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Conserved domains on  [gi|15600404|ref|NP_253898|]
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hypothetical protein PA5211 [Pseudomonas aeruginosa PAO1]

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 ...
 8-149 1.11e-27

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


:

Pssm-ID: 441193  Cd Length: 143  Bit Score: 99.89  E-value: 1.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600404   8 LDFWDWLAFGTVLLLLEIFGAGGYLLRVGLTAACVGALGALlpGLAWPWQVGLFVLLSGLVAALHRRRRRKAGSvEETPG 87
Cdd:COG1585   4 LPWLIWLILGLLLLIAELLTPGFFLLWFGLGALAVGLLALL--GLSLWLQLLVFAVLSLLLLLLWRRLLKRRLR-SDAPL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600404  88 LQRRGDDLFGRTFPLHRAIVGGLGELRVEDASWLVSGPD-LPRGALVRVTGQDGALLHVEPAA 149
Cdd:COG1585  81 LNTRVDALIGRTATVVEPIDNGRGRVKLGGEEWRARSEDdLPAGTRVRVVAVEGNTLIVEPVE 143
 
Name Accession Description Interval E-value
YbbJ COG1585
Membrane protein implicated in regulation of membrane protease activity [Posttranslational ...
 8-149 1.11e-27

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


Pssm-ID: 441193  Cd Length: 143  Bit Score: 99.89  E-value: 1.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600404   8 LDFWDWLAFGTVLLLLEIFGAGGYLLRVGLTAACVGALGALlpGLAWPWQVGLFVLLSGLVAALHRRRRRKAGSvEETPG 87
Cdd:COG1585   4 LPWLIWLILGLLLLIAELLTPGFFLLWFGLGALAVGLLALL--GLSLWLQLLVFAVLSLLLLLLWRRLLKRRLR-SDAPL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600404  88 LQRRGDDLFGRTFPLHRAIVGGLGELRVEDASWLVSGPD-LPRGALVRVTGQDGALLHVEPAA 149
Cdd:COG1585  81 LNTRVDALIGRTATVVEPIDNGRGRVKLGGEEWRARSEDdLPAGTRVRVVAVEGNTLIVEPVE 143
NfeD pfam01957
NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout ...
 60-147 2.82e-11

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: 56.05  E-value: 2.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600404    60 LFVLLSGLVAALHRRRRRKAGSVEETPGLQRRGDDLFGRTFPLHRAIVGGLGELRVEDASWLV--SGPDLPRGALVRVTG 137
Cdd:pfam01957   1 VFAVVSLVLLLLLRPLALKRLRKKSPGSLTNRDEALIGRTGVVLEDIRPDGGRVKIDGEEWTArsDGDFIPAGTRVRVVA 80

                          90
                  ....*....|
gi 15600404   138 QDGALLHVEP 147
Cdd:pfam01957  81 VEGLTLIVEP 90
 
Name Accession Description Interval E-value
YbbJ COG1585
Membrane protein implicated in regulation of membrane protease activity [Posttranslational ...
 8-149 1.11e-27

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


Pssm-ID: 441193  Cd Length: 143  Bit Score: 99.89  E-value: 1.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600404   8 LDFWDWLAFGTVLLLLEIFGAGGYLLRVGLTAACVGALGALlpGLAWPWQVGLFVLLSGLVAALHRRRRRKAGSvEETPG 87
Cdd:COG1585   4 LPWLIWLILGLLLLIAELLTPGFFLLWFGLGALAVGLLALL--GLSLWLQLLVFAVLSLLLLLLWRRLLKRRLR-SDAPL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600404  88 LQRRGDDLFGRTFPLHRAIVGGLGELRVEDASWLVSGPD-LPRGALVRVTGQDGALLHVEPAA 149
Cdd:COG1585  81 LNTRVDALIGRTATVVEPIDNGRGRVKLGGEEWRARSEDdLPAGTRVRVVAVEGNTLIVEPVE 143
NfeD pfam01957
NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout ...
 60-147 2.82e-11

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: 56.05  E-value: 2.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600404    60 LFVLLSGLVAALHRRRRRKAGSVEETPGLQRRGDDLFGRTFPLHRAIVGGLGELRVEDASWLV--SGPDLPRGALVRVTG 137
Cdd:pfam01957   1 VFAVVSLVLLLLLRPLALKRLRKKSPGSLTNRDEALIGRTGVVLEDIRPDGGRVKIDGEEWTArsDGDFIPAGTRVRVVA 80

                          90
                  ....*....|
gi 15600404   138 QDGALLHVEP 147
Cdd:pfam01957  81 VEGLTLIVEP 90
NfeD COG1030
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein ...
 14-148 3.52e-03

Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440653 [Multi-domain]  Cd Length: 413  Bit Score: 36.38  E-value: 3.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600404  14 LAFGTVLLLLEIF-------GAGGYLLrvgLTAACVGALGALLPGL--AWPWQVGLFVLLSGLVA-----ALHRRRRRKA 79
Cdd:COG1030 275 FLLGIILLILELFvpgfgilGIGGIIA---LVLGLLLLFDTDVPGLgvSALLIVAIALVIAIFLAfvlgkVLRARKRKPV 351

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600404  80 GSVEETPGLQrrgddlfGRTfplhRAIVGGLGELRVEDASWLV--SGPDLPRGALVRVTGQDGALLHVEPA 148
Cdd:COG1030 352 TGAEELIGKE-------GVA----LTDLRPSGKVRIDGERWDAvsEGEFIEKGEKVRVVGVEGLRLVVRPV 411
 
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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