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Conserved domains on  [gi|501579061|ref|WP_012583393|]
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MULTISPECIES: hypothetical protein [Dictyoglomus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FapA super family cl47856
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
298-380 1.84e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


The actual alignment was detected with superfamily member pfam03961:

Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501579061  298 GNVEFQGMVIVKGDV----KITGTGN-KIRGILYAAEVDTavqdlsiYGDPIIEGTSIGEDVSI---GGNSTVRH-NKQY 368
Cdd:pfam03961  14 GNIDFKGSVIIRGDVeegmKVKASGDiTVGGVVESATIEA-------GGDITIKGGIIGRGKGKikaGGNISAKFiQNAE 86
                          90
                  ....*....|....*
gi 501579061  369 IE---NIFKTHSITN 380
Cdd:pfam03961  87 VEaggDILVEKQILH 101
PilX super family cl34809
Type IV pilus assembly protein PilX [Cell motility, Extracellular structures];
12-152 4.59e-03

Type IV pilus assembly protein PilX [Cell motility, Extracellular structures];


The actual alignment was detected with superfamily member COG4726:

Pssm-ID: 443761 [Multi-domain]  Cd Length: 175  Bit Score: 37.77  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501579061  12 AVLIVLFVFLLGMIII-----QLMPSEYAITKRTVESNQAFYLAQSGLQQAIYFINNNPDLAFLELSLRKSGQSNLLSYT 86
Cdd:COG4726   16 AALIVALILLLVLTLLgvaamRSSLLEERMAGNLRDRQLAFQAAEAALRDAEAWLRNASAASLTGLSDCTAASNGLYTSW 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501579061  87 LTYTY--GGNKKENINLNSISLGEYSVNVTY-------SLSNMSSGGIIVSFPIYKIVSIGYIPSIANPRVVRSI 152
Cdd:COG4726   96 SDPVTwtDATATAVGVAYALGTDGVAATPRYiieylgdVTPPTSGGSSSSGSNYYRITARGFGGNANTVVVLQST 170
 
Name Accession Description Interval E-value
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
298-380 1.84e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501579061  298 GNVEFQGMVIVKGDV----KITGTGN-KIRGILYAAEVDTavqdlsiYGDPIIEGTSIGEDVSI---GGNSTVRH-NKQY 368
Cdd:pfam03961  14 GNIDFKGSVIIRGDVeegmKVKASGDiTVGGVVESATIEA-------GGDITIKGGIIGRGKGKikaGGNISAKFiQNAE 86
                          90
                  ....*....|....*
gi 501579061  369 IE---NIFKTHSITN 380
Cdd:pfam03961  87 VEaggDILVEKQILH 101
PilX COG4726
Type IV pilus assembly protein PilX [Cell motility, Extracellular structures];
12-152 4.59e-03

Type IV pilus assembly protein PilX [Cell motility, Extracellular structures];


Pssm-ID: 443761 [Multi-domain]  Cd Length: 175  Bit Score: 37.77  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501579061  12 AVLIVLFVFLLGMIII-----QLMPSEYAITKRTVESNQAFYLAQSGLQQAIYFINNNPDLAFLELSLRKSGQSNLLSYT 86
Cdd:COG4726   16 AALIVALILLLVLTLLgvaamRSSLLEERMAGNLRDRQLAFQAAEAALRDAEAWLRNASAASLTGLSDCTAASNGLYTSW 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501579061  87 LTYTY--GGNKKENINLNSISLGEYSVNVTY-------SLSNMSSGGIIVSFPIYKIVSIGYIPSIANPRVVRSI 152
Cdd:COG4726   96 SDPVTwtDATATAVGVAYALGTDGVAATPRYiieylgdVTPPTSGGSSSSGSNYYRITARGFGGNANTVVVLQST 170
 
Name Accession Description Interval E-value
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
298-380 1.84e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501579061  298 GNVEFQGMVIVKGDV----KITGTGN-KIRGILYAAEVDTavqdlsiYGDPIIEGTSIGEDVSI---GGNSTVRH-NKQY 368
Cdd:pfam03961  14 GNIDFKGSVIIRGDVeegmKVKASGDiTVGGVVESATIEA-------GGDITIKGGIIGRGKGKikaGGNISAKFiQNAE 86
                          90
                  ....*....|....*
gi 501579061  369 IE---NIFKTHSITN 380
Cdd:pfam03961  87 VEaggDILVEKQILH 101
PilX COG4726
Type IV pilus assembly protein PilX [Cell motility, Extracellular structures];
12-152 4.59e-03

Type IV pilus assembly protein PilX [Cell motility, Extracellular structures];


Pssm-ID: 443761 [Multi-domain]  Cd Length: 175  Bit Score: 37.77  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501579061  12 AVLIVLFVFLLGMIII-----QLMPSEYAITKRTVESNQAFYLAQSGLQQAIYFINNNPDLAFLELSLRKSGQSNLLSYT 86
Cdd:COG4726   16 AALIVALILLLVLTLLgvaamRSSLLEERMAGNLRDRQLAFQAAEAALRDAEAWLRNASAASLTGLSDCTAASNGLYTSW 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501579061  87 LTYTY--GGNKKENINLNSISLGEYSVNVTY-------SLSNMSSGGIIVSFPIYKIVSIGYIPSIANPRVVRSI 152
Cdd:COG4726   96 SDPVTwtDATATAVGVAYALGTDGVAATPRYiieylgdVTPPTSGGSSSSGSNYYRITARGFGGNANTVVVLQST 170
 
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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