW---KAGGSIQATIQNVHSAKDYLHcmea 356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDARVLfplNDSRSKDALLEALASLSYKLG---- 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336     357 dGWTDVNSALLAAASVLNHSNQepgrGPSVGRIPLIIFLTDGEPTAGvttPSVILSNVRQALGHRVSLFSLAFGDDADFT 436
Cdd:smart00327   77 -GGTNLGAALQYALENLFSKSA----GSRRGAPKVVILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148

                           170       180
                    ....*....|....*....|....*..
gi 38348336     437 LLRRLSLENRGiaRRIYEDTDAALQLK 463
Cdd:smart00327  149 ELKKLASAPGG--VYVFLPELLDLLID 173
VWA pfam00092
von Willebrand factor type A domain;
283-468 1.13e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 87.72  E-value: 1.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    283 NVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQA---NDYFNIISFSDTVNV---WKAGGSIQATIQNVHSAKDYLHcmea 356
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIgpdGTRVGLVQYSSDVRTefpLNDYSSKEELLSAVDNLRYLGG---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    357 dGWTDVNSALLAAASVLNHSNqepgRGPSVGRIPLIIFLTDGEPTAGvttpsVILSNVRQALGHRVSLFSLAFGdDADFT 436
Cdd:pfam00092   77 -GTTNTGKALKYALENLFSSA----AGARPGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDE 145

                          170       180       190
                   ....*....|....*....|....*....|..
gi 38348336    437 LLRRLSLENRgiARRIYEDTDAAlQLKGLYEE 468
Cdd:pfam00092  146 ELRKIASEPG--EGHVFTVSDFE-ALEDLQDQ 174
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 740-985 7.94e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.46  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   740 KPGSLSHQNPDILPTNSRTQVPPVKPGIPASPKadtvkcvTPLHSK-PGAPSHPqlgaLTSQAPKgLPQSrpgvstLQVP 818
Cdd:PTZ00449  560 KPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPE-------EPKKPKrPRSAQRP----TRPKSPK-LPEL------LDIP 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   819 KYPLH----TRPRVPAPKTRNNMPHLGPGILLSKTPKILLSLKPSAPPH-------QISTSISLSKpETPNPHMPQTPLP 887
Cdd:PTZ00449  622 KSPKRpespKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKfkekfydDYLDAAAKSK-ETKTTVVLDESFE 700

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   888 PRPDRPRPPLPESLSTFPNTISSSTGPSSTTTTSVLGEP-LPMP-----FTPTLPPGRFWHQ---YDLLPG--------P 950
Cdd:PTZ00449  701 SILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdAEQPddiefFTPPEEERTFFHEtpaDTPLPDilaeefkeE 780

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 38348336   951 QRTRQVLGP----SRPGVPTmsllnSSRPTPEGSPPNLP 985
Cdd:PTZ00449  781 DIHAETGEPdeamKRPDSPS-----EHEDKPPGDHPSLP 814
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 603-879 3.33e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    603 TPLTSLVMVQPKQASEETRRQTSTSAGPDTIMPSSSSRHGLGVSTAQPALVPKVISPKSRPVKPKFYLSSTTTASTKKM- 681
Cdd:pfam03154  200 TPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMp 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    682 -----------------------LSSKELEPLGESP----HTLSMPTYPKAKIPAQQDSGTLAQP---TLRTKPTILVPS 731
Cdd:pfam03154  280 hslqtgpshmqhpvppqpfpltpQSSQSQVPPGPSPaapgQSQQRIHTPPSQSQLQSQQPPREQPlppAPLSMPHIKPPP 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    732 NsgTLLPLKPGSLSHQNPDILPTNSRTQVPPVKPGIPASPKADTVkcvtPLHSKPGApsHPQLGALTSQA---------P 802
Cdd:pfam03154  360 T--TPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSL----STHHPPSA--HPPPLQLMPQSqqlppppaqP 431

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38348336    803 KGLPQSR--PGVSTLQVPKYPLHTRPRVPAPKTRNNMPHLGPGILlsktpkillslKPSAPPHQISTSISLSKPETPNP 879
Cdd:pfam03154  432 PVLTQSQslPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPIT-----------PPSGPPTSTSSAMPGIQPPSSAS 499
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 280-464 5.39e-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: 243.28  E-value: 5.39e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  280 MEKNVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVWKaGGSIQATIQNVHSAKDYLHCMEADGW 359
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFS-PSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  360 TDVNSALLAAASVLNHSNqepgrgpsvGRIPLIIFLTDGEptagVTTPSVILSNVRQALGHRVSLFSLAFGDDADFTLLR 439
Cdd:cd01461   80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146

                        170       180
                 ....*....|....*....|....*
gi 38348336  440 RLSLENRGIARRIYEDTDAALQLKG 464
Cdd:cd01461  147 RLAREGRGIARRIYETDDIESQLLR 171
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 1116-1297 1.78e-55

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: 190.87  E-value: 1.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   1116 KAGLHVSGKLLGAPPRPGHKDQTRTYFQIITVTtDKPRAYTITISRSSISLR-GEGTLRLSWDQPALLKRPQLELYVAAA 1194
Cdd:pfam06668    1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIV-VKPLGVKIEVTPEKITLKdGGDRLVLSWSDTASVKQDGLTVSVVKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   1195 ARLTLRLGPYLEFLVLRHRYRHPSTLQLPHLGFYVANGSGLSPSARGLIGQFQHA-DIRLVTGPMGPCLRRHH------G 1267
Cdd:pfam06668   80 SNVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEpEVEVTDVRPGSDPEKPDatmkvkG 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 38348336   1268 PDVPVILGKRLLKDSPRLLPRWASCWLVKR 1297
Cdd:pfam06668  160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
39-150 2.11e-50

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 174.08  E-value: 2.11e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336      39 SYSMRSTVVSRYAHTLVTSVLFNPHAEAHEAIFDLDLPHLAFISNFTMTINNKVYIAEVKEKHQAKKIYEEAHQQGKTAA 118
Cdd:smart00609   19 SLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAG 98

                            90       100       110
                    ....*....|....*....|....*....|..
gi 38348336     119 HVGIRDRESEKFRISTSLAAGTEVTFSLAYEE 150
Cdd:smart00609   99 LVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 277-478 6.03e-36

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 138.31  E-value: 6.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  277 LPPMekNVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVWKAGgsiqATIQNVHSAKDYLHCMEA 356
Cdd:COG2304   89 RPPL--NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPP----TPATDRAKILAAIDRLQA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  357 DGWTDVNSALLAAAsvlnhsnQEPGRGPSVGRIPLIIFLTDGEPTAGVTTPSVILSNVRQALGHRVSLFSLAFGDDADFT 436
Cdd:COG2304  163 GGGTALGAGLELAY-------ELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNED 235

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 38348336  437 LLRRLSLENRGIARRIYEDTDAALQLKGLYEEISMPLLADVR 478
Cdd:COG2304  236 LLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALAT 277
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 37-148 2.93e-35

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 129.91  E-value: 2.93e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336     37 MTSYSMRSTVVSRYAHTLVTSVLFNPHAEAHEAIFDLDLPHLAFISNFTMTINNKVYIAEVKEKHQAKKIYEEAHQQGKT 116
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 38348336    117 AAHVgiRDRESEKFRIS-TSLAAGTEVTFSLAY 148
Cdd:pfam08487   81 AGLL--EQDTPDVFTTSvGNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 283-463 1.87e-24

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 101.38  E-value: 1.87e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336     283 NVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQA---NDYFNIISFSDTVNVW---KAGGSIQATIQNVHSAKDYLHcmea 356
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDARVLfplNDSRSKDALLEALASLSYKLG---- 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336     357 dGWTDVNSALLAAASVLNHSNQepgrGPSVGRIPLIIFLTDGEPTAGvttPSVILSNVRQALGHRVSLFSLAFGDDADFT 436
Cdd:smart00327   77 -GGTNLGAALQYALENLFSKSA----GSRRGAPKVVILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148

                           170       180
                    ....*....|....*....|....*..
gi 38348336     437 LLRRLSLENRGiaRRIYEDTDAALQLK 463
Cdd:smart00327  149 ELKKLASAPGG--VYVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 283-442 1.09e-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: 98.79  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  283 NVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQA---NDYFNIISFSDTVNVWKAGGSIQATiQNVHSAKDYLHcMEADGW 359
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSAsppGDRVGLVTFGSNARVVLPLTTDTDK-ADLLEAIDALK-KGLGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  360 TDVNSALLAAASVLNhsnqepgRGPSVGRIPLIIFLTDGEPTAGVTTPSVILSNVRQAlghRVSLFSLAFGDDADFTLLR 439
Cdd:cd00198   80 TNIGAALRLALELLK-------SAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELK 149


                 ...
gi 38348336  440 RLS 442
Cdd:cd00198  150 EIA 152
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 278-469 1.62e-22

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 98.47  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  278 PPMEKNVVFVIDVSSSMFG-TKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVwkaggsIQATIQNVHSAKDYLHCMEA 356
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEV------LLPLTRDREALKRALDELPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  357 DGWTDVNSALLAAASVLNHSNQEpgrgpsvgRIPLIIFLTDGEPTAGVTTPSVIlsnVRQALGHRVSLFSLAFGDDA-DF 435
Cdd:COG1240  163 GGGTPLGDALALALELLKRADPA--------RRKVIVLLTDGRDNAGRIDPLEA---AELAAAAGIRIYTIGVGTEAvDE 231

                        170       180       190
                 ....*....|....*....|....*....|....
gi 38348336  436 TLLRRLSLENRGIARRIyedtDAALQLKGLYEEI 469
Cdd:COG1240  232 GLLREIAEATGGRYFRA----DDLSELAAIYREI 261
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 273-442 4.69e-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: 97.44  E-value: 4.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  273 APRGLPPMEKNVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVnVWKAGgsiQATIQNVHSAKDYLH 352
Cdd:COG2425  110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEV-VEDLP---LTADDGLEDAIEFLS 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  353 CMEADGWTDVNSALLAAASVLnhsnQEPGRGPSVgriplIIFLTDGEPTAGvttPSVILSNVRQALgHRVSLFSLAFGDD 432
Cdd:COG2425  186 GLFAGGGTDIAPALRAALELL----EEPDYRNAD-----IVLITDGEAGVS---PEELLREVRAKE-SGVRLFTVAIGDA 252

                        170
                 ....*....|
gi 38348336  433 ADFTLLRRLS 442
Cdd:COG2425  253 GNPGLLEALA 262
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
273-471 3.08e-21

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 93.07  E-value: 3.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  273 APRGLPpmeknVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDY------FNIISFSDTVNVwkaggsiqatIQNVHS 346
Cdd:COG4245    2 PMRRLP-----VYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletveVSVITFDGEAKV----------LLPLTD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  347 AKD-YLHCMEADGWTDVNSALLAAASVLNHSNQEPGRGPSVGRIPLIIFLTDGEPTAgvttpsvilSNVRQAL------- 418
Cdd:COG4245   67 LEDfQPPDLSASGGTPLGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTD---------SDWEAALqrlkdge 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 38348336  419 -GHRVSLFSLAFGDDADFTLLRRLSLENRGIarriyeDTDAALQLKGLYEEISM 471
Cdd:COG4245  138 aAKKANIFAIGVGPDADTEVLKQLTDPVRAL------DALDGLDFREFFKWLSA 185
VWA pfam00092
von Willebrand factor type A domain;
283-468 1.13e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 87.72  E-value: 1.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    283 NVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQA---NDYFNIISFSDTVNV---WKAGGSIQATIQNVHSAKDYLHcmea 356
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIgpdGTRVGLVQYSSDVRTefpLNDYSSKEELLSAVDNLRYLGG---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    357 dGWTDVNSALLAAASVLNHSNqepgRGPSVGRIPLIIFLTDGEPTAGvttpsVILSNVRQALGHRVSLFSLAFGdDADFT 436
Cdd:pfam00092   77 -GTTNTGKALKYALENLFSSA----AGARPGAPKVVVLLTDGRSQDG-----DPEEVARELKSAGVTVFAVGVG-NADDE 145

                          170       180       190
                   ....*....|....*....|....*....|..
gi 38348336    437 LLRRLSLENRgiARRIYEDTDAAlQLKGLYEE 468
Cdd:pfam00092  146 ELRKIASEPG--EGHVFTVSDFE-ALEDLQDQ 174
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 283-441 4.78e-16

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 77.31  E-value: 4.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  283 NVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVwkaggSIQATIQNVHSA-KDYLHCMEADGWTD 361
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET-----VLPATPVRDKAAiLAAIDRLTAGGSTA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  362 VNSALLAAASVLNHsnqepGRGPsvGRIPLIIFLTDGEPTAGVTTPSVILSNVRQALGHRVSLFSLAFGDDADFTLLRRL 441
Cdd:cd01465   77 GGAGIQLGYQEAQK-----HFVP--GGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 282-447 2.15e-14

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: 73.20  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  282 KNVVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSDTVNVWKA---GGSIQATIQNVHSAKDYLHCMEADG 358
Cdd:cd01463   14 KDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPcfnDTLVQATTSNKKVLKEALDMLEAKG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  359 WTDVNSALLAAASVLNHSNQEPGRGPSVGRIPLIIFLTDGEPTAgvTTPSVILSNVRQALGHRVSLFSLAFGDDA-DFTL 437
Cdd:cd01463   94 IANYTKALEFAFSLLLKNLQSNHSGSRSQCNQAIMLITDGVPEN--YKEIFDKYNWDKNSEIPVRVFTYLIGREVtDRRE 171

                        170
                 ....*....|
gi 38348336  438 LRRLSLENRG 447
Cdd:cd01463  172 IQWMACENKG 181
VWA_3 pfam13768
von Willebrand factor type A domain;
282-450 2.00e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 69.35  E-value: 2.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    282 KNVVFVIDVSSSMFGTKMEQtKTAMNVILSDLQANDYFNIISFSDTVNVWKAGGsiqatiQNVHS-----AKDYLHCMEA 356
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGW------RVVSPrslqeAFQFIKTLQP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    357 D-GWTDVNSALLAAASVLnhsnqepgrgPSVGRIPLIIFLTDGEPTAGVTTpsvILSNVRQALGHrVSLFSLAFGDDADF 435
Cdd:pfam13768   74 PlGGSDLLGALKEAVRAP----------ASPGYIRHVLLLTDGSPMQGETR---VSDLISRAPGK-IRFFAYGLGASISA 139

                          170
                   ....*....|....*
gi 38348336    436 TLLRRLSLENRGIAR 450
Cdd:pfam13768  140 PMLQLLAEASNGTYE 154
VWA_2 pfam13519
von Willebrand factor type A domain;
284-375 3.39e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 55.38  E-value: 3.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    284 VVFVIDVSSSM-----FGTKMEQTKTAMNVILSDLqANDYFNIISFSDTVNVWKAGGSIQATIQN-VHSAKDYlhcmeaD 357
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPEVLIPLTKDRAKILRaLRRLEPK------G 73

                           90
                   ....*....|....*...
gi 38348336    358 GWTDVNSALLAAASVLNH 375
Cdd:pfam13519   74 GGTNLAAALQLARAALKH 91
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 284-400 1.33e-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: 55.47  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  284 VVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDYFNIISFSdtvNVWKAGGSI-QATIQNVHSAKDYLHCMEADGWTDV 362
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFS---TSAKRLSPLrRMTAKGKRSAKRVVDGLQAGGGTNV 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 38348336  363 NSALLAAASVLNHSNQEpgrgpsvGRIPLIIFLTDGEP 400
Cdd:cd01466   80 VGGLKKALKVLGDRRQK-------NPVASIMLLSDGQD 110
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 284-442 2.01e-07

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: 52.34  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  284 VVFVIDVSSSMFGTKMEQTKTAMNVILSDLQANDY------FNIISFsdtvnvwkaGGSIQATIQNVHSAKDYLHCMEAD 357
Cdd:cd01464    6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYalesveISVITF---------DSAARVIVPLTPLESFQPPRLTAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  358 GWTDVNSALLAAASVLNHSNQEPgRGPSVG--RiPLIIFLTDGEPTagvTTPSVILSNVRQALGHRVSLFSLAFGDDADF 435
Cdd:cd01464   77 GGTSMGAALELALDCIDRRVQRY-RADQKGdwR-PWVFLLTDGEPT---DDLTAAIERIKEARDSKGRIVACAVGPKADL 151


                 ....*..
gi 38348336  436 TLLRRLS 442
Cdd:cd01464  152 DTLKQIT 158
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 283-434 4.73e-07

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: 52.05  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  283 NVVFVIDVSSSM------FGTKMEQTKTAMNVILSDLQANDYFNIISFS---DTVNVWKAGGSIQATIQNVHSAKDYLHC 353
Cdd:cd01456   22 NVAIVLDNSGSMrevdggGETRLDNAKAALDETANALPDGTRLGLWTFSgdgDNPLDVRVLVPKGCLTAPVNGFPSAQRS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  354 M---------EADGWTDVNSALLAAASVLNhsnqepgrgpsVGRIPLIIFLTDGEPTAGVTTPSVI-LSNVRQALGHRVS 423
Cdd:cd01456  102 AldaalnslqTPTGWTPLAAALAEAAAYVD-----------PGRVNVVVLITDGEDTCGPDPCEVArELAKRRTPAPPIK 170

                        170
                 ....*....|.
gi 38348336  424 LFSLAFGDDAD 434
Cdd:cd01456  171 VNVIDFGGDAD 181
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 284-403 2.03e-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: 49.58  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  284 VVFVIDVSSSM-FGTKMEQTKTAMNVILSD-LQANDYFNIISFSDTvnvwkaggsiQATI-----QNVHSAKDYLHCMEA 356
Cdd:cd01451    3 VIFVVDASGSMaARHRMAAAKGAVLSLLRDaYQRRDKVALIAFRGT----------EAEVllpptRSVELAKRRLARLPT 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 38348336  357 DGWTDVNSALLAAASVLNHSNQEPGRgpsvgrIPLIIFLTDGEPTAG 403
Cdd:cd01451   73 GGGTPLAAGLLAAYELAAEQARDPGQ------RPLIVVITDGRANVG 113
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 740-985 7.94e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.46  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   740 KPGSLSHQNPDILPTNSRTQVPPVKPGIPASPKadtvkcvTPLHSK-PGAPSHPqlgaLTSQAPKgLPQSrpgvstLQVP 818
Cdd:PTZ00449  560 KPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPE-------EPKKPKrPRSAQRP----TRPKSPK-LPEL------LDIP 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   819 KYPLH----TRPRVPAPKTRNNMPHLGPGILLSKTPKILLSLKPSAPPH-------QISTSISLSKpETPNPHMPQTPLP 887
Cdd:PTZ00449  622 KSPKRpespKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKfkekfydDYLDAAAKSK-ETKTTVVLDESFE 700

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   888 PRPDRPRPPLPESLSTFPNTISSSTGPSSTTTTSVLGEP-LPMP-----FTPTLPPGRFWHQ---YDLLPG--------P 950
Cdd:PTZ00449  701 SILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdAEQPddiefFTPPEEERTFFHEtpaDTPLPDilaeefkeE 780

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 38348336   951 QRTRQVLGP----SRPGVPTmsllnSSRPTPEGSPPNLP 985
Cdd:PTZ00449  781 DIHAETGEPdeamKRPDSPS-----EHEDKPPGDHPSLP 814
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 283-433 8.48e-06

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 47.71  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  283 NVVFVIDVSSSMFGTKMEQTK--TAMNVILSDL---QANDYFNIISFSDtvnvwkaGGSIQATIQNVH-SAKDYLH---C 353
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVKPSrlEAAKEVLSDFidrRENDRIGLVVFAG-------AAFTQAPLTLDReSLKELLEdikI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  354 MEADGWTDVNSALLAAASVLNHSNQepgrgpsVGRIplIIFLTDGEPTAGVTTPsVILSNVRQALGHRVslFSLAFGDDA 433
Cdd:cd01467   77 GLAGQGTAIGDAIGLAIKRLKNSEA-------KERV--IVLLTDGENNAGEIDP-ATAAELAKNKGVRI--YTIGVGKSG 144
PHA03378 PHA03378
EBNA-3B; Provisional
 682-882 1.85e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 49.30  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   682 LSSKELEPLGESPHTLSMPTYPKAKIPAQQDSgTLAQPTLRTKPTILV---PSNSGTLLPLKPGSLSHQNPDILPTNSRt 758
Cdd:PHA03378  628 LRPIPMRPLRMQPITFNVLVFPTPHQPPQVEI-TPYKPTWTQIGHIPYqpsPTGANTMLPIQWAPGTMQPPPRAPTPMR- 705

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   759 qvPPVKPGIPASPKADTVKCVTPLHSKPGAPSHPQLGALTSQAPKGLPQSRPGVSTLQVPKYPLHTRPRVPAPKTRnnmP 838
Cdd:PHA03378  706 --PPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPP---P 780

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 38348336   839 HLGPGILlsKTPKIllSLKPSAPPHQISTSISLSKPETPNPHMP 882
Cdd:PHA03378  781 QAPPAPQ--QRPRG--APTPQPPPQAGPTSMQLMPRAAPGQQGP 820
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 283-442 5.00e-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: 44.98  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  283 NVVFVIDVSSSMFGTKMEQTKTAMNVILSDL---QANDYFNIISFSDTVNVW------KAGGSIQATIQNVHSakdylhc 353
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDDVRVEfslndyKSKDDLLKAVKNLKY------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  354 MEADGwTDVNSALLAAASVLNHSNQEPGRGPSVgriplIIFLTDGEPTAGvTTPSVILSNVRQalgHRVSLFSLAFGdDA 433
Cdd:cd01450   75 LGGGG-TNTGKALQYALEQLFSESNARENVPKV-----IIVLTDGRSDDG-GDPKEAAAKLKD---EGIKVFVVGVG-PA 143


                 ....*....
gi 38348336  434 DFTLLRRLS 442
Cdd:cd01450  144 DEEELREIA 152
PHA03247 PHA03247
large tegument protein UL36; Provisional
 613-984 7.36e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   613 PKQASEETRRQT-STSAGPDTIMP----SSSSRHGLGVSTAQPALVPKVISPKSRPVKPKFYLSSTTTASTKKMLSSKEL 687
Cdd:PHA03247 2601 PVDDRGDPRGPApPSPLPPDTHAPdpppPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP 2680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   688 E---------------------PLGESPHTLSMPTYPKAKIPAQQDSGTLAQPTLRTKPtILVPSNSGTLLPLKPgslsh 746
Cdd:PHA03247 2681 QrprrraarptvgsltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP-APPAVPAGPATPGGP----- 2754

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   747 qNPDILPTNSRTQVPPVKPGIPAS--PKADTVKCVTPLH-SKPGAPSHPQLGALTSQAP---KGLPQSRPGVSTLQVPKY 820
Cdd:PHA03247 2755 -ARPARPPTTAGPPAPAPPAAPAAgpPRRLTRPAVASLSeSRESLPSPWDPADPPAAVLapaAALPPAASPAGPLPPPTS 2833

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   821 PLHTRPRVPAPKTRNNMPHLGP----GILLSKTPKILLSLKPSAPPH------------QISTSISLSKPETPNPHMPQT 884
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLGGSvapgGDVRRRPPSRSPAAKPAAPARppvrrlarpavsRSTESFALPPDQPERPPQPQA 2913

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336   885 PLPPRPDRPRPPLPESLSTFPNTISSSTGPSSTTTTSVLGEP---LPMPFTPTLPPGRFwhqydllpgpQRTRQVLGPSR 961
Cdd:PHA03247 2914 PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgaVPQPWLGALVPGRV----------AVPRFRVPQPA 2983

                         410       420
                  ....*....|....*....|...
gi 38348336   962 PgvptmsllnsSRPTPEGSPPNL 984
Cdd:PHA03247 2984 P----------SREAPASSTPPL 2996
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 284-433 8.80e-04

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: 41.54  E-value: 8.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  284 VVFVIDVSSSMFGT-KMEQTKTAMNVILSDLQA-NDYFNIISFSDtvnvwKAGGSIQATIQNVHSAKDYLH--------C 353
Cdd:cd01454    3 VTLLLDLSGSMRSDrRIDVAKKAAVLLAEALEAcGVPHAILGFTT-----DAGGRERVRWIKIKDFDESLHerarkrlaA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  354 MEADGWTDVNSALLAAASVLNHSNQEPgrgpsvgRIPLIIflTDGEPTAGVTTP------SVILSNVRQALGHRVSLFSL 427
Cdd:cd01454   78 LSPGGNTRDGAAIRHAAERLLARPEKR-------KILLVI--SDGEPNDLDYYEgnvfatEDALRAVIEARKLGIEVFGI 148


                 ....*.
gi 38348336  428 AFGDDA 433
Cdd:cd01454  149 TIDRDA 154
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 603-879 3.33e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    603 TPLTSLVMVQPKQASEETRRQTSTSAGPDTIMPSSSSRHGLGVSTAQPALVPKVISPKSRPVKPKFYLSSTTTASTKKM- 681
Cdd:pfam03154  200 TPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMp 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    682 -----------------------LSSKELEPLGESP----HTLSMPTYPKAKIPAQQDSGTLAQP---TLRTKPTILVPS 731
Cdd:pfam03154  280 hslqtgpshmqhpvppqpfpltpQSSQSQVPPGPSPaapgQSQQRIHTPPSQSQLQSQQPPREQPlppAPLSMPHIKPPP 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336    732 NsgTLLPLKPGSLSHQNPDILPTNSRTQVPPVKPGIPASPKADTVkcvtPLHSKPGApsHPQLGALTSQA---------P 802
Cdd:pfam03154  360 T--TPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSL----STHHPPSA--HPPPLQLMPQSqqlppppaqP 431

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38348336    803 KGLPQSR--PGVSTLQVPKYPLHTRPRVPAPKTRNNMPHLGPGILlsktpkillslKPSAPPHQISTSISLSKPETPNP 879
Cdd:pfam03154  432 PVLTQSQslPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPIT-----------PPSGPPTSTSSAMPGIQPPSSAS 499
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 282-440 5.59e-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: 38.87  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  282 KNVVFVIDVSSSMFGTKMEQTKTAM-NVILSDLQANDYFNIISFSDTVNVwkaggSIQATIQNVHSAKDYLHCMEADGWT 360
Cdd:cd01462    1 GPVILLVDQSGSMYGAPEEVAKAVAlALLRIALAENRDTYLILFDSEFQT-----KIVDKTDDLEEPVEFLSGVQLGGGT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38348336  361 DVNSALLAAASVLnhSNQEPGRGpsvgripLIIFLTDGEpTAGVT---TPSVILSNVRQALghrvsLFSLAFGDDADFTL 437
Cdd:cd01462   76 DINKALRYALELI--ERRDPRKA-------DIVLITDGY-EGGVSdelLREVELKRSRVAR-----FVALALGDHGNPGY 140


                 ...
gi 38348336  438 LRR 440
Cdd:cd01462  141 DRI 143
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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