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Conserved domains on  [gi|2441046415|ref|WP_272682582|]
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VWA domain-containing protein [Providencia sp. PROV124]

Protein Classification

vWA domain-containing protein( domain architecture ID 10008387)

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

CATH:  3.40.50.410
PubMed:  12579041|10830113|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
11-202 5.29e-63

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


:

Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 195.14  E-value: 5.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  11 TAKPLPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKMETEILVSVITFGNQVELQVPYTKASLVRWQGLQANGMT 90
Cdd:COG4245     2 PMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQPPDLSASGGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  91 PMGTALKMAKAMIEDK----ETTPSRAYRPTVVLVSDGQPNDS-WERPLEDFISEGRSSKCDRMAMAIGRDADETVLKRF 165
Cdd:COG4245    82 PLGAALELLLDLIERRvqkyTAEGKGDWRPVVFLITDGEPTDSdWEAALQRLKDGEAAKKANIFAIGVGPDADTEVLKQL 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2441046415 166 IEGTPhdLFYAENAGQLHEFFQRVTMSVTMRTQSKNP 202
Cdd:COG4245   162 TDPVR--ALDALDGLDFREFFKWLSASVSSVSRSVGP 196
 
Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
11-202 5.29e-63

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 195.14  E-value: 5.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  11 TAKPLPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKMETEILVSVITFGNQVELQVPYTKASLVRWQGLQANGMT 90
Cdd:COG4245     2 PMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQPPDLSASGGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  91 PMGTALKMAKAMIEDK----ETTPSRAYRPTVVLVSDGQPNDS-WERPLEDFISEGRSSKCDRMAMAIGRDADETVLKRF 165
Cdd:COG4245    82 PLGAALELLLDLIERRvqkyTAEGKGDWRPVVFLITDGEPTDSdWEAALQRLKDGEAAKKANIFAIGVGPDADTEVLKQL 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2441046415 166 IEGTPhdLFYAENAGQLHEFFQRVTMSVTMRTQSKNP 202
Cdd:COG4245   162 TDPVR--ALDALDGLDFREFFKWLSASVSSVSRSVGP 196
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 15-170 1.81e-30

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: 110.89  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  15 LPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKMETEILVSVITFGNQVELQVPYTKASLVRWQGLQANGMTPMGT 94
Cdd:cd01464     4 LPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFDSAARVIVPLTPLESFQPPRLTASGGTSMGA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  95 ALKMAKAMIEDKETTPSRA----YRPTVVLVSDGQPNDSWERPLEDfISEGRSSKCDRMAMAIGRDADETVLKRFIEGTP 170
Cdd:cd01464    84 ALELALDCIDRRVQRYRADqkgdWRPWVFLLTDGEPTDDLTAAIER-IKEARDSKGRIVACAVGPKADLDTLKQITEGVP 162
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-178 6.46e-20

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: 83.66  E-value: 6.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   17 VVLLLDVSSSMSGDKIENLNKAVEDMLDTFaqeEKMETEILVSVITFGNQVELQVPYTKA-------SLVRWQGLQANGM 89
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQL---DIGPDGDRVGLVTFSDDARVLFPLNDSrskdallEALASLSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   90 TPMGTALKMAKAMIEDKETTPSRAYRPTVVLVSDGQPNDSWERPLEDFISEgRSSKCDRMAMAIGRDADETVLKRfIEGT 169
Cdd:smart00327  79 TNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKEL-KRSGVKVFVVGVGNDVDEEELKK-LASA 156


                   ....*....
gi 2441046415  170 PHDLFYAEN 178
Cdd:smart00327 157 PGGVYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
17-188 1.21e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 69.23  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKmetEILVSVITFGNQVELQVPYT----KASL---VRWQGLQANGM 89
Cdd:pfam00092   2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD---GTRVGLVQYSSDVRTEFPLNdyssKEELlsaVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  90 TPMGTALKMAKAMIEDKETTPSRAYRPTVVLVSDGQPNDSwerPLEDFISEGRSSKCDRMAMAIGrDADETVLKRfIEGT 169
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG---DPEEVARELKSAGVTVFAVGVG-NADDEELRK-IASE 153

                         170       180
                  ....*....|....*....|.
gi 2441046415 170 PHD--LFYAENAGQLHEFFQR 188
Cdd:pfam00092 154 PGEghVFTVSDFEALEDLQDQ 174
bchD PRK13406
magnesium chelatase subunit D; Provisional
 58-127 3.50e-03

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 38.08  E-value: 3.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2441046415  58 VSVITF-GNQVELQVPYTKaSLVR----WQGLQANGMTPMGTALKMAKAMIEDKEttpSRAYRPTVVLVSDGQPN 127
Cdd:PRK13406  440 VALVAFrGRGAELLLPPTR-SLVRakrsLAGLPGGGGTPLAAGLDAAAALALQVR---RKGMTPTVVLLTDGRAN 510
 
Name Accession Description Interval E-value
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
11-202 5.29e-63

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 195.14  E-value: 5.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  11 TAKPLPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKMETEILVSVITFGNQVELQVPYTKASLVRWQGLQANGMT 90
Cdd:COG4245     2 PMRRLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALETVEVSVITFDGEAKVLLPLTDLEDFQPPDLSASGGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  91 PMGTALKMAKAMIEDK----ETTPSRAYRPTVVLVSDGQPNDS-WERPLEDFISEGRSSKCDRMAMAIGRDADETVLKRF 165
Cdd:COG4245    82 PLGAALELLLDLIERRvqkyTAEGKGDWRPVVFLITDGEPTDSdWEAALQRLKDGEAAKKANIFAIGVGPDADTEVLKQL 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2441046415 166 IEGTPhdLFYAENAGQLHEFFQRVTMSVTMRTQSKNP 202
Cdd:COG4245   162 TDPVR--ALDALDGLDFREFFKWLSASVSSVSRSVGP 196
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 15-170 1.81e-30

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: 110.89  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  15 LPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKMETEILVSVITFGNQVELQVPYTKASLVRWQGLQANGMTPMGT 94
Cdd:cd01464     4 LPIYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYALESVEISVITFDSAARVIVPLTPLESFQPPRLTASGGTSMGA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  95 ALKMAKAMIEDKETTPSRA----YRPTVVLVSDGQPNDSWERPLEDfISEGRSSKCDRMAMAIGRDADETVLKRFIEGTP 170
Cdd:cd01464    84 ALELALDCIDRRVQRYRADqkgdWRPWVFLLTDGEPTDDLTAAIER-IKEARDSKGRIVACAVGPKADLDTLKQITEGVP 162
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 4-219 5.10e-25

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 99.79  E-value: 5.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   4 PKKFTTPTAKPLPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKmeteilVSVITFGNQVELQVPYT----KASLV 79
Cdd:COG2304    81 PPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDR------VSIVTFAGDARVLLPPTpatdRAKIL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  80 RW-QGLQANGMTPMGTALKMAKAMIEdKETTPSRAYRptVVLVSDGQPNDSWERP--LEDFISEGRSSKCDRMAMAIGRD 156
Cdd:COG2304   155 AAiDRLQAGGGTALGAGLELAYELAR-KHFIPGRVNR--VILLTDGDANVGITDPeeLLKLAEEAREEGITLTTLGVGSD 231

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2441046415 157 ADETVLKRFIE---GTPHdlfYAENAGQLHEFFQRvtmsvtMRTQSKNPNVVPAPSEIMLDGGSVK 219
Cdd:COG2304   232 YNEDLLERLADaggGNYY---YIDDPEEAEKVFVR------EFSRIGYENRALATEDFPLPYGTLK 288
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 3-189 2.77e-23

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: 94.62  E-value: 2.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   3 DPKKFTTPTAKPLPVVLLLDVSSSMSG-DKIENLNKAVEDMLDTFAQEEKmeteilVSVITFGNQVELQVPYT--KASLV 79
Cdd:COG1240    81 LAPLALARPQRGRDVVLVVDASGSMAAeNRLEAAKGALLDFLDDYRPRDR------VGLVAFGGEAEVLLPLTrdREALK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  80 RW-QGLQANGMTPMGTALKMAKAMIEDKettpSRAYRPTVVLVSDGQPNDSWERPLEdFISEGRSSKCDRMAMAIGRDA- 157
Cdd:COG1240   155 RAlDELPPGGGTPLGDALALALELLKRA----DPARRKVIVLLTDGRDNAGRIDPLE-AAELAAAAGIRIYTIGVGTEAv 229

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2441046415 158 DETVLKRFIEGTPHDLFYAENAGQLHEFFQRV 189
Cdd:COG1240   230 DEGLLREIAEATGGRYFRADDLSELAAIYREI 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-175 4.53e-21

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 86.08  E-value: 4.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKmetEILVSVITFGNQVELQVPYTK-------ASLVRWQGLQANGM 89
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPP---GDRVGLVTFGSNARVVLPLTTdtdkadlLEAIDALKKGLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  90 TPMGTALKMAKAMIEDketTPSRAYRPTVVLVSDGQPNDSwERPLEDFISEGRSSKCDRMAMAIGRDADETVLKRFIEGT 169
Cdd:cd00198    80 TNIGAALRLALELLKS---AKRPNARRVIILLTDGEPNDG-PELLAEAARELRKLGITVYTIGIGDDANEDELKEIADKT 155


                  ....*.
gi 2441046415 170 PHDLFY 175
Cdd:cd00198   156 TGGAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-178 6.46e-20

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: 83.66  E-value: 6.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   17 VVLLLDVSSSMSGDKIENLNKAVEDMLDTFaqeEKMETEILVSVITFGNQVELQVPYTKA-------SLVRWQGLQANGM 89
Cdd:smart00327   2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQL---DIGPDGDRVGLVTFSDDARVLFPLNDSrskdallEALASLSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   90 TPMGTALKMAKAMIEDKETTPSRAYRPTVVLVSDGQPNDSWERPLEDFISEgRSSKCDRMAMAIGRDADETVLKRfIEGT 169
Cdd:smart00327  79 TNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKEL-KRSGVKVFVVGVGNDVDEEELKK-LASA 156


                   ....*....
gi 2441046415  170 PHDLFYAEN 178
Cdd:smart00327 157 PGGVYVFLP 165
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 4-167 9.39e-15

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 71.25  E-value: 9.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   4 PKKFTTPTAKPLPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKmeteilVSVITFGNQVELQVPYTK----ASLV 79
Cdd:COG2425   108 APASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRR------FGVILFDTEVVEDLPLTAddglEDAI 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  80 RW-QGLQANGMTPMGTALKMAKAMIEDkettpSRAYRPTVVLVSDGQPNDSWerplEDFISEGRSSKCD-RM-AMAIGRD 156
Cdd:COG2425   182 EFlSGLFAGGGTDIAPALRAALELLEE-----PDYRNADIVLITDGEAGVSP----EELLREVRAKESGvRLfTVAIGDA 252

                         170
                  ....*....|.
gi 2441046415 157 ADETVLKRFIE 167
Cdd:COG2425   253 GNPGLLEALAD 263
VWA pfam00092
von Willebrand factor type A domain;
17-188 1.21e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 69.23  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKmetEILVSVITFGNQVELQVPYT----KASL---VRWQGLQANGM 89
Cdd:pfam00092   2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD---GTRVGLVQYSSDVRTEFPLNdyssKEELlsaVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  90 TPMGTALKMAKAMIEDKETTPSRAYRPTVVLVSDGQPNDSwerPLEDFISEGRSSKCDRMAMAIGrDADETVLKRfIEGT 169
Cdd:pfam00092  79 TNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG---DPEEVARELKSAGVTVFAVGVG-NADDEELRK-IASE 153

                         170       180
                  ....*....|....*....|.
gi 2441046415 170 PHD--LFYAENAGQLHEFFQR 188
Cdd:pfam00092 154 PGEghVFTVSDFEALEDLQDQ 174
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 18-186 4.76e-13

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: 64.99  E-value: 4.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  18 VLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKmeteilVSVITFGNQVELQVPYTKAS-----LVRWQGLQANGMTPM 92
Cdd:cd01465     4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDR------LAIVTYDGAAETVLPATPVRdkaaiLAAIDRLTAGGSTAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  93 GTALKMAKAMIeDKETTPSRAYRptVVLVSDGQPN--DSWERPLEDFISEGRSSKCDRMAMAIGRDADETVLKRFIEGTP 170
Cdd:cd01465    78 GAGIQLGYQEA-QKHFVPGGVNR--ILLATDGDFNvgETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADAGN 154

                         170
                  ....*....|....*.
gi 2441046415 171 HDLFYAENAGQLHEFF 186
Cdd:cd01465   155 GNTAYIDNLAEARKVF 170
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 17-164 3.66e-11

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: 59.92  E-value: 3.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGDKIENLNKAVEDMLDtfaqeeKMETEILVSVITFGNQVEL----QVPYTKASL---VRW-QGLQANG 88
Cdd:cd01461     5 VVFVIDTSGSMSGTKIEQTKEALLTALK------DLPPGDYFNIIGFSDTVEEfspsSVSATAENVaaaIEYvNRLQALG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2441046415  89 MTPMGTALKMAkamIEDKETTPSRAyrPTVVLVSDGQPNDswERPLEDFISEGRSSKCDRMAMAIGRDADETVLKR 164
Cdd:cd01461    79 GTNMNDALEAA---LELLNSSPGSV--PQIILLTDGEVTN--ESQILKNVREALSGRIRLFTFGIGSDVNTYLLER 147
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 16-127 2.25e-09

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: 54.97  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  16 PVVLLLDVSSSMSG-DKIENLNKAVEDML-DTFAQEEKmeteilVSVITF-GNQVELQVPYTKaSLV----RWQGLQANG 88
Cdd:cd01451     2 LVIFVVDASGSMAArHRMAAAKGAVLSLLrDAYQRRDK------VALIAFrGTEAEVLLPPTR-SVElakrRLARLPTGG 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2441046415  89 MTPMGTALKMAKAMIEDKETTPSRayRPTVVLVSDGQPN 127
Cdd:cd01451    75 GTPLAAGLLAAYELAAEQARDPGQ--RPLIVVITDGRAN 111
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 17-128 8.18e-09

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 52.78  E-value: 8.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKMeteilvSVITFGNQVELQVPYTKASLVRWQ-------GLQANGM 89
Cdd:cd01466     3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRL------SIVTFSTSAKRLSPLRRMTAKGKRsakrvvdGLQAGGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2441046415  90 TPMGTALKMAKAMIED-KETTPSrayrPTVVLVSDGQPND 128
Cdd:cd01466    77 TNVVGGLKKALKVLGDrRQKNPV----ASIMLLSDGQDNH 112
VWA_2 pfam13519
von Willebrand factor type A domain;
17-121 1.53e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 48.06  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGD-----KIENLNKAVEDMLDTFAqeekmetEILVSVITFGNQVELQVPYTK------ASLVRWQglQ 85
Cdd:pfam13519   1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLP-------GDRVGLVTFGDGPEVLIPLTKdrakilRALRRLE--P 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2441046415  86 ANGMTPMGTALKMAKAMIEDKettpSRAYRPTVVLV 121
Cdd:pfam13519  72 KGGGTNLAAALQLARAALKHR----RKNQPRRIVLI 103
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-175 2.14e-07

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: 49.21  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGDKIENLNKAVEDMLDTFaqeEKMETEILVSVITFGNQVELQVPY----TKASLVR-WQGLQANGMTP 91
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKL---DIGPDKTRVGLVQYSDDVRVEFSLndykSKDDLLKaVKNLKYLGGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  92 --MGTALKMAKAMIedKETTPSRAYRPTV-VLVSDGQPNDswERPLEDFISEGRSSKCDRMAMAIGrDADETVLKRfIEG 168
Cdd:cd01450    80 tnTGKALQYALEQL--FSESNARENVPKViIVLTDGRSDD--GGDPKEAAAKLKDEGIKVFVVGVG-PADEEELRE-IAS 153


                  ....*..
gi 2441046415 169 TPHDLFY 175
Cdd:cd01450   154 CPSERHV 160
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 13-185 1.72e-06

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 47.38  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  13 KPLPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEKMETeilVSVITFGNQVELQVPY----TKASLV----RWQGL 84
Cdd:cd01475     1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATR---VGLVQYSSTVKQEFPLgrfkSKADLKravrRMEYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  85 QANGMTpmGTALK--MAKAMIEDKETTPSRAYRPTVVLV-SDGQPNDSwerpLEDFISEGRSSKCDRMAMAIGRdADETV 161
Cdd:cd01475    78 ETGTMT--GLAIQyaMNNAFSEAEGARPGSERVPRVGIVvTDGRPQDD----VSEVAAKARALGIEMFAVGVGR-ADEEE 150

                         170       180
                  ....*....|....*....|....*.
gi 2441046415 162 LkRFIEGTPHD--LFYAENAGQLHEF 185
Cdd:cd01475   151 L-REIASEPLAdhVFYVEDFSTIEEL 175
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 14-193 1.07e-05

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: 44.69  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  14 PLPVVLLLDVSSSMSGDKIENLNKAVEDMLDTFAQEEkmeteiLVSVITFGNQVELQVPYTKASLVRwqglqangMTPMG 93
Cdd:cd01463    13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDND------FFNIITFSNEVNPVVPCFNDTLVQ--------ATTSN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  94 -TALKMAKAMIEDKETTPSRAYRPTVVLVSdgqpndsweRPLEDFISEGRSSKCDRMAMAIGRDADEtvlkrfiegTPHD 172
Cdd:cd01463    79 kKVLKEALDMLEAKGIANYTKALEFAFSLL---------LKNLQSNHSGSRSQCNQAIMLITDGVPE---------NYKE 140

                         170       180
                  ....*....|....*....|..
gi 2441046415 173 LFYAENAGQLHEFFQRV-TMSV 193
Cdd:cd01463   141 IFDKYNWDKNSEIPVRVfTYLI 162
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 2-135 1.51e-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: 41.65  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415   2 FDPKKFTTPTAKPLPVVLLLDVSSSMS------GDKIENLNKAVEDMLDTFAQEEKMEteilvsVITFGNQVELQVPYTK 75
Cdd:cd01456     8 FALEPVETEPQLPPNVAIVLDNSGSMRevdgggETRLDNAKAALDETANALPDGTRLG------LWTFSGDGDNPLDVRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  76 ASLVRWQGLQANGM---------------------TPMGTALKMAKAMIEDKETTpsrayrpTVVLVSDGqPNDSWERPL 134
Cdd:cd01456    82 LVPKGCLTAPVNGFpsaqrsaldaalnslqtptgwTPLAAALAEAAAYVDPGRVN-------VVVLITDG-EDTCGPDPC 153


                  .
gi 2441046415 135 E 135
Cdd:cd01456   154 E 154
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 19-125 2.71e-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: 40.57  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  19 LLLDVSSSMSGDKIENLNkAVEDMLDTFaqeekMETEILVSVITFGNQVELQVPYTKASLVRWQGLQA------NGMTPM 92
Cdd:cd01474     9 FVLDKSGSVAANWIEIYD-FVEQLVDRF-----NSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVlkkvtpSGQTYI 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2441046415  93 GTALKMAKAMIEdKETTPSRAYRPTVVLVSDGQ 125
Cdd:cd01474    83 HEGLENANEQIF-NRNGGGRETVSVIIALTDGQ 114
VWA_3 pfam13768
von Willebrand factor type A domain;
17-164 3.65e-04

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 39.69  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGdkienLNKAVEDMLDTFAQeeKMETEILVSVITFGNQVELQVPY-----------TKASLVRWQGlq 85
Cdd:pfam13768   3 VVIVVDVSSSMSG-----EPKLQKDALSVALR--QLPTGDKFAVLGFGTLPRPLFPGwrvvsprslqeAFQFIKTLQP-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  86 ANGMTPMGTALKMAKAmiedkeTTPSRAYRPTVVLVSDGQPNDSWERpLEDFISEGRSS-KCDrmAMAIGRDADETVLKR 164
Cdd:pfam13768  74 PLGGSDLLGALKEAVR------APASPGYIRHVLLLTDGSPMQGETR-VSDLISRAPGKiRFF--AYGLGASISAPMLQL 144
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 17-153 8.19e-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: 38.85  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  17 VVLLLDVSSSMSGD-KIENLNKAVEDMLDTFAQEEKMeTEIL-----------VSVITFGnqvELQVPYTKASLVRWQGL 84
Cdd:cd01454     3 VTLLLDLSGSMRSDrRIDVAKKAAVLLAEALEACGVP-HAILgfttdaggrerVRWIKIK---DFDESLHERARKRLAAL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  85 QANGMTPMGTALK-MAKAMIEDKETtpsrayRPTVVLVSDGQPNDSWErpledfiSEGRSSKCDRMAMAI 153
Cdd:cd01454    79 SPGGNTRDGAAIRhAAERLLARPEK------RKILLVISDGEPNDLDY-------YEGNVFATEDALRAV 135
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 14-186 2.03e-03

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 38.14  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  14 PLPVVLLLDVSSSMSG---DKIENLNKAVEDMLDTFAQEEKMETEILVSVITFGNQVELQVPYT---------KASL--V 79
Cdd:cd01480     2 PVDITFVLDSSESVGLqnfDITKNFVKRVAERFLKDYYRKDPAGSWRVGVVQYSDQQEVEAGFLrdirnytslKEAVdnL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2441046415  80 RWqglqANGMTPMGTALKmakAMIEDKETTPSRAYRPTVVLVSDGQPNDSWERPLEDFISEGRSSKCDRMAMAIGRDADE 159
Cdd:cd01480    82 EY----IGGGTFTDCALK---YATEQLLEGSHQKENKFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQNEE 154

                         170       180
                  ....*....|....*....|....*..
gi 2441046415 160 TVLKrfIEGTPHDLFYAENAGQLHEFF 186
Cdd:cd01480   155 PLSR--IACDGKSALYRENFAELLWSF 179
bchD PRK13406
magnesium chelatase subunit D; Provisional
 58-127 3.50e-03

magnesium chelatase subunit D; Provisional


Pssm-ID: 237378 [Multi-domain]  Cd Length: 584  Bit Score: 38.08  E-value: 3.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2441046415  58 VSVITF-GNQVELQVPYTKaSLVR----WQGLQANGMTPMGTALKMAKAMIEDKEttpSRAYRPTVVLVSDGQPN 127
Cdd:PRK13406  440 VALVAFrGRGAELLLPPTR-SLVRakrsLAGLPGGGGTPLAAGLDAAAALALQVR---RKGMTPTVVLLTDGRAN 510
 
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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