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Conserved domains on  [gi|1877245511|emb|VUX56413|]
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putative General secretion pathway, GspH [uncultured Woeseiaceae bacterium]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
3-72 1.12e-16

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


:

Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 70.65  E-value: 1.12e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877245511   3 IRRTTGGYSLYELIITIGLVALVMSLGVPSFGKILANHRLKVEVDALFHAVHLARKESVVRRRAVTLCPS 72
Cdd:COG4970     4 LRRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAALRLARSEAIRRGQPVTLSPS 73
GspH pfam12019
Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all ...
45-161 1.09e-14

Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all pilins, GspH has an N terminus alpha helix. This helix is followed by nine beta strands forming two beta sheets, one of five antiparallel strands and one of four antiparallel strands. GspH is a minor pseudopilin; it is expressed much less than other pseudopilins in the type II secretion pilus (major pilins). The function and localization of minor pseudo-pilins are still to be fully unraveled. It has been suggested that some minor pseudopilins may assemble either into the base or the tip of pili, or both. They function as initiators or regulators of pilus biogenesis and dynamics, and/or as adaptors between various pseudopilin component and other members of the T2SS.


:

Pssm-ID: 463433  Cd Length: 108  Bit Score: 66.46  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877245511  45 EVDALFHAVHLARKESVVRRRAVTLCPSrdgqncepdfDWSDGWIMFVnlDRDVPATRDSDEPLLQRF----SGILHNKV 120
Cdd:pfam12019   1 AANRLAAALQLARSEAIKRGRPVTVCPS----------DWSGGWIVFV--DANANGDLDGGEDLLRVGaalaGGDVLVTA 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1877245511 121 TANRRSFSFRTTALRATNGTFIFCDkAGRAEVRALIVSYTG 161
Cdd:pfam12019  69 SSASPQITFNPDGRAATPGTLTLCS-GGSGRSRRVVVSASG 108
 
Name Accession Description Interval E-value
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
3-72 1.12e-16

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 70.65  E-value: 1.12e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877245511   3 IRRTTGGYSLYELIITIGLVALVMSLGVPSFGKILANHRLKVEVDALFHAVHLARKESVVRRRAVTLCPS 72
Cdd:COG4970     4 LRRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAALRLARSEAIRRGQPVTLSPS 73
GspH pfam12019
Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all ...
45-161 1.09e-14

Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all pilins, GspH has an N terminus alpha helix. This helix is followed by nine beta strands forming two beta sheets, one of five antiparallel strands and one of four antiparallel strands. GspH is a minor pseudopilin; it is expressed much less than other pseudopilins in the type II secretion pilus (major pilins). The function and localization of minor pseudo-pilins are still to be fully unraveled. It has been suggested that some minor pseudopilins may assemble either into the base or the tip of pili, or both. They function as initiators or regulators of pilus biogenesis and dynamics, and/or as adaptors between various pseudopilin component and other members of the T2SS.


Pssm-ID: 463433  Cd Length: 108  Bit Score: 66.46  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877245511  45 EVDALFHAVHLARKESVVRRRAVTLCPSrdgqncepdfDWSDGWIMFVnlDRDVPATRDSDEPLLQRF----SGILHNKV 120
Cdd:pfam12019   1 AANRLAAALQLARSEAIKRGRPVTVCPS----------DWSGGWIVFV--DANANGDLDGGEDLLRVGaalaGGDVLVTA 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1877245511 121 TANRRSFSFRTTALRATNGTFIFCDkAGRAEVRALIVSYTG 161
Cdd:pfam12019  69 SSASPQITFNPDGRAATPGTLTLCS-GGSGRSRRVVVSASG 108
 
Name Accession Description Interval E-value
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
3-72 1.12e-16

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


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 70.65  E-value: 1.12e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877245511   3 IRRTTGGYSLYELIITIGLVALVMSLGVPSFGKILANHRLKVEVDALFHAVHLARKESVVRRRAVTLCPS 72
Cdd:COG4970     4 LRRRQRGFTLIELLVVLAILAILAAIAVPSFSSLIARQRLRAAANELAAALRLARSEAIRRGQPVTLSPS 73
GspH pfam12019
Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all ...
45-161 1.09e-14

Type II transport protein GspH; GspH is involved in bacterial type II export systems. Like all pilins, GspH has an N terminus alpha helix. This helix is followed by nine beta strands forming two beta sheets, one of five antiparallel strands and one of four antiparallel strands. GspH is a minor pseudopilin; it is expressed much less than other pseudopilins in the type II secretion pilus (major pilins). The function and localization of minor pseudo-pilins are still to be fully unraveled. It has been suggested that some minor pseudopilins may assemble either into the base or the tip of pili, or both. They function as initiators or regulators of pilus biogenesis and dynamics, and/or as adaptors between various pseudopilin component and other members of the T2SS.


Pssm-ID: 463433  Cd Length: 108  Bit Score: 66.46  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1877245511  45 EVDALFHAVHLARKESVVRRRAVTLCPSrdgqncepdfDWSDGWIMFVnlDRDVPATRDSDEPLLQRF----SGILHNKV 120
Cdd:pfam12019   1 AANRLAAALQLARSEAIKRGRPVTVCPS----------DWSGGWIVFV--DANANGDLDGGEDLLRVGaalaGGDVLVTA 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1877245511 121 TANRRSFSFRTTALRATNGTFIFCDkAGRAEVRALIVSYTG 161
Cdd:pfam12019  69 SSASPQITFNPDGRAATPGTLTLCS-GGSGRSRRVVVSASG 108
 
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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