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Conserved domains on  [gi|947654100|ref|WP_056316815|]
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MULTISPECIES: NfeD family protein [Achromobacter]

Protein Classification

NfeD family protein( domain architecture ID 10003982)

NfeD (nodulation formation efficiency D) family protein containing only the C-terminal soluble OB-fold NfeD (NfeDC) domain, may function by associating with neighboring slipin clusters; similar to Escherichia coli inner membrane protein YbbJ

CATH:  2.40.50.140
Gene Ontology:  GO:0016020
PubMed:  20012272|18687870
SCOP:  4001808

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YbbJ COG1585
Membrane protein implicated in regulation of membrane protease activity [Posttranslational ...
 2-139 1.36e-13

Membrane protein implicated in regulation of membrane protease activity [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441193  Cd Length: 143  Bit Score: 63.29  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947654100   2 WIWLGLAALALIGELATGTFYLLLVALGLAAGGIAAWLSAGLQWELVACGVVLLLGLLVLRKTRVLKKREVNSARNADVN 81
Cdd:COG1585    7 LIWLILGLLLLIAELLTPGFFLLWFGLGALAVGLLALLGLSLWLQLLVFAVLSLLLLLLWRRLLKRRLRSDAPLLNTRVD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 947654100  82 LDIGQTVVVEAWSDSGAARVWYRGAHWQAELAKGHAAHpGEHIITELRGSILVLTPKR 139
Cdd:COG1585   87 ALIGRTATVVEPIDNGRGRVKLGGEEWRARSEDDLPAG-TRVRVVAVEGNTLIVEPVE 143
 
Name Accession Description Interval E-value
YbbJ COG1585
Membrane protein implicated in regulation of membrane protease activity [Posttranslational ...
 2-139 1.36e-13

Membrane protein implicated in regulation of membrane protease activity [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441193  Cd Length: 143  Bit Score: 63.29  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947654100   2 WIWLGLAALALIGELATGTFYLLLVALGLAAGGIAAWLSAGLQWELVACGVVLLLGLLVLRKTRVLKKREVNSARNADVN 81
Cdd:COG1585    7 LIWLILGLLLLIAELLTPGFFLLWFGLGALAVGLLALLGLSLWLQLLVFAVLSLLLLLLWRRLLKRRLRSDAPLLNTRVD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 947654100  82 LDIGQTVVVEAWSDSGAARVWYRGAHWQAELAKGHAAHpGEHIITELRGSILVLTPKR 139
Cdd:COG1585   87 ALIGRTATVVEPIDNGRGRVKLGGEEWRARSEDDLPAG-TRVRVVAVEGNTLIVEPVE 143
NfeD pfam01957
NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout ...
 65-137 1.53e-07

NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout prokaryotes and are frequently associated with genes encoding stomatin-like proteins (slipins). There appear to be three major groups: an ancestral group with only an N-terminal serine protease domain and this C-terminal beta sheet-rich domain which is structurally very similar to the OB-fold domain, associated with its neighbouring slipin cluster; a second major group with an additional middle, membrane-spanning domain, associated in some species with eoslipin and in others with yqfA; a final 'artificial' group which unites truncated forms lacking the protease region and associated with their ancestral gene partner, either yqfA or eoslipin. This NefD, C-terminal, domain appears to be the major one for relating to the associated protein. NfeD homologs are clearly reliant on their conserved gene neighbour which is assumed to be necessary for function, either through direct physical interaction or by functioning in the same pathway, possibly involve with lipid-rafts.


Pssm-ID: 460395  Cd Length: 90  Bit Score: 46.42  E-value: 1.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 947654100   65 RVLKKREVNSARNADVNLdIGQTVVVEAWSDSGAARVWYRGAHWQAELAKGHAAHPGEHIITELRGSILVLTP 137
Cdd:pfam01957  19 KRLRKKSPGSLTNRDEAL-IGRTGVVLEDIRPDGGRVKIDGEEWTARSDGDFIPAGTRVRVVAVEGLTLIVEP 90
 
Name Accession Description Interval E-value
YbbJ COG1585
Membrane protein implicated in regulation of membrane protease activity [Posttranslational ...
 2-139 1.36e-13

Membrane protein implicated in regulation of membrane protease activity [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441193  Cd Length: 143  Bit Score: 63.29  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947654100   2 WIWLGLAALALIGELATGTFYLLLVALGLAAGGIAAWLSAGLQWELVACGVVLLLGLLVLRKTRVLKKREVNSARNADVN 81
Cdd:COG1585    7 LIWLILGLLLLIAELLTPGFFLLWFGLGALAVGLLALLGLSLWLQLLVFAVLSLLLLLLWRRLLKRRLRSDAPLLNTRVD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 947654100  82 LDIGQTVVVEAWSDSGAARVWYRGAHWQAELAKGHAAHpGEHIITELRGSILVLTPKR 139
Cdd:COG1585   87 ALIGRTATVVEPIDNGRGRVKLGGEEWRARSEDDLPAG-TRVRVVAVEGNTLIVEPVE 143
NfeD pfam01957
NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout ...
 65-137 1.53e-07

NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout prokaryotes and are frequently associated with genes encoding stomatin-like proteins (slipins). There appear to be three major groups: an ancestral group with only an N-terminal serine protease domain and this C-terminal beta sheet-rich domain which is structurally very similar to the OB-fold domain, associated with its neighbouring slipin cluster; a second major group with an additional middle, membrane-spanning domain, associated in some species with eoslipin and in others with yqfA; a final 'artificial' group which unites truncated forms lacking the protease region and associated with their ancestral gene partner, either yqfA or eoslipin. This NefD, C-terminal, domain appears to be the major one for relating to the associated protein. NfeD homologs are clearly reliant on their conserved gene neighbour which is assumed to be necessary for function, either through direct physical interaction or by functioning in the same pathway, possibly involve with lipid-rafts.


Pssm-ID: 460395  Cd Length: 90  Bit Score: 46.42  E-value: 1.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 947654100   65 RVLKKREVNSARNADVNLdIGQTVVVEAWSDSGAARVWYRGAHWQAELAKGHAAHPGEHIITELRGSILVLTP 137
Cdd:pfam01957  19 KRLRKKSPGSLTNRDEAL-IGRTGVVLEDIRPDGGRVKIDGEEWTARSDGDFIPAGTRVRVVAVEGLTLIVEP 90
 
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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