NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|552848658|ref|XP_005852152|]
View 

hypothetical protein CHLNCDRAFT_15257, partial [Chlorella variabilis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
clpX super family cl35307
ATP-dependent Clp protease ATP-binding subunit ClpX;
1-74 4.69e-24

ATP-dependent Clp protease ATP-binding subunit ClpX;


The actual alignment was detected with superfamily member PRK05342:

Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 92.53  E-value: 4.69e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552848658   1 LQALDEQELAHVLCRPRNALSKQYSGIFGKNGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMFHV 74
Cdd:PRK05342 309 LEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFEL 382
 
Name Accession Description Interval E-value
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
1-74 4.69e-24

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 92.53  E-value: 4.69e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552848658   1 LQALDEQELAHVLCRPRNALSKQYSGIFGKNGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMFHV 74
Cdd:PRK05342 309 LEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFEL 382
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 1-74 4.66e-23

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 89.72  E-value: 4.66e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552848658   1 LQALDEQELAHVLCRPRNALSKQYSGIFGKNGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMFHV 74
Cdd:COG1219  309 LEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYEL 382
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 4-72 1.69e-11

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 53.99  E-value: 1.69e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552848658    4 LDEQELAHVLCRPRNALSKQYSgifgKNGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMF 72
Cdd:smart01086  1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLA 65
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 4-72 4.01e-03

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.


Pssm-ID: 463090 [Multi-domain]  Cd Length: 81  Bit Score: 32.38  E-value: 4.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552848658   4 LDEQELAHVLcrpRNALSKQYSGIFGKnGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMF 72
Cdd:pfam10431  1 LSKEELRKIV---DLQLKELQKRLAER-GITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLA 65
 
Name Accession Description Interval E-value
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
1-74 4.69e-24

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 92.53  E-value: 4.69e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552848658   1 LQALDEQELAHVLCRPRNALSKQYSGIFGKNGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMFHV 74
Cdd:PRK05342 309 LEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFEL 382
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 1-74 4.66e-23

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 89.72  E-value: 4.66e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552848658   1 LQALDEQELAHVLCRPRNALSKQYSGIFGKNGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMFHV 74
Cdd:COG1219  309 LEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYEL 382
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 4-72 1.69e-11

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 53.99  E-value: 1.69e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552848658    4 LDEQELAHVLCRPRNALSKQYSgifgKNGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMF 72
Cdd:smart01086  1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLA 65
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 4-72 4.01e-03

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.


Pssm-ID: 463090 [Multi-domain]  Cd Length: 81  Bit Score: 32.38  E-value: 4.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552848658   4 LDEQELAHVLcrpRNALSKQYSGIFGKnGCRFHATPAGVAAIAREARTKGVGARGLRSILERALLEAMF 72
Cdd:pfam10431  1 LSKEELRKIV---DLQLKELQKRLAER-GITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLA 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH