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Conserved domains on  [gi|2747583653|ref|WP_350669759|]
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SPFH domain-containing protein, partial [Pseudoalteromonas sp. 43-MNA-CIBAN-0464]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11029 super family cl32628
protease modulator HflC;
1-69 4.07e-23

protease modulator HflC;


The actual alignment was detected with superfamily member PRK11029:

Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 89.03  E-value: 4.07e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583653   1 MKNFSLVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKDSDDQAIVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:PRK11029    1 MRKSVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNKPLVYAPGLHFKIPFIETVKMLDARI 69
 
Name Accession Description Interval E-value
PRK11029 PRK11029
protease modulator HflC;
1-69 4.07e-23

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 89.03  E-value: 4.07e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583653   1 MKNFSLVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKDSDDQAIVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:PRK11029    1 MRKSVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNKPLVYAPGLHFKIPFIETVKMLDARI 69
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 1-69 2.16e-16

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 70.58  E-value: 2.16e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583653   1 MKNFSLVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKDSDDQAIVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:TIGR01932   1 MRKIGIVVIVLLIVVLFQPFFIIKEGERGIITRFGKILKDNNHHVLVYEPGLHFKIPFIEHVKIFDAKI 69
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-69 6.40e-15

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 66.40  E-value: 6.40e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583653   4 FSLVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKdsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:COG0330     5 LLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVR-------TLEPGLHFKIPFIDRVRKVDVRE 63
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 19-69 4.01e-12

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 58.27  E-value: 4.01e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2747583653  19 SVFVVPEGQKAIVMLFSKVQKDsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:cd03405     1 SVFIVDETEQAVVLQFGKPVRV------ITEPGLHFKLPFIQNVRKFDKRI 45
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 21-69 1.92e-05

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 39.61  E-value: 1.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2747583653  21 FVVPEGQKAIVMLFSKVQKdsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSR-------VLEPGLHFIIPFIQRVVTVDVRV 42
PHB smart00244
prohibitin homologues; prohibitin homologues
 18-69 4.07e-05

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 38.80  E-value: 4.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2747583653   18 SSVFVVPEGQKAIVMLFSKVQKdsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-------VLGPGLHFLIPFIDDVKKVDLRA 45
 
Name Accession Description Interval E-value
PRK11029 PRK11029
protease modulator HflC;
1-69 4.07e-23

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 89.03  E-value: 4.07e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583653   1 MKNFSLVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKDSDDQAIVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:PRK11029    1 MRKSVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNKPLVYAPGLHFKIPFIETVKMLDARI 69
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 1-69 2.16e-16

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 70.58  E-value: 2.16e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747583653   1 MKNFSLVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKDSDDQAIVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:TIGR01932   1 MRKIGIVVIVLLIVVLFQPFFIIKEGERGIITRFGKILKDNNHHVLVYEPGLHFKIPFIEHVKIFDAKI 69
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-69 6.40e-15

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 66.40  E-value: 6.40e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747583653   4 FSLVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKdsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:COG0330     5 LLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVR-------TLEPGLHFKIPFIDRVRKVDVRE 63
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 19-69 4.01e-12

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 58.27  E-value: 4.01e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2747583653  19 SVFVVPEGQKAIVMLFSKVQKDsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:cd03405     1 SVFIVDETEQAVVLQFGKPVRV------ITEPGLHFKLPFIQNVRKFDKRI 45
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 6-67 5.94e-08

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 47.12  E-value: 5.94e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2747583653   6 LVILLAAIVMSFSSVFVVPEGQKAIVMLFSKVQKdsddqaiVYGPGLQFKVPF---------FSQVRRIDA 67
Cdd:cd03404     1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVR-------TVGPGLHWKLPFpievvekvnVTQVRSVEI 64
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 20-69 2.51e-07

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: 44.81  E-value: 2.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2747583653  20 VFVVPEGQKAIVMLFSKVQKDSddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDE-----VLGEGLHFKIPWIQVVIIYDVRT 45
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 21-69 1.92e-05

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 39.61  E-value: 1.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2747583653  21 FVVPEGQKAIVMLFSKVQKdsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSR-------VLEPGLHFIIPFIQRVVTVDVRV 42
PHB smart00244
prohibitin homologues; prohibitin homologues
 18-69 4.07e-05

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 38.80  E-value: 4.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2747583653   18 SSVFVVPEGQKAIVMLFSKVQKdsddqaiVYGPGLQFKVPFFSQVRRIDARI 69
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-------VLGPGLHFLIPFIDDVKKVDLRA 45
 
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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