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Conserved domains on  [gi|517998445|ref|WP_019168653|]
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NfeD family protein [Staphylococcus intermedius]

Protein Classification

NfeD family protein( domain architecture ID 1002096)

NfeD (nodulation formation efficiency D) family protein containing only the C-terminal soluble OB-fold NfeD (NfeDC) domain, may interact with other spatially proximal membrane proteins and regulate their activities

CATH:  2.40.50.140
PubMed:  20012272
SCOP:  4001808

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NfeD super family cl34070
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein ...
20-225 4.69e-34

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


The actual alignment was detected with superfamily member COG1030:

Pssm-ID: 440653 [Multi-domain]  Cd Length: 413  Bit Score: 125.74  E-value: 4.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  20 WITSQTISLILTCIVFLGFLYQLYSRKINFGGIFAFFALLMIFLGFVIqgSLTVVTIMIFIIGVILVIIELFV--FGAVL 97
Cdd:COG1030  218 FLTNPNVAYILLLIGILGLIFELYTPGFGVPGVIGAIALLLAFYGLYL--PANYAGLLLFLLGIILLILELFVpgFGILG 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  98 GIIGMILIILSFITLGNDLPM----MLFNVVFALILTLIEWVILVKFFKKSislfdkvvLKDSTSkesgytshnDRSHLV 173
Cdd:COG1030  296 IGGIIALVLGLLLLFDTDVPGlgvsALLIVAIALVIAIFLAFVLGKVLRAR--------KRKPVT---------GAEELI 358
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517998445 174 DQTAVTYTDLRPSGIIILNNERIDAVSEGSYISKDTEVKIIEVEGTRVVVRE 225
Cdd:COG1030  359 GKEGVALTDLRPSGKVRIDGERWDAVSEGEFIEKGEKVRVVGVEGLRLVVRP 410
 
Name Accession Description Interval E-value
NfeD COG1030
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein ...
20-225 4.69e-34

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


Pssm-ID: 440653 [Multi-domain]  Cd Length: 413  Bit Score: 125.74  E-value: 4.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  20 WITSQTISLILTCIVFLGFLYQLYSRKINFGGIFAFFALLMIFLGFVIqgSLTVVTIMIFIIGVILVIIELFV--FGAVL 97
Cdd:COG1030  218 FLTNPNVAYILLLIGILGLIFELYTPGFGVPGVIGAIALLLAFYGLYL--PANYAGLLLFLLGIILLILELFVpgFGILG 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  98 GIIGMILIILSFITLGNDLPM----MLFNVVFALILTLIEWVILVKFFKKSislfdkvvLKDSTSkesgytshnDRSHLV 173
Cdd:COG1030  296 IGGIIALVLGLLLLFDTDVPGlgvsALLIVAIALVIAIFLAFVLGKVLRAR--------KRKPVT---------GAEELI 358
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517998445 174 DQTAVTYTDLRPSGIIILNNERIDAVSEGSYISKDTEVKIIEVEGTRVVVRE 225
Cdd:COG1030  359 GKEGVALTDLRPSGKVRIDGERWDAVSEGEFIEKGEKVRVVGVEGLRLVVRP 410
NfeD pfam01957
NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout ...
144-225 7.31e-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: 56.82  E-value: 7.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  144 SISLFDKVVLKDSTSKESGYTShNDRSHLVDQTAVTYTDLRPS-GIIILNNERIDAVSEGSYISKDTEVKIIEVEGTRVV 222
Cdd:pfam01957   9 LLLLLRPLALKRLRKKSPGSLT-NRDEALIGRTGVVLEDIRPDgGRVKIDGEEWTARSDGDFIPAGTRVRVVAVEGLTLI 87

                  ...
gi 517998445  223 VRE 225
Cdd:pfam01957  88 VEP 90
 
Name Accession Description Interval E-value
NfeD COG1030
Membrane-bound serine protease NfeD, ClpP class [Posttranslational modification, protein ...
20-225 4.69e-34

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


Pssm-ID: 440653 [Multi-domain]  Cd Length: 413  Bit Score: 125.74  E-value: 4.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  20 WITSQTISLILTCIVFLGFLYQLYSRKINFGGIFAFFALLMIFLGFVIqgSLTVVTIMIFIIGVILVIIELFV--FGAVL 97
Cdd:COG1030  218 FLTNPNVAYILLLIGILGLIFELYTPGFGVPGVIGAIALLLAFYGLYL--PANYAGLLLFLLGIILLILELFVpgFGILG 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  98 GIIGMILIILSFITLGNDLPM----MLFNVVFALILTLIEWVILVKFFKKSislfdkvvLKDSTSkesgytshnDRSHLV 173
Cdd:COG1030  296 IGGIIALVLGLLLLFDTDVPGlgvsALLIVAIALVIAIFLAFVLGKVLRAR--------KRKPVT---------GAEELI 358
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517998445 174 DQTAVTYTDLRPSGIIILNNERIDAVSEGSYISKDTEVKIIEVEGTRVVVRE 225
Cdd:COG1030  359 GKEGVALTDLRPSGKVRIDGERWDAVSEGEFIEKGEKVRVVGVEGLRLVVRP 410
NfeD pfam01957
NfeD-like C-terminal, partner-binding; NfeD-like proteins are widely distributed throughout ...
144-225 7.31e-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: 56.82  E-value: 7.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517998445  144 SISLFDKVVLKDSTSKESGYTShNDRSHLVDQTAVTYTDLRPS-GIIILNNERIDAVSEGSYISKDTEVKIIEVEGTRVV 222
Cdd:pfam01957   9 LLLLLRPLALKRLRKKSPGSLT-NRDEALIGRTGVVLEDIRPDgGRVKIDGEEWTARSDGDFIPAGTRVRVVAVEGLTLI 87

                  ...
gi 517998445  223 VRE 225
Cdd:pfam01957  88 VEP 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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