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Conserved domains on  [gi|820894824|ref|WP_046800957|]
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MULTISPECIES: nitric oxide reductase activation protein NorD [Rhizobium/Agrobacterium group]

Protein Classification

nitric oxide reductase activation protein NorD( domain architecture ID 11468261)

nitric oxide reductase activation protein similar to Brucella suis protein NorD, which is an essential virulence factor, probably involved in the detoxification of nitric oxide (NO) produced in the macrophages during the innate response against infection

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
210-632 2.24e-139

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


:

Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 413.34  E-value: 2.24e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 210 APPRYLPMLPVPLWPDT----LLRETSEARQSEDQPAAGAAPQGAEAARHIAVREKAENRQTERSPFILNRFEKILAMAE 285
Cdd:COG4548   10 LLLLLLLAARALLAAALaalaAAAEALAAAALLLELLLALLAALRLALLREAAARALALLLGALRLAALLSAGLLELALD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 286 MVNVDRPGDDSDDADGSAADELDDMTLGERKGRPSARFRFDLDLPPEALKHTPLTAELTYPEWDYRSGTYLADHCRVIAG 365
Cdd:COG4548   90 ALPLGRAEPEADAADALDALRDERALDAAADELGDEAPEALGEEPEAPDAAASELSAAGYPEWDYRKQRYRPDWCTVLER 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 366 PAKDAETAPEPD--PDTKSLIRRVRRQFEVLRPRHEMLRAQLDGNDLDLDAVVRARSDIAAGGQGSDRIHMASRPQAHDL 443
Cdd:COG4548  170 RPPEGDPAFLDAtlARHRRLIRRLRRQFEALRPQRVRLRRQEDGDELDLDAAIRALADRRAGGEPDPRIYMRRRRKERDL 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 444 AVTILVDVSLSTDAWFDN-RRVLDVEKEALLVLAHGLSACGDSHSILTFTSRRRSWVRVETVKDFDEPMGHTVERRIAAL 522
Cdd:COG4548  250 AVLLLLDLSLSTDAWVGSgRRVLDVEREALLLLAEALEALGDPFAIYGFSSDGRHRVRYYRIKDFDEPYDDAVRARIAGL 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 523 KPGFYTRIGPAIRHASAKLHERPERRKLLLLLTDGKPNDVDHYEGRFAIEDSRRAVSEARRSGVSVFGVTVDSKAQSYIP 602
Cdd:COG4548  330 EPGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPNDIDVYEGRYGIEDTRQAVREARRAGIHPFCITIDPEADDYLP 409

                        410       420       430
                 ....*....|....*....|....*....|
gi 820894824 603 AMFGQNGYAIVSRIAKLPAALPAIYRSLAG 632
Cdd:COG4548  410 RIFGRGGYTVIDDVERLPERLPQLYRRLTR 439
 
Name Accession Description Interval E-value
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
210-632 2.24e-139

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 413.34  E-value: 2.24e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 210 APPRYLPMLPVPLWPDT----LLRETSEARQSEDQPAAGAAPQGAEAARHIAVREKAENRQTERSPFILNRFEKILAMAE 285
Cdd:COG4548   10 LLLLLLLAARALLAAALaalaAAAEALAAAALLLELLLALLAALRLALLREAAARALALLLGALRLAALLSAGLLELALD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 286 MVNVDRPGDDSDDADGSAADELDDMTLGERKGRPSARFRFDLDLPPEALKHTPLTAELTYPEWDYRSGTYLADHCRVIAG 365
Cdd:COG4548   90 ALPLGRAEPEADAADALDALRDERALDAAADELGDEAPEALGEEPEAPDAAASELSAAGYPEWDYRKQRYRPDWCTVLER 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 366 PAKDAETAPEPD--PDTKSLIRRVRRQFEVLRPRHEMLRAQLDGNDLDLDAVVRARSDIAAGGQGSDRIHMASRPQAHDL 443
Cdd:COG4548  170 RPPEGDPAFLDAtlARHRRLIRRLRRQFEALRPQRVRLRRQEDGDELDLDAAIRALADRRAGGEPDPRIYMRRRRKERDL 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 444 AVTILVDVSLSTDAWFDN-RRVLDVEKEALLVLAHGLSACGDSHSILTFTSRRRSWVRVETVKDFDEPMGHTVERRIAAL 522
Cdd:COG4548  250 AVLLLLDLSLSTDAWVGSgRRVLDVEREALLLLAEALEALGDPFAIYGFSSDGRHRVRYYRIKDFDEPYDDAVRARIAGL 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 523 KPGFYTRIGPAIRHASAKLHERPERRKLLLLLTDGKPNDVDHYEGRFAIEDSRRAVSEARRSGVSVFGVTVDSKAQSYIP 602
Cdd:COG4548  330 EPGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPNDIDVYEGRYGIEDTRQAVREARRAGIHPFCITIDPEADDYLP 409

                        410       420       430
                 ....*....|....*....|....*....|
gi 820894824 603 AMFGQNGYAIVSRIAKLPAALPAIYRSLAG 632
Cdd:COG4548  410 RIFGRGGYTVIDDVERLPERLPQLYRRLTR 439
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 443-613 2.04e-58

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: 193.70  E-value: 2.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 443 LAVTILVDVSLSTDAWfdnrRVLDVEKEALLVLAHGLSACGDSHSILTFTSRR--RSWVRVETVKDFDEPMGHTVERRIA 520
Cdd:cd01454    1 LAVTLLLDLSGSMRSD----RRIDVAKKAAVLLAEALEACGVPHAILGFTTDAggRERVRWIKIKDFDESLHERARKRLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 521 ALKPGFYTRIGPAIRHASAKLHERPERRKLLLLLTDGKPNDVDHYEGR-FAIEDSRRAVSEARRSGVSVFGVTVDSKAQ- 598
Cdd:cd01454   77 ALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNvFATEDALRAVIEARKLGIEVFGITIDRDATt 156

                        170
                 ....*....|....*...
gi 820894824 599 ---SYIPAMFGQNGYAIV 613
Cdd:cd01454  157 vdkEYLKNIFGEEGYALI 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 445-610 9.99e-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: 86.74  E-value: 9.99e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824   445 VTILVDVSLSTdawfdNRRVLDVEKEALLVLAHGLSAC--GDSHSILTFTSRRRSWVRVETVKDFDEpmghtVERRIAAL 522
Cdd:smart00327   2 VVFLLDGSGSM-----GGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDA-----LLEALASL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824   523 KP--GFYTRIGPAIRHA-----SAKLHERPERRKLLLLLTDGKPNDvdhyegrfAIEDSRRAVSEARRSGVSVFGVTVDS 595
Cdd:smart00327  72 SYklGGGTNLGAALQYAlenlfSKSAGSRRGAPKVVILITDGESND--------GPKDLLKAAKELKRSGVKVFVVGVGN 143

                          170
                   ....*....|....*.
gi 820894824   596 KA-QSYIPAMFGQNGY 610
Cdd:smart00327 144 DVdEEELKKLASAPGG 159
VWA pfam00092
von Willebrand factor type A domain;
445-595 2.79e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 53.82  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824  445 VTILVDVSLSTDawfdnRRVLDVEKEALLVLAHGLSACGDSH--SILTFTSRRRSWVRVETVKDFDEpmghtVERRIAAL 522
Cdd:pfam00092   2 IVFLLDGSGSIG-----GDNFEKVKEFLKKLVESLDIGPDGTrvGLVQYSSDVRTEFPLNDYSSKEE-----LLSAVDNL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824  523 K--PGFYTRIGPAIRHASAKL-----HERPERRKLLLLLTDGKPNDvdhyegrfaiEDSRRAVSEARRSGVSVFGVTVDS 595
Cdd:pfam00092  72 RylGGGTTNTGKALKYALENLfssaaGARPGAPKVVVLLTDGRSQD----------GDPEEVARELKSAGVTVFAVGVGN 141
 
Name Accession Description Interval E-value
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
210-632 2.24e-139

Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 413.34  E-value: 2.24e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 210 APPRYLPMLPVPLWPDT----LLRETSEARQSEDQPAAGAAPQGAEAARHIAVREKAENRQTERSPFILNRFEKILAMAE 285
Cdd:COG4548   10 LLLLLLLAARALLAAALaalaAAAEALAAAALLLELLLALLAALRLALLREAAARALALLLGALRLAALLSAGLLELALD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 286 MVNVDRPGDDSDDADGSAADELDDMTLGERKGRPSARFRFDLDLPPEALKHTPLTAELTYPEWDYRSGTYLADHCRVIAG 365
Cdd:COG4548   90 ALPLGRAEPEADAADALDALRDERALDAAADELGDEAPEALGEEPEAPDAAASELSAAGYPEWDYRKQRYRPDWCTVLER 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 366 PAKDAETAPEPD--PDTKSLIRRVRRQFEVLRPRHEMLRAQLDGNDLDLDAVVRARSDIAAGGQGSDRIHMASRPQAHDL 443
Cdd:COG4548  170 RPPEGDPAFLDAtlARHRRLIRRLRRQFEALRPQRVRLRRQEDGDELDLDAAIRALADRRAGGEPDPRIYMRRRRKERDL 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 444 AVTILVDVSLSTDAWFDN-RRVLDVEKEALLVLAHGLSACGDSHSILTFTSRRRSWVRVETVKDFDEPMGHTVERRIAAL 522
Cdd:COG4548  250 AVLLLLDLSLSTDAWVGSgRRVLDVEREALLLLAEALEALGDPFAIYGFSSDGRHRVRYYRIKDFDEPYDDAVRARIAGL 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 523 KPGFYTRIGPAIRHASAKLHERPERRKLLLLLTDGKPNDVDHYEGRFAIEDSRRAVSEARRSGVSVFGVTVDSKAQSYIP 602
Cdd:COG4548  330 EPGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPNDIDVYEGRYGIEDTRQAVREARRAGIHPFCITIDPEADDYLP 409

                        410       420       430
                 ....*....|....*....|....*....|
gi 820894824 603 AMFGQNGYAIVSRIAKLPAALPAIYRSLAG 632
Cdd:COG4548  410 RIFGRGGYTVIDDVERLPERLPQLYRRLTR 439
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 443-613 2.04e-58

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: 193.70  E-value: 2.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 443 LAVTILVDVSLSTDAWfdnrRVLDVEKEALLVLAHGLSACGDSHSILTFTSRR--RSWVRVETVKDFDEPMGHTVERRIA 520
Cdd:cd01454    1 LAVTLLLDLSGSMRSD----RRIDVAKKAAVLLAEALEACGVPHAILGFTTDAggRERVRWIKIKDFDESLHERARKRLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 521 ALKPGFYTRIGPAIRHASAKLHERPERRKLLLLLTDGKPNDVDHYEGR-FAIEDSRRAVSEARRSGVSVFGVTVDSKAQ- 598
Cdd:cd01454   77 ALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNvFATEDALRAVIEARKLGIEVFGITIDRDATt 156

                        170
                 ....*....|....*...
gi 820894824 599 ---SYIPAMFGQNGYAIV 613
Cdd:cd01454  157 vdkEYLKNIFGEEGYALI 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 445-610 9.99e-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: 86.74  E-value: 9.99e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824   445 VTILVDVSLSTdawfdNRRVLDVEKEALLVLAHGLSAC--GDSHSILTFTSRRRSWVRVETVKDFDEpmghtVERRIAAL 522
Cdd:smart00327   2 VVFLLDGSGSM-----GGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDA-----LLEALASL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824   523 KP--GFYTRIGPAIRHA-----SAKLHERPERRKLLLLLTDGKPNDvdhyegrfAIEDSRRAVSEARRSGVSVFGVTVDS 595
Cdd:smart00327  72 SYklGGGTNLGAALQYAlenlfSKSAGSRRGAPKVVILITDGESND--------GPKDLLKAAKELKRSGVKVFVVGVGN 143

                          170
                   ....*....|....*.
gi 820894824   596 KA-QSYIPAMFGQNGY 610
Cdd:smart00327 144 DVdEEELKKLASAPGG 159
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 443-600 2.21e-13

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: 68.36  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 443 LAVTILVDVSLSTdawfdNRRVLDVEKEALLVLAHGLSA--CGDSHSILTFTSRRRSWVRVETVKDFDEpmghtVERRIA 520
Cdd:cd00198    1 ADIVFLLDVSGSM-----GGEKLDKAKEALKALVSSLSAspPGDRVGLVTFGSNARVVLPLTTDTDKAD-----LLEAID 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 521 ALK--PGFYTRIGPAIRHASAKLHE--RPERRKLLLLLTDGKPNDvdhyegrfAIEDSRRAVSEARRSGVSVFGVTVDSK 596
Cdd:cd00198   71 ALKkgLGGGTNIGAALRLALELLKSakRPNARRVIILLTDGEPND--------GPELLAEAARELRKLGITVYTIGIGDD 142


                 ....
gi 820894824 597 AQSY 600
Cdd:cd00198  143 ANED 146
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 364-597 2.23e-12

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: 67.66  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 364 AGPAKDAETAPEPDPDTKSLIRRVRRQFEVLRPRHEMLRAQLDGNDLDLDAVVRARSDIAAGGQGSDRIHMASRPQAHDL 443
Cdd:COG1240   14 ALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 444 AVTILVDVSLSTDAwfdnRRVLDVEKEALLVLAHGLSAcGDSHSILTFtsRRRSWVRVETVKDFDepmghTVERRIAALK 523
Cdd:COG1240   94 DVVLVVDASGSMAA----ENRLEAAKGALLDFLDDYRP-RDRVGLVAF--GGEAEVLLPLTRDRE-----ALKRALDELP 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820894824 524 PGFYTRIGPAIRHASAKL-HERPERRKLLLLLTDGKPNDvdhyegrfAIEDSRRAVSEARRSGVSVFGVTVDSKA 597
Cdd:COG1240  162 PGGGTPLGDALALALELLkRADPARRKVIVLLTDGRDNA--------GRIDPLEAAELAAAAGIRIYTIGVGTEA 228
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 361-594 2.22e-09

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 58.96  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 361 RVIAGPAKDAETAPEPDPDTKSLIRRVRRQFEVLRPRHEMLRAQLDGNDLDLDAVVRARSDIAAGGQGSDRIHMASRPQA 440
Cdd:COG2304    2 EAGFAAADTVPLSTSSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYPLPTGRLAQSPWNPQTRLLLVGLQP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 441 HDLA--------VTILVDVSLSTDAwfdNRrvLDVEKEALLVLAHGLSAcGDSHSILTFTSRRRSWVRVETVKDFDEpmg 512
Cdd:COG2304   82 PKAAaeerpplnLVFVIDVSGSMSG---DK--LELAKEAAKLLVDQLRP-GDRVSIVTFAGDARVLLPPTPATDRAK--- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 513 htVERRIAALKPGFYTRIGPAIRHASAKL--HERPERRKLLLLLTDGKPNdvdhyEGRFAIEDSRRAVSEARRSGV--SV 588
Cdd:COG2304  153 --ILAAIDRLQAGGGTALGAGLELAYELArkHFIPGRVNRVILLTDGDAN-----VGITDPEELLKLAEEAREEGItlTT 225


                 ....*.
gi 820894824 589 FGVTVD 594
Cdd:COG2304  226 LGVGSD 231
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 445-593 2.94e-09

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: 56.15  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 445 VTILVDVSLS-TDAWFDNrrvldvEKEALLVLAHGLSACGDSH--SILTFTSRRRSWVRVETVKDFDEpmghtVERRIAA 521
Cdd:cd01450    3 IVFLLDGSESvGPENFEK------VKDFIEKLVEKLDIGPDKTrvGLVQYSDDVRVEFSLNDYKSKDD-----LLKAVKN 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820894824 522 LKP--GFYTRIGPAIRHASAKL----HERPERRKLLLLLTDGKPNDVDhyegrfaieDSRRAVSEARRSGVSVFGVTV 593
Cdd:cd01450   72 LKYlgGGGTNTGKALQYALEQLfsesNARENVPKVIIVLTDGRSDDGG---------DPKEAAAKLKDEGIKVFVVGV 140
VWA pfam00092
von Willebrand factor type A domain;
445-595 2.79e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 53.82  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824  445 VTILVDVSLSTDawfdnRRVLDVEKEALLVLAHGLSACGDSH--SILTFTSRRRSWVRVETVKDFDEpmghtVERRIAAL 522
Cdd:pfam00092   2 IVFLLDGSGSIG-----GDNFEKVKEFLKKLVESLDIGPDGTrvGLVQYSSDVRTEFPLNDYSSKEE-----LLSAVDNL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824  523 K--PGFYTRIGPAIRHASAKL-----HERPERRKLLLLLTDGKPNDvdhyegrfaiEDSRRAVSEARRSGVSVFGVTVDS 595
Cdd:pfam00092  72 RylGGGTTNTGKALKYALENLfssaaGARPGAPKVVVLLTDGRSQD----------GDPEEVARELKSAGVTVFAVGVGN 141
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
442-556 5.16e-04

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


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 42.50  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 442 DLAVTILVDVSLSTDAWFDNRRVLDVEKEALLVLAHGLSACGDSHSILTFTSRRRSWVRVETVKDFdepmGHTVERRIAA 521
Cdd:COG1721  147 ELTVVLLLDTSASMRFGSGGPSKLDLAVEAAASLAYLALRQGDRVGLLTFGDRVRRYLPPRRGRRH----LLRLLEALAR 222

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 820894824 522 LKPGFYTRIGPAIRHASAKLHerpeRRKLLLLLTD 556
Cdd:COG1721  223 LEPAGETDLAAALRRLARRLP----RRSLVVLISD 253
VWA_2 pfam13519
von Willebrand factor type A domain;
445-554 8.03e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 39.20  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824  445 VTILVDVSLSTDAWFDNRRVLDVEKEALLVLAHGLSacGDSHSILTFTSrrrswvRVETVKDFDEPMGHtVERRIAALKP 524
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKDAVLALLKSLP--GDRVGLVTFGD------GPEVLIPLTKDRAK-ILRALRRLEP 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 820894824  525 -GFYTRIGPAIRHASAKL-HERPERRKLLLLL 554
Cdd:pfam13519  72 kGGGTNLAAALQLARAALkHRRKNQPRRIVLI 103
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 528-593 2.07e-03

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 39.13  E-value: 2.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820894824 528 TRIGPAIRHASAKL-----HERPERRKLLLLLTDGKPNDvdhyegrfaieDSRRAVSEARRSGVSVFGVTV 593
Cdd:cd01472   79 TNTGKALKYVRENLfteasGSREGVPKVLVVITDGKSQD-----------DVEEPAVELKQAGIEVFAVGV 138
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 469-595 3.45e-03

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: 38.74  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 469 KEALLVLAHGLSAcGDSHSILTFTSRRRSWvRVETVKDFDEPMGHTVERrIAALKPGFYTRIGPAIRHASAKLHERPERR 548
Cdd:cd01461   24 KEALLTALKDLPP-GDYFNIIGFSDTVEEF-SPSSVSATAENVAAAIEY-VNRLQALGGTNMNDALEAALELLNSSPGSV 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 820894824 549 KLLLLLTDGKPNDvdhyegRFAIEdsrRAVSEARRSGVSVF----GVTVDS 595
Cdd:cd01461  101 PQIILLTDGEVTN------ESQIL---KNVREALSGRIRLFtfgiGSDVNT 142
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 528-593 5.34e-03

Collagen: 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: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 38.04  E-value: 5.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820894824 528 TRIGPAIRHASAKLHE-----RPERRKLLLLLTDGKPNDvdhyegrfaieDSRRAVSEARRSGVSVFGVTV 593
Cdd:cd01482   79 TRTGKALTHVREKNFTpdagaRPGVPKVVILITDGKSQD-----------DVELPARVLRNLGVNVFAVGV 138
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
434-597 6.62e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 38.37  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 434 MASRPqahdLAVTILVDVSLSTDAwfdnrRVLDVEKEALLVLAHGLSAcgDSH-------SILTFTSRRRSWVRVETVKD 506
Cdd:COG4245    1 NPMRR----LPVYLLLDTSGSMSG-----EPIEALNEGLQALIDELRQ--DPYaletvevSVITFDGEAKVLLPLTDLED 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 507 FDEPmghtverriaALKPGFYTRIGPAIRHASAKLHER---------PERRKLLLLLTDGKPNDVDhYEGrfAIedsRRA 577
Cdd:COG4245   70 FQPP----------DLSASGGTPLGAALELLLDLIERRvqkytaegkGDWRPVVFLITDGEPTDSD-WEA--AL---QRL 133

                        170       180
                 ....*....|....*....|
gi 820894824 578 VSEARRSGVSVFGVTVDSKA 597
Cdd:COG4245  134 KDGEAAKKANIFAIGVGPDA 153
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 443-561 8.65e-03

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 37.38  E-value: 8.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820894824 443 LAVTILVDVSLSTDAWFDNRRvlDVEKEALLVLAHGLSAcgDSHSILTFTSRRRSWVRVETVKdfdEPMGHTVERRIAAL 522
Cdd:cd01476    1 LDLLFVLDSSGSVRGKFEKYK--KYIERIVEGLEIGPTA--TRVALITYSGRGRQRVRFNLPK---HNDGEELLEKVDNL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 820894824 523 KP-GFYTRIGPAIRHASAKLHERPERR----KLLLLLTDGKPND 561
Cdd:cd01476   74 RFiGGTTATGAAIEVALQQLDPSEGRRegipKVVVVLTDGRSHD 117
 
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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