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Conserved domains on  [gi|1176154921|gb|OQX72068|]
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MAG: hypothetical protein B6D62_00090 [Candidatus Cloacimonas sp. 4484_275]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
flgD super family cl31396
flagellar basal body rod modification protein; Reviewed
 10-61 2.37e-07

flagellar basal body rod modification protein; Reviewed


The actual alignment was detected with superfamily member PRK12812:

Pssm-ID: 139245 [Multi-domain]  Cd Length: 259  Bit Score: 45.64  E-value: 2.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1176154921  10 IEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIYFYKLTVNGK 61
Cdd:PRK12812  145 LEIYDSNNKLVEKIDFKEISQGLFTMEWDGRDNDGVYAGDGEYTIKAVYNNK 196
 
Name Accession Description Interval E-value
flgD PRK12812
flagellar basal body rod modification protein; Reviewed
 10-61 2.37e-07

flagellar basal body rod modification protein; Reviewed


Pssm-ID: 139245 [Multi-domain]  Cd Length: 259  Bit Score: 45.64  E-value: 2.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1176154921  10 IEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIYFYKLTVNGK 61
Cdd:PRK12812  145 LEIYDSNNKLVEKIDFKEISQGLFTMEWDGRDNDGVYAGDGEYTIKAVYNNK 196
T9SS_sortase NF033707
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the ...
 10-66 3.75e-07

type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the protease responsible for both removing the C-terminal sorting signal found in substrates and for its replacement by anionic LPS, through which most T9SS substrates become attached to the cell surface after secretion.


Pssm-ID: 468145 [Multi-domain]  Cd Length: 1056  Bit Score: 45.24  E-value: 3.75e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176154921   10 IEIYNIKGQKVKKLVGNKLLKGWNS--IVWDGKDKNGKFVNSGIYFYKLTV---NGKTKAMK 66
Cdd:NF033707   988 VQVFTVSGKLVWTHNQTVTSTGFLSytITWDGRDDFGDRLGKGVYIYRLTVkssDGNKKAEK 1049
FLgD_tudor pfam13861
FlgD Tudor-like domain; This domain has a tudor domain-like beta barrel fold. It is found in ...
 6-62 8.34e-07

FlgD Tudor-like domain; This domain has a tudor domain-like beta barrel fold. It is found in the FlgD protein the flagellar hook capping protein. The structure for this domain shows that it contains a nested Ig-like domain within it. However in some firmicute proteins this inserted domain is absent such as Q67K21.


Pssm-ID: 433533  Cd Length: 136  Bit Score: 42.97  E-value: 8.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1176154921   6 EKAIIEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIyfYKLTVNGKT 62
Cdd:pfam13861  40 DNVTVTIYDSSGQVVRTIDLGAQAAGNVSFTWDGKDSDGNQLPDGT--YTFSVTATA 94
FlgD COG1843
Flagellar hook-capping protein FlgD [Cell motility];
6-65 3.72e-06

Flagellar hook-capping protein FlgD [Cell motility];


Pssm-ID: 441448 [Multi-domain]  Cd Length: 223  Bit Score: 41.91  E-value: 3.72e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154921   6 EKAIIEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIYFYKLTVNGKTKAM 65
Cdd:COG1843   123 DSVTVTITDANGNVVRTIDLGAQSAGVHTFTWDGTDDDGNALPDGTYTFSVEATDDGEPV 182
 
Name Accession Description Interval E-value
flgD PRK12812
flagellar basal body rod modification protein; Reviewed
 10-61 2.37e-07

flagellar basal body rod modification protein; Reviewed


Pssm-ID: 139245 [Multi-domain]  Cd Length: 259  Bit Score: 45.64  E-value: 2.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1176154921  10 IEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIYFYKLTVNGK 61
Cdd:PRK12812  145 LEIYDSNNKLVEKIDFKEISQGLFTMEWDGRDNDGVYAGDGEYTIKAVYNNK 196
T9SS_sortase NF033707
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the ...
 10-66 3.75e-07

type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the protease responsible for both removing the C-terminal sorting signal found in substrates and for its replacement by anionic LPS, through which most T9SS substrates become attached to the cell surface after secretion.


Pssm-ID: 468145 [Multi-domain]  Cd Length: 1056  Bit Score: 45.24  E-value: 3.75e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176154921   10 IEIYNIKGQKVKKLVGNKLLKGWNS--IVWDGKDKNGKFVNSGIYFYKLTV---NGKTKAMK 66
Cdd:NF033707   988 VQVFTVSGKLVWTHNQTVTSTGFLSytITWDGRDDFGDRLGKGVYIYRLTVkssDGNKKAEK 1049
FLgD_tudor pfam13861
FlgD Tudor-like domain; This domain has a tudor domain-like beta barrel fold. It is found in ...
 6-62 8.34e-07

FlgD Tudor-like domain; This domain has a tudor domain-like beta barrel fold. It is found in the FlgD protein the flagellar hook capping protein. The structure for this domain shows that it contains a nested Ig-like domain within it. However in some firmicute proteins this inserted domain is absent such as Q67K21.


Pssm-ID: 433533  Cd Length: 136  Bit Score: 42.97  E-value: 8.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1176154921   6 EKAIIEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIyfYKLTVNGKT 62
Cdd:pfam13861  40 DNVTVTIYDSSGQVVRTIDLGAQAAGNVSFTWDGKDSDGNQLPDGT--YTFSVTATA 94
FlgD COG1843
Flagellar hook-capping protein FlgD [Cell motility];
6-65 3.72e-06

Flagellar hook-capping protein FlgD [Cell motility];


Pssm-ID: 441448 [Multi-domain]  Cd Length: 223  Bit Score: 41.91  E-value: 3.72e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154921   6 EKAIIEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIYFYKLTVNGKTKAM 65
Cdd:COG1843   123 DSVTVTITDANGNVVRTIDLGAQSAGVHTFTWDGTDDDGNALPDGTYTFSVEATDDGEPV 182
FlgD_ig pfam13860
FlgD Ig-like domain; This domains has an immunoglobulin like beta sandwich fold. It is found ...
 6-57 1.75e-05

FlgD Ig-like domain; This domains has an immunoglobulin like beta sandwich fold. It is found in the FlgD protein the flagellar hook capping protein. THe structure for this domain shows that it is inserted within a TUDOR like beta barrel domain.


Pssm-ID: 433532 [Multi-domain]  Cd Length: 78  Bit Score: 38.48  E-value: 1.75e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1176154921  6 EKAIIEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIYFYKLT 57
Cdd:pfam13860 23 DSVTVTIYDAAGQLVRTIDLGAQSAGDVSFTWDGTDDDGNKLADGTYTFSVS 74
flgD PRK06655
flagellar hook assembly protein FlgD;
1-66 1.02e-04

flagellar hook assembly protein FlgD;


Pssm-ID: 235847 [Multi-domain]  Cd Length: 225  Bit Score: 38.00  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176154921   1 MDKKEEKAIIEIYNIKGQKVKKLVGNKLLKGWNSIVWDGKDKNGKFVNSGIYFYKL--TVNGKTKAMK 66
Cdd:PRK06655  121 LPSAADNVTVTITDSAGQVVRTIDLGAQSAGVVSFTWDGTDTDGNALPDGNYTIKAsaSVGGKQLVAQ 188
 
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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