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Conserved domains on  [gi|447171610|ref|WP_001248866|]
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MULTISPECIES: nitric oxide reductase activation protein NorD [Bacillus]

Protein Classification

vWA domain-containing protein( domain architecture ID 10106921)

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:  10830113|12388743|12579041
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 431-599 1.15e-60

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: 199.47  E-value: 1.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 431 VAFQLLVDCSGSMYN--KMEETKKSVVLFHEALKSLKIPHAISGFWEDAssaKPEDKPNVIHEVvTYKNSTLPNVGPEIM 508
Cdd:cd01454    1 LAVTLLLDLSGSMRSdrRIDVAKKAAVLLAEALEACGVPHAILGFTTDA---GGRERVRWIKIK-DFDESLHERARKRLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 509 QLREEEDNRDGYIIRIVSEKLAKRPEKHKFLLVFTDGEPSALDYQQDGILDTHE---AVKLARKSGMEVIGIFIeEGEAK 585
Cdd:cd01454   77 ALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVFATEDalrAVIEARKLGIEVFGITI-DRDAT 155

                        170
                 ....*....|....
gi 447171610 586 EATYQLMKNIYNHH 599
Cdd:cd01454  156 TVDKEYLKNIFGEE 169
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 431-599 1.15e-60

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: 199.47  E-value: 1.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 431 VAFQLLVDCSGSMYN--KMEETKKSVVLFHEALKSLKIPHAISGFWEDAssaKPEDKPNVIHEVvTYKNSTLPNVGPEIM 508
Cdd:cd01454    1 LAVTLLLDLSGSMRSdrRIDVAKKAAVLLAEALEACGVPHAILGFTTDA---GGRERVRWIKIK-DFDESLHERARKRLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 509 QLREEEDNRDGYIIRIVSEKLAKRPEKHKFLLVFTDGEPSALDYQQDGILDTHE---AVKLARKSGMEVIGIFIeEGEAK 585
Cdd:cd01454   77 ALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVFATEDalrAVIEARKLGIEVFGITI-DRDAT 155

                        170
                 ....*....|....
gi 447171610 586 EATYQLMKNIYNHH 599
Cdd:cd01454  156 TVDKEYLKNIFGEE 169
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
415-608 8.75e-35

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


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 137.16  E-value: 8.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 415 QPRMFYKkgQESQELDVAFQLLVDCSGSM-------YNKMEETKKSVVLFHEALKSLKIPHAISGFwedaSSAKPEDkpN 487
Cdd:COG4548  235 DPRIYMR--RRRKERDLAVLLLLDLSLSTdawvgsgRRVLDVEREALLLLAEALEALGDPFAIYGF----SSDGRHR--V 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 488 VIHEVVTYKNSTLPNVGPEIMQLREEEDNRDGYIIRIVSEKLAKRPEKHKFLLVFTDGEPSALDYQ--QDGILDTHEAVK 565
Cdd:COG4548  307 RYYRIKDFDEPYDDAVRARIAGLEPGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPNDIDVYegRYGIEDTRQAVR 386

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 447171610 566 LARKSGMEVIGIFIEEgEAKEatYqlMKNIY-NHHFLVANHAED 608
Cdd:COG4548  387 EARRAGIHPFCITIDP-EADD--Y--LPRIFgRGGYTVIDDVER 425
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 430-602 1.19e-11

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: 63.63  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610   430 DVAFqlLVDCSGSMY-NKMEETKKSVVLFHEALKS--LKIPHAISGFWEDA----SSAKPEDKPNVIHEV--VTYKNSTL 500
Cdd:smart00327   1 DVVF--LLDGSGSMGgNRFELAKEFVLKLVEQLDIgpDGDRVGLVTFSDDArvlfPLNDSRSKDALLEALasLSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610   501 PNVGPEIMQLREEednrdgyiirIVSEKLAKRPEKHKFLLVFTDGEPsaldyqQDGILDTHEAVKLARKSGMEVIGIFIE 580
Cdd:smart00327  79 TNLGAALQYALEN----------LFSKSAGSRRGAPKVVILITDGES------NDGPKDLLKAAKELKRSGVKVFVVGVG 142

                          170       180
                   ....*....|....*....|...
gi 447171610   581 EGEAKEATYQL-MKNIYNHHFLV 602
Cdd:smart00327 143 NDVDEEELKKLaSAPGGVYVFLP 165
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
 420-547 3.89e-04

Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial cobalamin biosynthesis (CobT) proteins. CobT is involved in the transformation of precorrin-3 into cobyrinic acid.


Pssm-ID: 288608 [Multi-domain]  Cd Length: 220  Bit Score: 42.32  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610  420 YKKGQESQELDVAFQLLVDCSGSMYN-KMEETKKSVVLFHEALKSLKIPHAISGF-------------WEDASSAKPEDK 485
Cdd:pfam11775   2 FMHEEDARARDACVQLLIDLSGSMGGrKIQLAAACADIIADALDRCGVKNEILGFttfawkggpdreaMLAAGFPAFEAL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447171610  486 PNVIHEVVtYKNSTLPNV-GPEIMQLREEE----DNRDGYIIRIVSEKLAKRPEKHKFLLVFTDGEP 547
Cdd:pfam11775  82 LLDIIHII-NEKADAPEIrARKNLGCMCEEfllkENIDGEALAQAAKLFAGRMEDKKILLMISDGAP 147
 
Name Accession Description Interval E-value
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 431-599 1.15e-60

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: 199.47  E-value: 1.15e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 431 VAFQLLVDCSGSMYN--KMEETKKSVVLFHEALKSLKIPHAISGFWEDAssaKPEDKPNVIHEVvTYKNSTLPNVGPEIM 508
Cdd:cd01454    1 LAVTLLLDLSGSMRSdrRIDVAKKAAVLLAEALEACGVPHAILGFTTDA---GGRERVRWIKIK-DFDESLHERARKRLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 509 QLREEEDNRDGYIIRIVSEKLAKRPEKHKFLLVFTDGEPSALDYQQDGILDTHE---AVKLARKSGMEVIGIFIeEGEAK 585
Cdd:cd01454   77 ALSPGGNTRDGAAIRHAAERLLARPEKRKILLVISDGEPNDLDYYEGNVFATEDalrAVIEARKLGIEVFGITI-DRDAT 155

                        170
                 ....*....|....
gi 447171610 586 EATYQLMKNIYNHH 599
Cdd:cd01454  156 TVDKEYLKNIFGEE 169
NorD COG4548
Nitric oxide reductase activation protein [Inorganic ion transport and metabolism];
415-608 8.75e-35

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


Pssm-ID: 443612 [Multi-domain]  Cd Length: 439  Bit Score: 137.16  E-value: 8.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 415 QPRMFYKkgQESQELDVAFQLLVDCSGSM-------YNKMEETKKSVVLFHEALKSLKIPHAISGFwedaSSAKPEDkpN 487
Cdd:COG4548  235 DPRIYMR--RRRKERDLAVLLLLDLSLSTdawvgsgRRVLDVEREALLLLAEALEALGDPFAIYGF----SSDGRHR--V 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 488 VIHEVVTYKNSTLPNVGPEIMQLREEEDNRDGYIIRIVSEKLAKRPEKHKFLLVFTDGEPSALDYQ--QDGILDTHEAVK 565
Cdd:COG4548  307 RYYRIKDFDEPYDDAVRARIAGLEPGYYTRMGAAIRHATALLAAQPARRRLLLVLTDGKPNDIDVYegRYGIEDTRQAVR 386

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 447171610 566 LARKSGMEVIGIFIEEgEAKEatYqlMKNIY-NHHFLVANHAED 608
Cdd:COG4548  387 EARRAGIHPFCITIDP-EADD--Y--LPRIFgRGGYTVIDDVER 425
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 430-602 1.19e-11

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: 63.63  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610   430 DVAFqlLVDCSGSMY-NKMEETKKSVVLFHEALKS--LKIPHAISGFWEDA----SSAKPEDKPNVIHEV--VTYKNSTL 500
Cdd:smart00327   1 DVVF--LLDGSGSMGgNRFELAKEFVLKLVEQLDIgpDGDRVGLVTFSDDArvlfPLNDSRSKDALLEALasLSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610   501 PNVGPEIMQLREEednrdgyiirIVSEKLAKRPEKHKFLLVFTDGEPsaldyqQDGILDTHEAVKLARKSGMEVIGIFIE 580
Cdd:smart00327  79 TNLGAALQYALEN----------LFSKSAGSRRGAPKVVILITDGES------NDGPKDLLKAAKELKRSGVKVFVVGVG 142

                          170       180
                   ....*....|....*....|...
gi 447171610   581 EGEAKEATYQL-MKNIYNHHFLV 602
Cdd:smart00327 143 NDVDEEELKKLaSAPGGVYVFLP 165
CobT_C pfam11775
Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial ...
 420-547 3.89e-04

Cobalamin biosynthesis protein CobT VWA domain; This family consists of several bacterial cobalamin biosynthesis (CobT) proteins. CobT is involved in the transformation of precorrin-3 into cobyrinic acid.


Pssm-ID: 288608 [Multi-domain]  Cd Length: 220  Bit Score: 42.32  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610  420 YKKGQESQELDVAFQLLVDCSGSMYN-KMEETKKSVVLFHEALKSLKIPHAISGF-------------WEDASSAKPEDK 485
Cdd:pfam11775   2 FMHEEDARARDACVQLLIDLSGSMGGrKIQLAAACADIIADALDRCGVKNEILGFttfawkggpdreaMLAAGFPAFEAL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447171610  486 PNVIHEVVtYKNSTLPNV-GPEIMQLREEE----DNRDGYIIRIVSEKLAKRPEKHKFLLVFTDGEP 547
Cdd:pfam11775  82 LLDIIHII-NEKADAPEIrARKNLGCMCEEfllkENIDGEALAQAAKLFAGRMEDKKILLMISDGAP 147
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
435-554 3.57e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 39.14  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447171610 435 LLVDCSGSMY-NKMEETKKSVVLFHEALKSLKIPH-----AISGFwedASSAKpedkpnVIHEVVTYKNSTLPNV----- 503
Cdd:COG4245   10 LLLDTSGSMSgEPIEALNEGLQALIDELRQDPYALetvevSVITF---DGEAK------VLLPLTDLEDFQPPDLsasgg 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 447171610 504 ---GPEIMQLREEEDNRDGYIIRivSEKLAKRPekhkFLLVFTDGEPSALDYQQ 554
Cdd:COG4245   81 tplGAALELLLDLIERRVQKYTA--EGKGDWRP----VVFLITDGEPTDSDWEA 128
 
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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