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Conserved domains on  [gi|1277893505|gb|PIU98994.1|]
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hypothetical protein COS60_00095 [Candidatus Wolfebacteria bacterium CG03_land_8_20_14_0_80_39_317]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HflC super family cl33838
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 37-180 6.56e-08

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0330:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 53.30  E-value: 6.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893505  37 AFTLLGLGTIAAILIFNAVVIVPVVHFGIPTRVGKRIKkadgkvvILHEGFDFVLPLIDDLEeknIISKKLTTKEIKT-K 115
Cdd:COG0330     3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVR-------TLEPGLHFKIPFIDRVR---KVDVREQVLDVPPqE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277893505 116 AISRDRLEVFLVGSLQYSPFDPNTYIE--REPETIskgLVDAIESEFGKVCGTKDAD-AFVKSRTEIE 180
Cdd:COG0330    73 VLTKDNNIVDVDAVVQYRITDPAKFLYnvENAEEA---LRQLAESALREVIGKMTLDeVLSTGRDEIN 137
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 37-180 6.56e-08

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 53.30  E-value: 6.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893505  37 AFTLLGLGTIAAILIFNAVVIVPVVHFGIPTRVGKRIKkadgkvvILHEGFDFVLPLIDDLEeknIISKKLTTKEIKT-K 115
Cdd:COG0330     3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVR-------TLEPGLHFKIPFIDRVR---KVDVREQVLDVPPqE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277893505 116 AISRDRLEVFLVGSLQYSPFDPNTYIE--REPETIskgLVDAIESEFGKVCGTKDAD-AFVKSRTEIE 180
Cdd:COG0330    73 VLTKDNNIVDVDAVVQYRITDPAKFLYnvENAEEA---LRQLAESALREVIGKMTLDeVLSTGRDEIN 137
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 55-183 8.51e-03

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 37.11  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893505  55 VVIVPVVHFGIPTRVGKrikkaDGKVVILHEGFDFVLPLIDDLEeknIISKKLTTKEIKTKAISRDRLEVFLVGSLQYSP 134
Cdd:cd03401     1 FYTVDAGEVGVVFRRGK-----GVKDEVLGEGLHFKIPWIQVVI---IYDVRTQPREITLTVLSKDGQTVNIDLSVLYRP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277893505 135 fDPNT--YIERE--PETISKGLVDAIESEFGKVCGTKDADAFVKSRTEIEVLI 183
Cdd:cd03401    73 -DPEKlpELYQNlgPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEI 124
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 37-180 6.56e-08

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 53.30  E-value: 6.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893505  37 AFTLLGLGTIAAILIFNAVVIVPVVHFGIPTRVGKRIKkadgkvvILHEGFDFVLPLIDDLEeknIISKKLTTKEIKT-K 115
Cdd:COG0330     3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVR-------TLEPGLHFKIPFIDRVR---KVDVREQVLDVPPqE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277893505 116 AISRDRLEVFLVGSLQYSPFDPNTYIE--REPETIskgLVDAIESEFGKVCGTKDAD-AFVKSRTEIE 180
Cdd:COG0330    73 VLTKDNNIVDVDAVVQYRITDPAKFLYnvENAEEA---LRQLAESALREVIGKMTLDeVLSTGRDEIN 137
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 55-183 8.51e-03

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 37.11  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277893505  55 VVIVPVVHFGIPTRVGKrikkaDGKVVILHEGFDFVLPLIDDLEeknIISKKLTTKEIKTKAISRDRLEVFLVGSLQYSP 134
Cdd:cd03401     1 FYTVDAGEVGVVFRRGK-----GVKDEVLGEGLHFKIPWIQVVI---IYDVRTQPREITLTVLSKDGQTVNIDLSVLYRP 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277893505 135 fDPNT--YIERE--PETISKGLVDAIESEFGKVCGTKDADAFVKSRTEIEVLI 183
Cdd:cd03401    73 -DPEKlpELYQNlgPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEI 124
 
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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