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Conserved domains on  [gi|6323229|ref|NP_013301|]
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tubulin-binding prefolding complex subunit YKE2 [Saccharomyces cerevisiae S288C]

Protein Classification

prefoldin subunit 6( domain architecture ID 19227319)

prefoldin subunit 6 (PFDN6) is a beta subunit of prefoldin, a hexameric co-chaperone prefoldin complex that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly

Gene Ontology:  GO:0016272|GO:0061077|GO:0051082|GO:0003714
PubMed:  9630229|11106732|33137104

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
 6-103 9.52e-37

Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


:

Pssm-ID: 467477 [Multi-domain]  Cd Length: 101  Bit Score: 120.28  E-value: 9.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:cd23161   2 KEFQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAKSNVDKRLEFITGEIKRVEKQ 81

                        90
                ....*....|....*...
gi 6323229   86 IRDKQEELEKMRSELIKL 103
Cdd:cd23161  82 IKDLEKKQEKKREKIAKL 99
 
Name Accession Description Interval E-value
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
 6-103 9.52e-37

Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467477 [Multi-domain]  Cd Length: 101  Bit Score: 120.28  E-value: 9.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:cd23161   2 KEFQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAKSNVDKRLEFITGEIKRVEKQ 81

                        90
                ....*....|....*...
gi 6323229   86 IRDKQEELEKMRSELIKL 103
Cdd:cd23161  82 IKDLEKKQEKKREKIAKL 99
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 6-103 4.72e-19

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 75.34  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229      6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:pfam01920   2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEKQ 81

                          90
                  ....*....|....*...
gi 6323229     86 IRDKQEELEKMRSELIKL 103
Cdd:pfam01920  82 LEKLEKELEELKEELYKK 99
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
3-100 5.63e-10

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 52.58  E-value: 5.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    3 ELGAKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRC 82
Cdd:COG1382  11 NQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKETLELRLKTL 90

                        90
                ....*....|....*...
gi 6323229   83 EKNIRDKQEELEKMRSEL 100
Cdd:COG1382  91 EKQEERLQKQLEELQEKL 108
PRK09343 PRK09343
prefoldin subunit beta; Provisional
 6-102 8.98e-09

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 49.30  E-value: 8.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229     6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEIT---RC 82
Cdd:PRK09343  14 AQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPIYKIVGNLLVKVDKTKVEKELKERKELLELRSRtleKQ 93

                         90       100
                 ....*....|....*....|
gi 6323229    83 EKNIRDKQEELEKMRSELIK 102
Cdd:PRK09343  94 EKKLREKLKELQAKINEMLS 113
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
 6-100 1.47e-08

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 48.50  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229      6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:TIGR02338  10 AQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTPVYKSVGNLLVKTDKEEAIQELKEKKETLELRVKTLQRQ 89

                          90
                  ....*....|....*
gi 6323229     86 IRDKQEELEKMRSEL 100
Cdd:TIGR02338  90 EERLREQLKELQEKI 104
 
Name Accession Description Interval E-value
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
 6-103 9.52e-37

Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467477 [Multi-domain]  Cd Length: 101  Bit Score: 120.28  E-value: 9.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:cd23161   2 KEFQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAKSNVDKRLEFITGEIKRVEKQ 81

                        90
                ....*....|....*...
gi 6323229   86 IRDKQEELEKMRSELIKL 103
Cdd:cd23161  82 IKDLEKKQEKKREKIAKL 99
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 6-103 4.72e-19

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 75.34  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229      6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:pfam01920   2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEKQ 81

                          90
                  ....*....|....*...
gi 6323229     86 IRDKQEELEKMRSELIKL 103
Cdd:pfam01920  82 LEKLEKELEELKEELYKK 99
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
3-100 5.63e-10

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 52.58  E-value: 5.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    3 ELGAKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRC 82
Cdd:COG1382  11 NQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTDKEEVIKELEEKKETLELRLKTL 90

                        90
                ....*....|....*...
gi 6323229   83 EKNIRDKQEELEKMRSEL 100
Cdd:COG1382  91 EKQEERLQKQLEELQEKL 108
Prefoldin_beta_GimC cd23162
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric ...
 6-95 5.77e-10

Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467478 [Multi-domain]  Cd Length: 102  Bit Score: 52.10  E-value: 5.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEIT---RC 82
Cdd:cd23162   4 AQLQQLQQQLQAVLLQKQQLEAELREIERALEELEKLPDDAEVYKSVGTILVKVDKEEVIKELKERKETLELRLKtleKQ 83

                        90
                ....*....|...
gi 6323229   83 EKNIRDKQEELEK 95
Cdd:cd23162  84 EERLRKQLEELQK 96
PRK09343 PRK09343
prefoldin subunit beta; Provisional
 6-102 8.98e-09

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 49.30  E-value: 8.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229     6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEIT---RC 82
Cdd:PRK09343  14 AQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPIYKIVGNLLVKVDKTKVEKELKERKELLELRSRtleKQ 93

                         90       100
                 ....*....|....*....|
gi 6323229    83 EKNIRDKQEELEKMRSELIK 102
Cdd:PRK09343  94 EKKLREKLKELQAKINEMLS 113
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
 6-100 1.47e-08

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 48.50  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229      6 AKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:TIGR02338  10 AQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTPVYKSVGNLLVKTDKEEAIQELKEKKETLELRVKTLQRQ 89

                          90
                  ....*....|....*
gi 6323229     86 IRDKQEELEKMRSEL 100
Cdd:TIGR02338  90 EERLREQLKELQEKI 104
Prefoldin_beta cd00632
Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, ...
 22-90 9.13e-05

Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467469  Cd Length: 78  Bit Score: 38.09  E-value: 9.13e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323229   22 RQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKNIRDKQ 90
Cdd:cd00632   9 KEELERKINEQKVVLDELSNLKKNRKVYRQQGNIFILASKEETLSELKKTLDHLQKEIKELEQQLKAKE 77
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
 3-99 8.50e-04

prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467479  Cd Length: 100  Bit Score: 35.95  E-value: 8.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    3 ELGAKYQQLQNELEEFIVARQKLETQLQENKIVNEEFDQLEEDTPVYKLTGNVLlpVEQS--EARTNVDKRLEFIETEIT 80
Cdd:cd23163   1 EVVAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVL--VERTvgEVLPALEENKENLEEVIE 78

                        90
                ....*....|....*....
gi 6323229   81 RCEKNIRDKQEELEKMRSE 99
Cdd:cd23163  79 QLNEQLEEKEKELNEFREK 97
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 6-100 1.63e-03

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 35.21  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323229    6 AKYQQLQNELEEFIVARQKLETQLQEnkiVNEEFDQLEEDTPVYKLTGNVLLPVEQSEARTNVDKRLEFIETEITRCEKN 85
Cdd:cd23165   9 SRLNARLHELKEELKAKKKELENLED---ASDELELADDDEPVPYKIGEVFVHLSLEEAQERLEKAKEELEEEIEKLEEE 85

                        90
                ....*....|....*
gi 6323229   86 IRDKQEELEKMRSEL 100
Cdd:cd23165  86 IDEIEEEMKELKVQL 100
 
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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